U.S. patent application number 11/838489 was filed with the patent office on 2007-12-06 for processed cheese with improved firmness using cross-linking enzymes.
This patent application is currently assigned to Schreiber Foods, Inc.. Invention is credited to Charles C. Hunt, Jeng-Jung Yee.
Application Number | 20070281053 11/838489 |
Document ID | / |
Family ID | 27805083 |
Filed Date | 2007-12-06 |
United States Patent
Application |
20070281053 |
Kind Code |
A1 |
Yee; Jeng-Jung ; et
al. |
December 6, 2007 |
PROCESSED CHEESE WITH IMPROVED FIRMNESS USING CROSS-LINKING
ENZYMES
Abstract
A method of making a processed cheese with improved firmness
comprises mixing a protein cross-linking enzyme and optionally
first other ingredients with a cheese material having a pH of less
than 5.6, a moisture content of less than 60% and preferably
containing one or more coagulating agents, to form a mixture;
providing temperature and pH conditions and allowing time for the
enzyme to react with protein in the mixture to cross link at least
a portion of the protein; and combining one or more emulsifying
agents and optionally second other ingredients with the mixture and
heating the combination to thereby produce processed cheese from
the combined cheese material contain cross-linked proteins,
emulsifying agents and optional first and second other
ingredients.
Inventors: |
Yee; Jeng-Jung; (Green Bay,
WI) ; Hunt; Charles C.; (DePere, WI) |
Correspondence
Address: |
BRINKS HOFER GILSON & LIONE;UTAH OFFICE
405 South Main Street
Suite 800
SALT LAKE CITY
UT
84111-3400
US
|
Assignee: |
Schreiber Foods, Inc.
|
Family ID: |
27805083 |
Appl. No.: |
11/838489 |
Filed: |
August 14, 2007 |
Related U.S. Patent Documents
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Application
Number |
Filing Date |
Patent Number |
|
|
10382227 |
Mar 4, 2003 |
7267831 |
|
|
11838489 |
Aug 14, 2007 |
|
|
|
60361828 |
Mar 4, 2002 |
|
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Current U.S.
Class: |
426/38 ; 426/36;
426/40; 426/582 |
Current CPC
Class: |
A23C 19/082 20130101;
A23C 19/063 20130101; C12Y 203/02013 20130101; A23C 19/0285
20130101 |
Class at
Publication: |
426/038 ;
426/036; 426/040; 426/582 |
International
Class: |
A23C 19/06 20060101
A23C019/06; A23C 19/02 20060101 A23C019/02 |
Claims
1-31. (canceled)
32. A method of making a processed cheese comprising: a) producing
cheese curds; b) mixing transglutaminase with the cheese curds; c)
packing the mixture of cheese curds and transglutaminase to form
cheese; d) allowing the cheese to age for a period of at least 24
hours, the transglutaminase reacting with protein in the curds to
cross link the protein while the cheese is aging, and e) mixing the
transglutaminase-treated cheese with other processed cheese
ingredients and heating and mixing the combination to produce the
processed cheese.
33. The method of claim 32 wherein the other processed cheese
ingredients comprise one or more emulsifying agents.
34. The method of claim 33 wherein the other processed cheese
ingredients also include cheese made by ultrafiltration and
diafiltration of milk.
35. The method of claim 32 wherein the transglutaminase is mixed
with the curds, at a level of between about 0.2 units per gram of
protein in the curds and about 5 units per gram of protein in the
curds.
36. A method of making processed cheese comprising: a)
ultrafiltering and diafiltering milk to produce a retentate; b)
fermenting the retentate; c) adding transglutaminase to the
retentate; d) removing water from the fermented retentate; e)
providing temperature and pH conditions and allowing a period of
time for the transglutaminase to cross link at least a portion of
proteins in the retentate; and f) combining the fermented dewatered
retentate with cross-linked proteins therein with other processed
cheese ingredients, and heating and mixing the combination to
produce the processed cheese.
37. The method of claim 36 wherein the transglutaminase is added to
the retentate after fermentation and before removal of water.
38. The method of claim 36 wherein the period of time for cross
linking comprises at least 24 hours and is between when water is
removed and when the fermented, dewatered retentate is combined
with other processed cheese making ingredients.
39. The method of claim 36 wherein a starter culture is added to
the retentate to start fermentation and the transglutaminase is
mixed with the retentate prior to or when the starter culture is
added.
40. A method of making processed cheese comprising: a) providing
cheese material and other ingredients used to make the processed
cheese; b) mixing transglutaminase with the cheese material and
providing temperature and pH conditions and allowing time for the
transglutaminase to cross link at least a portion of proteins in
the cheese material; and c) heating and mixing the cheese material,
transglutaminase and other processed cheese ingredients to form the
processed cheese.
41. The method of claim 40 wherein the cheese material and
transglutaminase are mixed in a blender and later placed in a
cooker.
42. The method of claim 41 wherein water is added with the cheese
material and transglutaminase in the blender.
43. The method of claim 42 wherein water is also added in the
cooker in the form of steam.
44. The method of claim 41 wherein the cheese material and
transglutaminase are heated to a temperature of between about
50.degree. F. and about 120.degree. F. in the cooker.
45. The method of claim 44 wherein the cheese material and
transglutaminase are mixed in the cooker for a period of between
about 1 hour and about 3 hours while being heated, thus providing
said time for cross linking.
46. The method of claim 45 wherein the other processed cheese
ingredients comprise one or more emulsifying agents and the one or
more emulsifying agents are added to the cooker after said period
of between about 1 hour and about 3 hours.
47. The method of claim 46 wherein the cheese material,
transglutaminase and one or more emulsifying agents are heated to a
temperature of between about 170.degree. F. and about 210.degree.
F. in the cooker.
48. The method of claim 40 wherein the other processed cheese
ingredients comprise one or more emulsifying agents and the one or
more emulsifying agents are mixed with the cheese material and
transglutaminase prior to allowing said time for cross-linking.
49-56. (canceled)
57. A processed cheese made by the method of claim 1.
58. The processed cheese of claim 57 having an Instron firmness,
corrected to 40% moisture, of at least 1 kgf.
59. The processed cheese of claim 57 having a Mettler melt
temperature of between about 120.degree. F. and about 200.degree.
F.
60. The processed cheese of claim 57 having a Schreiber melt score
of at least 3.
61. The processed cheese of claim 60 also having an Instron
firmness, corrected to 40% moisture, of at least 1.5 kgf.
62. A mixture of a cheese material and a protein cross-linking
enzyme comprising: a) a cheese material selected from the group
consisting of comminuted natural cheese, conventional cheese curds
and fermented UF retentate, and b) transglutaminase, wherein the
transglutaminase is present at a level of between about 0.2 units
and about 10 units of transglutaminase per gram of protein in the
mixture.
63. The mixture of claim 62 wherein the mixture is essentially free
of emulsifying agents.
64. The mixture of claim 62 wherein the cheese material has not
been melted.
65. A process of adding a protein cross-linking enzyme to a cheese
material so as to allow the enzyme to cross link protein in the
cheese material comprising the steps of: a) ultrafiltering and
diafiltering milk to produce a UF retentate; b) adding
transglutaminase to the retentate at a level of between about 0.2
units and about 10 units of transglutaminase per gram of protein in
the UF retentate; and c) evaporating water from the retentate to
produce a UF cheese containing active transglutaminase.
66. The process of claim 65 wherein the transglutaminase is allowed
to cross link protein in the UF cheese for at least 24 hours before
the transglutaminase is deactivated.
67. A process of adding a protein cross-linking enzyme to a cheese
material so as to allow the enzyme to cross link protein in the
cheese material comprising the steps of: a) producing conventional
cheese curds; b) mixing transglutaminase with the cheese curds at a
level of between about 0.2 units and about 10 units of
transglutaminase per gram of protein in the curds; and c) packing
the mixed curds and transglutaminase into a container.
68. The process of claim 67 wherein the transglutaminase is allowed
to cross link protein in the curds for at least 24 hours before the
transglutaminase is deactivated.
Description
REFERENCE TO EARLIER FILED APPLICATION
[0001] The present application claims the benefit of the filing
date under 35 U.S.C. .sctn. 119(e) of Provisional U.S. Patent
Application Ser. No. 60/361,828, filed Mar. 4, 2002, which is
hereby incorporated by reference in its entirety.
BACKGROUND OF THE INVENTION
[0002] The present invention relates to processed cheese and
methods of making processed cheese. In particular, the invention
relates to the use of a protein cross-linking enzyme during the
manufacturing process to produce a processed cheese having an
improved firmness.
[0003] Processed cheese has become a staple of the food industry.
It is also a commodity, meaning that there are many suppliers of
processed cheese. As a result, the price charged for processed
cheese has a great impact on a supplier's share of the market. Thus
processed cheese manufacturers are under constant pressure to
reduce their costs. On the other hand, government regulations
regarding the ingredients that can be used, and the desire for
functional qualities such as taste, firmness, mouth feel and
meltability, constrain efforts to reduce costs. In addition to the
quality perceived by the consumer, functional qualities are also
important in the manufacturing process.
[0004] One of the efforts to reduce cost for cheese has been to
keep the whey proteins from being lost in the cheese making
process. For example, U.S. Pat. No. 5,356,639 discloses a process
for making cheese by using ultrafiltration and diafiltration to
keep all of the whey proteins in the final cheese. Also, U.S. Pat.
No. 5,681,598 discloses the use of transglutaminase to cross-link
proteins in milk to increase the yield of the curds from the milk.
In addition, whey solids are a common ingredient mixed with cheese
to make processed cheese. However, the presence of whey solids in
processed cheese has a negative impact on the firmness of the
processed cheese. Other ingredients that may be added to processed
cheese may also have a negative impact on the firmness or
meltability of the processed cheese. Also, many other measures
taken to reduce cost often have a negative impact on the firmness
of processed cheese.
[0005] Transglutaminase has been suggested for use in various food
products. Transglutaminase cross-links proteins in meat products to
improve the hardness and elasticity of the products, as well as to
improve the texture of products containing low meat content.
Transglutaminase has also been disclosed for use in dairy products.
For example, U.S. Pat. No. 6,224,914 discloses a process for
incorporating whey proteins into cheese using transglutaminase, and
U.S. Pat. No. 6,242,036 discloses cheese curd made using
transglutaminase and a non-rennet protease. U.S. Pat. No. 6,270,814
discloses incorporation of whey into process cheese. However, the
common problem with many of these processes is that
transglutaminase is currently fairly expensive. Thus, the benefit
it provides is not worth its cost. None of the foregoing processes
using transgutaminase are believed to be currently used on a
commercial basis in the United States.
[0006] Another approach for utilizing transglutaminase in processed
cheese is disclosed in Japanese Patent Publication No. 2594340. In
the disclosed process, cheese and other ingredients are melted,
mixed together and cooked to make a processed cheese. The
temperature is then reduced and transglutaminase is added and
allowed to act on the melted cheese mixture to produce a product
with optimal stringiness and high temperature shape retention. One
problem with this process is that the processed cheese is stirred
at a medium temperature, such as 50.degree. C. (122.degree. F.),
for 30 minutes while the transglutaminase reacts. This material
then has to be reheated to 85.degree. C. (185.degree. F.) to
deactivate the transgutaminase. All of this post-manufacture
processing of the processed cheese is impractical in making a
commodity processed cheese, which otherwise requires only a very
short residence time in the mixing and cooking equipment.
[0007] Hence, there is still a need for a process for making
processed cheese that has good firmness, but which is commercially
practical. Also, a processed cheese that is inexpensive, but still
has good firmness and melt properties would be highly
desirable.
BRIEF SUMMARY OF THE INVENTION
[0008] A process has been invented that allows an efficient use of
a protein cross-linking enzyme, such as transglutaminase, in making
a processed cheese with improved firmness.
[0009] In a first aspect the invention is a method of making a
processed cheese with improved firmness comprising: mixing a
protein cross-linking enzyme and optionally first other ingredients
with a cheese material having a pH of less than 5.6, a moisture
content of less than 60% and preferably containing one or more
coagulating agents to form a mixture; providing temperature and pH
conditions and allowing time for the enzyme to react with protein
in the mixture to cross link at least a portion of the protein; and
thereafter combining one or more emulsifying agents and optionally
second other ingredients with the mixture and heating the
combination to thereby produce processed cheese from the combined
cheese material containing cross-linked proteins, emulsifying
agents and optional first and second other ingredients.
[0010] In a second aspect, the invention is a method of making a
processed cheese comprising: producing cheese curds; mixing
transglutaminase with the cheese curds; packing the mixture of
cheese curds and transglutaminase to form cheese; allowing the
cheese to age for a period of at least 24 hours, the
transglutaminase reacting with protein in the curds to cross-link
the protein while the cheese is aging, and combining the
transglutaminase-treated cheese with other processed cheese
ingredients and heating and mixing the combination to produce the
processed cheese.
[0011] In a third aspect, the invention is a method of making
processed cheese comprising: ultrafiltering and diafiltering milk
to produce a retentate; fermenting the retentate; adding
transglutaminase to the retentate; removing water from the
fermented retentate; providing temperature and pH conditions and
allowing a period of time for the transglutaminase to cross link at
least a portion of proteins in the retentate; and combining the
fermented dewatered retentate with cross-linked proteins therein
with other processed cheese ingredients, and heating and mixing the
combination to produce the processed cheese.
[0012] In a fourth aspect, the invention is a method of making
processed cheese comprising: providing cheese material and other
ingredients used to make the processed cheese; mixing
transglutaminase with the cheese material and providing temperature
and pH conditions and allowing time for the transglutaminase to
cross link at least a portion of proteins in the cheese material;
and heating and mixing the cheese material, transglutaminase and
other processed cheese ingredients to form the processed
cheese.
[0013] The present invention also encompasses a processed cheese
made by any of the foregoing methods, as well as novel intermediate
compositions and methods of adding a protein cross-linking enzyme
to a cheese material. In this regard, in another aspect the
invention is a mixture of a cheese material and a protein
cross-linking enzyme comprising: a cheese material selected from
the group consisting of comminuted natural cheese, conventional
cheese curds and fermented of retentate, and transglutaminase,
wherein the transglutaminase is present at a level of between about
0.2 units and about 10 units of transglutaminase per gram of
protein in the mixture.
[0014] In yet another aspect, the invention is a process of adding
a protein cross-linking enzyme to a cheese material so as to allow
the enzyme to cross link protein in the cheese material comprising
the steps of: ultrafiltering and diafiltering milk to produce a UF
retentate; adding transglutaminase to the retentate at a level of
between about 0.2 units and about 10 units of transglutaminase per
gram of protein in the UF retentate; and evaporating water from the
retentate to produce a UF cheese containing active
transglutaminase.
[0015] In still yet a further aspect, the invention is a process of
adding a protein cross-linking enzyme to a cheese material so as to
allow the enzyme to cross link protein in the cheese material
comprising the steps of: producing conventional cheese curds;
mixing transglutaminase with the cheese curds at a level of between
about 0.2 units and about 10 units of transglutaminase per gram of
protein in the curds; and packing the mixed curds and
transglutaminase into a container.
[0016] In addition to increased firmness, there are other
advantages of the present invention. Primarily, the cross-linking
enzyme is utilized in a composition that has a fairly high solids
level. In many of the prior art processes, transglutaminase is used
in milk, or other dilute casein sources, or compositions where
casein only makes up a small percentage of the composition. As a
result, either large quantities of transglutaminase must be used,
or long reaction times must be allowed, both of which are not very
cost efficient. Further, in the present invention, the
cross-linking enzyme is preferably mixed with a cheese material at
a stage in the overall processed cheese manufacturing process when
the cheese material (such as cheese curds or UF cheese) is normally
given time to age. As a result, in preferred embodiments of the
invention, the cross-linking reaction can occur over a fairly long
period of time without adding to the time required to actually make
the processed cheese.
[0017] Finally, the preferred embodiments of the invention utilize
temperatures normally encountered in processed cheese manufacturing
processes to deactivate the cross-linking enzyme, as opposed to
additional mixing, holding and deactivation steps after processed
cheese is made.
[0018] These and other advantages of the invention, as well as the
invention itself, will be best understood in light of the following
detailed description and examples, which are given by way of
explanation and are not to be considered as limiting the
invention.
DETAILED DESCRIPTION OF THE INVENTION AND PREFERRED EMBODIMENTS
Definitions
[0019] Unless indicated otherwise, percentages given for components
in a composition are percentages by weight of the composition.
[0020] "Conventional cheese" as used herein means a cheese made by
the traditional method of coagulating milk, cutting the coagulated
milk to form discrete curds, stirring and heating the curd,
draining off the whey, and collecting or pressing the curd. Milk
from many different mammals is used to make cheese, though cow's
milk is the most common milk for cheese used to make processed
cheese. Cow's milk contains whey proteins and casein at a weight
ratio of about 1:4 whey proteins to casein. The conventional
process for making natural cheese recovers the casein from the
milk. Whey proteins dissolved in the whey are mostly discharged
during the whey drainage step. The ratio of whey proteins to casein
is between about 1:150 and about 1:40 for conventional cheese. For
example, Cheddar cheese contains about 0.3% whey proteins. The
ratio of whey proteins to casein is about 1.100 in typical Cheddar
cheese, the most common conventional cheese. Cheddar cheese
contains about 23% to about 26% protein by weight. Conventional
cheese is often categorized by its age. Within 0 to 24 hours after
the whey is drained, the material is often referred to as fresh
curd. The curds are pressed and fused together to become cheese.
Young cheese is often categorized as cheese that has been aged
either 1-7 days, 1-2 weeks or 2 weeks to 1 month. Medium cheese is
often categorized as aged 1-3 months or 3-6 months Aged cheese is
usually older than 6 months.
[0021] "American-type cheeses" as used herein means the group of
conventional cheeses including Cheddar, washed curd, Colby, stirred
curd cheese and Monterey Jack. All must contain at least 50% fat in
dry matter (FDM). Modifications in the process for making Cheddar
led to the development of the other three varieties. Washed curd
cheese is prepared as Cheddar through the milling stage, when the
curd is covered with cold water for 5 to 30 minutes. Washing
increases moisture to a maximum of 42%. Stirred curd cheese has
practically the same composition as Cheddar but has a more open
texture and shorter (Less elastic) body. It is manufactured as
Cheddar except that agitation of cooked curd particles is used to
promote whey drainage, and the Cheddaring and milling steps are
eliminated. Colby cheese and Monterey Jack cheese are manufactured
the same way as stirred curd except that water is added to wash and
cool the curd when most of the whey has been drained away, thus
increasing the moisture content to a maximum of 40% for Colby
cheese and 44% for Monterey Jack cheese.
[0022] "Pasta filata-type cheese" as used herein means a type of
cheese having a plastic, pliable, homogeneous, stringy structure.
The pasta filata cheeses are traditionally made by producing curds
and whey, draining the whey and immersing the curd in hot water or
hot whey and working, stretching, and molding the curd while it is
in a plastic condition. The principal varieties of pasta filata
cheeses are: cociocavallo, provolone, provolette, pizza cheese,
mozzarella, provole, scamorze, and provatura. The most well known
example of pasta filata-type cheese is mozzarella. In the U.S., the
standards of identity of the code of federal regulations subdivide
mozzarella cheeses into: "mozzarella", "low moisture mozzarella,"
"part skim mozzarella", and "low moisture part skim mozzarella." As
defined by food and drug administration (FDA) regulations,
mozzarella has a moisture content of more than 52 but not more than
60 weight percent and fat in dry matter (FDM) of not less than 45
percent by weight. The low moisture mozzarella has moisture content
of more than 45 but not more than 52 weight percent and FDM of not
less than 45 weight percent. The part skim mozzarella contains more
than 52 but not more than 60 percent of moisture by weight and has
FDM of less than 45 but not less than 30 percent. The low moisture
part skim mozzarella contains more than 45 but not more than 52
percent of moisture by weight and has FDM of less than 45 but not
less than 30 percent.
[0023] "UF cheese" means a cheese produced by a process in which
milk is processed by ultrafiltration and usually diafiltration to
remove water and lactose, but leave the whey proteins in the UF
retentate. Fermentation or direct acidification, followed by
further water removal, results in UF cheese. If fermentation is
used, a starter culture is added to the UF retentate. Fermented UF
retentates often contain about 55-60% moisture, and are evaporated
to less than 40% moisture, and most preferably to about 30-35%
moisture in the final UF cheese. The final evaporation step may be
made easier if the retentate is preheated to a temperature of
between about 140.degree. F. and about 212.degree. F. before being
evaporated, as disclosed in U.S. Pat. No. 5,356,639, which is
incorporated herein by reference. As also disclosed in the '639
patent, rennet may be added to the retentate prior to evaporation,
and possibly at the same time as the starter culture, to make a
product more suitable for conversion to processed cheese. However,
the amount of rennet may be sufficient to coagulate the retentate,
contrary to the statement on col. 15 lines 58-59 of the '639
patent.
[0024] "Processed cheese" as used herein generally refers to a
class of cheese products that are produced by comminuting, mixing
and heating natural cheese into a homogeneous, plastic mass, with
emulsifying agents and optional ingredients, depending on the class
of processed cheese produced. The comminuted cheese is blended and
sent to cookers or the like, which commonly heat the mass to a
temperature of 150.degree.-210.degree. F., preferably
165.degree.-190.degree. F. During cooking, fat is stabilized with
the protein and water by the emulsifying agents, which are
typically citrate or phosphate salts, usually at a level of about
3%. The emulsifying agent causes the protein to become more
soluble. Under these circumstances a stable emulsion of protein,
fat and water occurs to provide a smooth, homogeneous mass. The hot
mass is packaged directly, or formed into slices and packaged.
There are four main classes of processed cheese in the U.S.:
pasteurized process cheese, pasteurized process cheese food,
pasteurized process cheese spread and pasteurized process cheese
product. All four classes of processed cheese are made with
emulsifying agents. Standards of identity apply to pasteurized
processed cheese and are established by the FDA. By those
standards, whey solids, including whey proteins, may not be added
to the pasteurized process cheese.
[0025] "Emulsifying agents" as used herein means emulsifying agents
used in the making of processed cheese. These include one or any
mixture of two or more of the following inorganic salts: monosodium
phosphate, disodium phosphate, dipotassium phosphate, trisodium
phosphate, sodium metaphosphate, sodium acid pyrophosphate,
tetrasodium pyrophosphate, sodium aluminum phosphate, sodium
citrate, potassium citrate, calcium citrate, sodium tartrate, and
sodium potassium tartrate. In processed cheese, these emulsifying
agents act as calcium sequestering (or chelating) agents.
[0026] "Natural cheese" as used herein means a cheese that does not
contain emulsifying agents. Conventional cheeses (containing very
small amounts of whey proteins) and cheeses made using an UF
process (containing high levels of whey proteins) are the usual
varieties of natural cheeses.
[0027] "Cheese material" as used herein includes conventional
cheese, UF cheese and intermediate materials in the conventional or
UF cheese making process. The most common cheese materials used in
the present invention are cheese curds, comminuted natural cheese
and UF cheese. Cheese materials also include cheese made from other
than fresh milk. For example, cheese material may be made from
dairy liquids such as reconstituted dry milk powder. The fat
content of the milk or other dairy liquid may be adjusted before
making the cheese material. Preferably the cheese material will
have a pH of less than 5.6, a moisture content of less than 60% and
contain one or more coagulating agents, such as a protease, and
most commonly rennet. Preferably, the cheese material will contain
at least 15% protein by weight, more preferably at least 20%
protein by weight and preferably at least 10% casein by weight.
Test Procedures
[0028] The present invention and the benefits thereof are most
easily understood when described in terms of several standards for
evaluating the firmness and melt properties of processed
cheese.
Schreiber Melt Test
[0029] The L. D. Schreiber melt test is a well-known and accepted
standardized test for determining the melt properties of cheese.
The test uses a kitchen oven and a standardized piece of cheese,
and measures the size of the cheese piece after it is melted. The
instructions for the procedure, as used in tests with results
reported below, are as follows:
[0030] 1. Preheat oven to 450.degree. F. (232.2.degree. C.).
[0031] 2. Slice cheese 3/16 thick (5 mm). If cheese is already
sliced, use 2-3 slices to get closest to the 3/16 thickness.
[0032] 3. Cut a circle out of the cheese slice using a copper
sampler with a diameter of 39.5 mm.
[0033] 4. Center the cheese circle in a thin wall 15.times.100 mm
petri dish, cover and place on the center rack of the oven. Do this
quickly so the oven temperature does not drop below 400.degree. F.
(204.4.degree. C.).
[0034] 5. Bake for 5 minutes and remove. Up to 4 dishes may be done
at the same time.
[0035] 6. Once cooled, the melt is measured on the score sheet.
[0036] The score sheet comprises a series of concentric circles
with increasing diameters. The first circle has a diameter of 40.0
mm. Each succeeding circle is 6.5 mm larger is diameter. The melted
cheese receives a score of 1 if it fills the first circle, a score
of 2 if it fills the second circle, etc. As used herein, the scores
include a "+" (or "-") indicating that the cheese was slightly
larger (or smaller) than the indicated score ring. A cheese with an
acceptable Schreiber melt test will score 3 or above.
Mettler Melt Test
[0037] The meltabilities of cheeses can also be compared using an
apparatus for determination of dropping point or softening point,
such as the Mettler FP 800 thermosystem. In such an apparatus, the
temperature at which a plug of cheese falls through an orifice is
measured. In general, cheeses with acceptable melt characteristics
have a Mettler melt temperature below 200.degree. F. Cheeses
exhibiting non-melt characteristics will not melt at 230.degree.
F., which is the shut-off temperature of the Mettler FP 800
instrument as set up for this test, which prevented the temperature
from rising too high and burning non-melting samples inside the
instrument. The Mettler FP 800 instrument was set up with the start
temperature at 100.0.degree. F. and the heating temperature rate at
5.0.degree. F./minute.
[0038] The instructions for sample preparation are as follows:
[0039] 1. The sample cup (middle piece) is pushed through the
cheese sample until the sample extruded from the small top hole of
the cup.
[0040] 2. A knife is used to carefully trim around the cup and
square off cheese at the top and bottom.
[0041] 3. Samples of cheese to be prepared are kept in airtight
bags to prevent drying out. Samples of cheese that are prepared for
analysis in their cups are kept in a petri dish to prevent drying
out if they are not to be analyzed immediately.
[0042] 4. The bottom holder and top holder of the sample cup are
assembled with the center section.
[0043] 5. The entire assembly, using the top holder stem, is placed
in the oven and gently turned until it is seated on the bottom of
the oven.
[0044] 6. After the sample is placed in the instrument, the
run/stop button is pushed. At this point there is a 30 second
countdown while the oven temperature equilibrates at 100.degree. F.
The oven temperature will begin to rise and will shut off at the
softening point of the cheese or at 230.degree. F., in case the
cheese does not soften and flow. The softening point reading will
be printed on paper, or the end temperature (230.degree. F.) will
be printed if the cheese does not soften.
[0045] 7. A fan inside the oven will turn on to bring the
temperature back to 100.degree. F. or below. When the fan has
turned off, the entire assembly is removed from the oven and
disassembled. The sections are cleaned using the scraper provided
for the cup and tweezers to remove cheese from the bottom
holder.
Instron Firmness Measurement
[0046] The firmness of the cheese is measured by an Instron Tester
(Model 5542-Canton, Mass.). The cheese is cut into chunk size
(2''.times.3''.times.4'') and tempered at 40.degree. F. overnight.
A compressive loading force is applied to the cheese sample with a
McCormic Fruit Tester plunger (8 mm diameter) attached to a load
cell (500 Newton). The maximum force (kg) recorded for the plunger
as it travels downward (at a speed of 330 mm/min.) with a
penetration depth of 11 mm into cheese is defined as the firmness
of the cheese.
[0047] Because the moisture content of processed cheese has a
significant impact on the Instron firmness measurement, it is
useful to compare firmness data of different processed cheeses on a
comparable moisture content basis. To do this, a correction factor
of 0.2 kgf for each 1% moisture decrease has been found to be
fairly accurate. Therefore, this correction factor is used herein
to determine firmness at a corrected moisture content of 40%. For
example, a processed cheese with actual moisture at 39.8% and a
measured Instron firmness of 1.0 kgf would have an Instron firmness
value corrected to 40% moisture of 0.96 kgf.
[0048] Transglutaminases are enzymes that catalyze the transfer of
the .gamma.-carboxamide group of a glutaminyl residue in a protein
or peptide to the .epsilon.-amino of a lysyl residue of the same or
a different protein or peptide, thereby forming a .gamma.-carboxyl
.epsilon.-amino cross-link. Transglutaminases have a broad
occurrence in living systems, and may be obtained, for example,
from microorganisms such as those belonging to the genus
Streptoverticillium, Bacillus subtilis, various Actinomycetes and
Myxomycetes, or from plants, fish species, and mammalian sources
including pig liver and the blood clotting protein activated Factor
XIII. In general, transglutaminases from animal sources require
calcium ions for activity. Recombinant forms of transglutaminase
enzymes may be obtained by genetic engineering methods as
heterologous proteins produced in bacterial, yeast, and insect or
mammalian cell culture systems. The principal requirement of any
transglutaminase employed in the instant invention is that it have
the cross-linking activity discussed above. Any enzyme having
transglutaminase activity may be employed in the methods of the
present invention. In a preferred embodiment, the transglutaminase
is obtained from the genus Streptoverticillium.
[0049] Transglutaminase activity may be determined using known
procedures. One such colorimetric procedure uses
benzyloxycarbonyl-L-glutaminyl-glycine and hydroxylamine to form a
.gamma.-carboxyl-hydroxamic acid if transglutaminase is present. An
iron complex of the hydroxamic acid can be formed in the presence
of ferric chloride and trichloroacetic acid. Using the absorbance
at 525 nm with appropriate standards, the activity of enzyme
present may be determined. Activity in the present invention is
determined and defined as follows. A reaction system containing
benzyloxycarbonyl-L-glutamylglycine and hydroxylamine as substrates
is reacted with transglutaminase in a tris buffer (pH 6.0) at a
temperature of 37.degree. C., and the hydroxamic acid formed is
transformed into an iron complex in the presence of trichloroacetic
acid. Then, the absorbance at 525 nm is measured, and the amount of
hydroxamic acid is calculated using a calibration curve. Thus, the
amount of enzyme by which 1 .mu.mol of hydroxamic acid is formed in
1 minute is defined as 1 unit (1 U) of transglutaminase activity.
The complete procedure for determining activity is disclosed in
U.S. Pat. No. 5,156,956, which is hereby incorporated by
reference.
[0050] There are three presently preferred embodiments of the
invention. These embodiments are explained in detail by the
examples that follow. In the first embodiment, transglutaminase is
mixed with the comminuted cheese during the normal processed cheese
manufacturing process, but this mixture is given time to react
before it is heated up to the temperature at which processed cheese
is pasteurized. In the second embodiment, transglutaminase is added
to cheese curds as the cheese curds are packed into blocks or
barrels. The transglutaminase can then cross link proteins in the
cheese curds while the curds knit together as the cheese is aged
before it is comminuted and used to make processed cheese. In the
third embodiment, transglutaminase is added to UF cheese as it is
manufactured and before it is placed in barrels. Again, the
transglutaminase can cross link proteins while the UF cheese is
aged before being made into processed cheese.
[0051] All three of these preferred embodiments are common in that
transglutaminase is allowed to react on, and cross link the
proteins in, a cheese material rather than on a dilute system such
as milk or other dairy liquid. As noted above, the cheese material
will preferably have a moisture content of less than 60%, and more
preferably less than 50%. The cheese material will also preferably
have a pH of less than 5.6, and more preferably less than 5.3.
However, a UF cheese with a pH of between 5.6 and 6.0, and even as
high as 6.6, may also be used as a cheese material in some
embodiments of the invention. It is typical that the
transglutaminase will be mixed with the cheese material after the
cheese material has already been formed with those moisture and pH
properties. However, as explained below, there are modifications of
the process in which the transglutaminase may be mixed with a
material that then later has those properties. The key factor is
that during the majority of the time that the transglutaminase is
allowed to react on the protein in the cheese material, the
moisture content is preferably less than 60%. In this fashion, the
protein will be concentrated and the amount of transglutaminase
needed to catalyze the cross-linking reaction can be minimized.
[0052] It is possible that other ingredients that will eventually
be in the processed cheese may be mixed with the transglutaminase
as it is allowed to cross-link the proteins. However, such
ingredients are optional, and added only as a matter of convenience
or for some reason unrelated to the cross-linking reaction. For
example salt such as sodium chloride, is often added to curds
before the curds are packed in blocks or barrels. The
transglutaminase may be mixed with the salt or otherwise added to
the curds with the salt, the salt being an optional first other
ingredient in the second preferred embodiment of the invention.
Also, the cheese material in the preferred embodiments has not been
melted prior to the cross-linking reaction.
[0053] After the transglutaminase and cheese making material have
been mixed, conditions are provided under which the cross-linking
reaction can favorably occur. Commercially available ACTIVA TG-TI
transglutaminase sold by Ajinomoto U.S.A. Inc. has high activity in
a range of pH from 5-8. As with all reactions, the higher the
temperature the greater the reaction speed. However, the commercial
enzyme activity decreases gradually above about 50.degree. C.
(122.degree. F.) and drops to a fairly low level at 60.degree. C.
(140.degree. F.). At 80.degree. C. (176.degree. F.) the enzyme is
deactivated within 1 minute. Thus there is a balance between
stability and reaction rate that must be made. As a result the
optimum temperature range for the commercial enzyme is between
about 20.degree. C. (78.degree. F.) and about 60.degree. C.
(140.degree. F.). However, if sufficiently long reaction times are
available, lower temperatures may be used. The commercially
available enzyme is active at 15.degree. C. (59.degree. F.) and
even at 5.degree. C. (41.degree. F.). The preferred reaction
temperature are thus in the range of between about 50.degree. F.
and about 120.degree. F.
[0054] The reaction time, temperature and pH must be sufficient to
allow at least a portion of the proteins in the cheese material to
become cross-linked. Of course, a high degree of cross-linking is
desired. Normally the reaction time will be shorter in the first
preferred embodiment of the invention, and longer in the second and
third preferred embodiments. It would be preferable to give the
enzyme plenty of time to react. However, it is cost prohibitive to
significantly lengthen the manufacturing time for making processed
cheese. Of course, higher levels of enzyme can be added to achieve
a sufficient reaction, but again the enzyme cost is currently a
considerable factor that precludes this option. In the first
preferred embodiment of the invention the reaction time will
preferably be in the range of about 10 minutes to about 3 hours,
more preferably between about 11 and about 21/2 hours, and most
preferably about 2 hours. In this embodiment the enzyme will be
mixed at a ratio of between about 0.2 and about 10 units per gram
of protein. In the second and third preferred embodiments of the
invention, the enzyme can be used at lower levels, preferably less
than 5 units per gram of protein. The reaction time for these
embodiments of the invention will typically be greater than 24
hours, and more preferably greater than two weeks. These long
reaction times coincide with the periods that conventional cheese
and UF cheese are normally aged before being used to make processed
cheese. Thus in these embodiments, the time it takes to manufacture
process cheese is not lengthened at all.
[0055] The end of the reaction time occurs when the enzyme is
deactivated, which preferably occurs during the normal practice of
making processed cheese. Government regulations require the
processed cheese to be heated to a temperature of 150.degree. F.,
but it is more common that it is heated to 170.degree. F. or even
up to 210.degree. F. As noted above, these temperatures will
deactivate the commercially available transglutaminase.
[0056] In the preferred embodiments of the invention, the mixture
is preferably essentially free of emulsifying agents during the
reaction time. Thus, the preferred methods of the invention include
the step of mixing emulsifying agents with the mixture of cheese
material and transglutaminase after the reaction time has occurred.
The emulsifying agents are those normally used in making processed
cheese. Sodium citrate, trisodium phosphate and disodium phosphate
are the presently preferred emulsifying agents.
[0057] Typically additional processed cheese ingredients will be
added along with the cheese material having cross-linked proteins
to make the processed cheese. These second other optional
ingredients typically include sorbic acid, sodium chloride, dry
cream, concentrated milk fat, whey powder, whey protein
concentrate, milk protein concentrate, non-fat dry milk, buttermilk
powder and water.
[0058] As will be seen in the examples below, the optional second
ingredients in the second and third preferred embodiments may
include an additional cheese material that has not been treated
with transglutaminase.
[0059] As will also be seen in the examples below, the finished
processed cheese will typically have a moisture content of between
about 30% and about 60%, a fat content of between about 10% and
about 40%, and a protein content of between about 10% and about
30%. The processed cheese of the present invention will preferably
have a Mettler melt temperature of between about 120.degree. F. and
about 200.degree. F., more preferably between about 120.degree. F.
and about 150.degree. F. and a Schreiber melt score of at least 3
and more preferably at least 5.
[0060] It has been found that the firmness of processed cheese can
be affected by a number of factors unrelated to the cross linking
of proteins. For example, it has been found that processed cheese
made in a pilot plant typically has an Instron firmness of about
0.5 kgf less than that of processed cheese made on commercial
equipment. It is believed that the sheer applied to the cheese
material when making processed cheese has a big impact on the
resulting firmness, and that commercial scale equipment usually
involves higher sheer rates and greater firmness. Also, the age of
the cheese used to make the processed cheese has a major impact on
firmness. The use of younger cheese will result in greater
firmness. While the processed cheese of the present invention will
generally have an Instron firmness, corrected to 40% moisture, of
at least 1 kg, the preferred processed cheese of the present
invention made in commercial equipment, after being cooled for 3
days at 40.degree. F., will have an Instron firmness, corrected to
40% moisture, of at least 1.5 kgf. More preferably the Instron
firmness, corrected to 40% moisture, will be at least 1.8 kgf, and
most preferably at least 2.0 kgf In any event, it is preferred that
the cross linking increase the firmness of processed cheese to be
at least 5% greater than the firmness of processed cheese made by
the same procedure but without the cross-linking enzyme. The
following examples show how such a comparison can be made. It is
more preferred that the firmness increase by at least 10%. With
some preferred embodiments of the invention, firmness will be
increased by more than 25% and even 30%.
EXAMPLE 1
Treating Cheese Blend with Transglutaminase Shortly Before
Converting it into Processed Cheese
[0061] A ten pound processed cheese formula with a target finished
product composition of 39.5% moisture, 32.0% fat and 2.3% salt is
shown in Table 1 below: TABLE-US-00001 TABLE 1 Processed Cheese (10
lbs.) Cheese/Ingredient Weight (lb) Barrel Cheese (1.5 months old)
4.24 UF Cheese (1 month old) 2.08 Trisodium Phosphate 0.013 Sodium
Citrate 0.348 Sorbic Acid 0.02 Salt 0.117 Dry Cream 0.231
Concentrated Milk Fat 1.08 Whey Powder 0.37 Water 1.50 10 lbs
[0062] The above processed cheese formula was made using two types
of cheese: conventional barrel cheese and the UF cheese. The
conventional barrel cheese (500 lbs) was purchased from Associated
Milk Producers, Inc. (Paynsville, Wis.). The finished barrel cheese
met the standards of Cheddar cheese for manufacturing as defined by
21 C.F.R. .sctn.133.114 (2001). The UF cheese was made using the
Jameson et al. process as disclosed in U.S. Pat. No. 5,356,639;
with the modification that rennet was added. The UF cheese was
prepared by ultrafiltering and diafiltering milk to produce a
retentate, adding salt to the retentate, fermenting the retentate
and evaporating the fermented retentate to produce cheese
containing all the casein and whey protein of the original milk.
The fermented retentate was treated with rennet in an amount
sufficient to coagulate the fermented retentate prior to the
evaporation. Also, the fermented retentate was preheated to a
temperature of between about 170.degree. F. and about 190.degree.
F. before being introduced into the evaporator.
[0063] The transglutaminase enzyme preparation (ACTIVA TG-TI) was
obtained from Ajinomoto U.S.A. Inc. (Teanack, N.J.). The ACTIVA
TG-TI contains about 100 units of activity per gram. ACTIVA TG-TI
contains 99% maltodexrin and 1% transglutaminase enzyme.
[0064] A cheese blend containing the ground barrel cheese (4.24
lbs), UF cheese (2.08 lbs) and water (1.5 lbs) was mixed with 35
grams of ACTIVA TG-TI in a 10 lb size Rietz cooker for 2 hours at
85.degree. F. with the auger speed set at 1. This provided time for
the transglutaminase to cross link at least a portion of the
proteins in the cheese blend. The calculated ratio of ACTIVA TG-TI
(35 gram) to cheese blend (7.82 lbs) was estimated at .about.1.0%,
and the ratio of transglutaminase cross-linking enzyme to protein
was estimated at .about.5.13 units per gram of protein. A control
processed cheese was made using the same cheese blend except 35
grams of maltodextrin were used to replace the 35 grams of ACTIVA
TG-TI.
[0065] After the 2 hour, 85.degree. F. mixing, other ingredients
were added to the cooker and the temperature was increased as in a
normal processed cheese manufacturing process. Both control and
transglutaminase-treated cheese blends were used to make control
and inventive processed cheese according to the processed cheese
formula (Table 1). The control and inventive processed cheese
mixtures were each cooked to 170.degree. F. with indirect steam
jacket heating with the auger speed set at 4. It took approximately
10 minutes to reach the 170.degree. F. temperature in each case.
The indirect steam heat was then turned off. The finished processed
cheeses had a homogeneous, plastic, molten consistency when they
were discharged at 170.degree. F. to 14 oz. tubs. The cook
temperature of 170.degree. F. also provided the necessary heat to
deactivate the transglutaminase in the inventive cheese blend. The
finished processed cheeses were cooled at 40.degree. F. for 3 days.
The proximate composition, melt properties, and Instron firmness of
the finished processed cheeses are shown in Table 2 below:
TABLE-US-00002 TABLE 2 Processed Cheese Composition % SFI Mettler
Instron Increase Melt Temp Firmness in Cheese Blend % H.sub.2O %
Fat % Salt pH Score (.degree. F.) kgf* Firmness 1. Control 39.82
32.0 2.72 5.85 5 131 1.015 -- 2. Transglutaminase treated 39.48
32.5 2.44 5.87 4+ 148 1.441 41.97 (.about.1% ACTIVE TG-TI) *Instron
firmness readings corrected to 40% moisture.
[0066] The composition differences between the control and
transglutaminase-treated processed cheeses reflect normal
variations due to cheese ingredients and measurement error. The
data in Table 2 clearly demonstrates that the
transglutaminase-treated cheese blend of Example 1 resulted in a
significant increase in firmness (+41.9%) as compared to the
control.
EXAMPLE 2
Treating Cheese Curd with Transglutaminase During the Manufacture
of the Conventional Cheddar Cheese
[0067] Cheddar cheese in a 40 lb block form was made at Carr Valley
Cheese Co., Inc., (Lavelle, Wis.) following the conventional milled
curd process. A commercial transglutaminase enzyme preparation,
ACTIVA TG-TI, was first mixed with salt and then applied to the
milled curd during the regular salting step of the make process.
The curd/salt/ACTIVA TG-TI ratios were set at 1000 lbs curd/27.3
lbs salt/2.5 lbs ACTIVA TG-TI.
[0068] The calculated ratio of ACTIVA TG-TI to the curd was
.about.0.25%. The ratio of transglutaminase activity to protein was
estimated at .about.1 unit per gram of protein. A control Cheddar
cheese was made in an identical fashion compared to the cheese made
with the transglutaminase treatment except maltodextrin was used to
replace ACTIVA TG-TI.
[0069] The control and AVTIVA TG-TI treated cheese curd were then
each pressed in 40 lb hoops overnight and packed/stored in a
40.degree. F. cooler until their use in the processed cheese
formulation. The produced Cheddar cheeses had the following
proximate composition: TABLE-US-00003 TABLE 3 Cheddar Cheese (40 lb
Composition block) % H.sub.2O % Fat % Salt pH 1. Control 37.47 33
1.74 4.97 2. Transglutaminase treated 36.82 34 1.72 5.00
(.about.0.25% ACTIVA TG-TI)
[0070] Both control and transglutaminase-treated Cheddar cheeses
had a typical Cheddar cheese composition with acceptable flavor and
texture. Both the control and transglutaminase-treated Cheddar
cheeses were made into processed cheese as described below in
conjunction with Example 4.
EXAMPLE 3
Treating Fermented Milk Retentate with Transglutaminase During the
Manufacture of UF Cheese
[0071] The UF cheese was manufactured according to the modified
Jameson et al. process disclosed in U.S. Pat. No. 5,356,639
described in Example 1.
[0072] An ACTIVA TG-TI suspension (.about.28%) was first prepared
by dispersing 12 lbs ACTIVA TG-TI in 5 gallons of cold water. The
prepared ACTIVA TG-TI solution was then injected into the feed
stream of fermented retentate immediately after the preheating step
(which was at 170.degree. F.-190.degree. F.) and before reaching
the evaporator. The flash evaporation in the evaporator reduced the
temperature of the cheese material to about 120.degree. F. so that
the transglutaminase was not deactivated. Evaporation was completed
in a swept-surface evaporator with a product exit temperature of
90.degree. F.-95.degree. F. The feed rate of the fermented
retentate to the evaporator was set to produce .about.4900 lbs.
cheese/hr. The injection rate of the ACTIVA TG-TI solution
(.about.28%) was set at 5 gallons/hr.
[0073] The resulting UF cheese was calculated as containing (after
evaporation) 0.25% active ACTIVA TG-TI. The ratio of
transglutaminase activity to protein was calculated to be
.about.1.09 units/gram of protein. A control UF cheese was prepared
using identical feed materials and processing conditions except
that an injection of 28% maltodextrin was used to replace the
ACTIVA TG-TI solution.
[0074] Both control and transglutaminase-treated UF cheeses were
packed in 500 lbs. barrels and stored in a cooler at
.about.40.degree. F. until their use in the processed cheese
formulation. The produced UF cheeses had the following proximate
composition: TABLE-US-00004 TABLE 4 Composition UF Cheese (500 lbs.
barrel) % H.sub.2O % Fat % Salt pH 1. Control 33.23 38.0 1.76 5.51
2. Transglutaminase treated 32.82 37.5 1.78 5.58 (.about.0.25%
ACTIVA TG-TI)
[0075] Both control and transglutaminase-treated UF cheeses had a
typical UF cheese composition with acceptable flavor and texture.
Both the control and transglutaminase-treated UF cheeses were made
into processed cheese as described below in conjunction with
Example 4.
EXAMPLE 4
Processed Cheese made from Cheddar Cheese (Example 2) and UF Cheese
(Example 3)
[0076] Cheddar cheese (aged 28 days with approximately 0.25%
transglutaminase) from Example 2 and UF cheese (aged 22 days with
approximately 0.25% transglutaminase) from Example 3 were cooked
into process cheese following the formula of Table 5.
TABLE-US-00005 TABLE 5 Processed Cheese (10 lbs) Cheese/Ingredient
Weight (lbs) Cheddar Cheese (28 days, Example 2) 4.24 UF Cheese (22
days, Example 3) 2.08 Trisodium Phosphate 0.013 Sodium Citrate
0.348 Sorbic Acid 0.02 Salt 0.117 Dry Cream 0.231 Concentrated Milk
Fat 1.08 Whey Powder 0.37 Water 1.50 10 lbs
[0077] To demonstrate the impact of transglutaminase-treated cheese
on the finished processed cheese firmness, four 10 lb cook
experiments were conducted using different combinations of control
and transglutaminase-treated cheese materials as outlined below.
TABLE-US-00006 Cheese type used in processed cheese formulation
Cook ID Cheddar (Example 2) UF Cheese (Example 3) 1 Control Control
2 Transglutaminase Control 3 Control Transglutaminase 4
Transglutaminase Transglutaminase
[0078] A mixture of the ground Cheddar cheese (Example 2 or
control) and UF cheese (Example 3 or control) were blended with
other ingredients as shown in the above formula (Table 5). The
blend mixtures were cooked in a 10 lb Rietz cooker with indirect
steam jacket heating at an auger speed setting of 4. The finished
processed cheeses were heated to 170.degree. F. in a period of
about 10 minutes to achieve homogeneous, molten, plastic body and
immediately discharged into 14 oz. tubs for cooling
(.about.40.degree. F., 3 days). Cook ID 2, 3 and 4 thus relate to
Examples 2, 3 and 4, respectively. The proximate composition, melt
properties and Instron firmness of the processed cheeses are shown
in Table 6. TABLE-US-00007 TABLE 6 Processed Cheese Cheese Type
Mettler Instron UF Temp Firmness Cook ID Cheddar Cheese % H.sub.2O
% Fat % Salt pH SFI Melt (.degree. F.) kgf* 1 Control Control 40.45
33.0 2.46 5.78 7+ 125 1.026 2 Transgl. Control 40.46 33.5 2.58 5.82
5+ 134 1.317 3 Control Transgl. 40.70 34.5 2.48 5.81 5+ 134 1.152 4
Transgl. Transgl. 40.49 33.5 2.58 5.81 5+ 136 1.388 *Instron
firmness corrected to 40% moisture.
[0079] From the Instron firmness data in Table 6, the impact of
0.25% transglutaminase-treated Cheddar and UF cheese on processed
cheese firmness was calculated and is shown in Table 7.
TABLE-US-00008 TABLE 7 Instron* Processed Cheese Firmness Firmness
Comparison Increase Impact due to 1. Cook 2 vs. Cook 1 28.36% 0.25%
ACTIVA TG-TI treated Cheddar 2. Cook 4 vs. Cook 3 20.48% 0.25%
ACTIVA TG-TI treated Cheddar 3. Cook 3 vs. Cook 1 12.28% 0.25%
ACTIVA TG-TI treated UF cheese 4. Cook 4 vs. Cook 2 5.39% 0.25%
ACTIVA TG-TI treated UF cheese 5. Cook 4 vs. Cook 1 35.28% 0.25%
ACTIVA TG-TI treated Cheddar cheese and UP cheese * .times. 1.
.times. .times. 1.317 - 1.026 1.026 100 = 28.36 .times. % ##EQU1##
* .times. 2. .times. .times. 1.388 - 1.152 1.152 100 = 20.48
.times. % ##EQU2## * .times. 3. .times. .times. 1.152 - 1.026 1.026
100 = 12.28 .times. % ##EQU3## * .times. 4. .times. .times. 1.388 -
1.317 1.317 100 = 5.39 .times. % ##EQU4## * .times. 5. .times.
.times. 1.388 - 1.026 1.026 100 = 35.28 .times. % ##EQU5##
[0080] The results reported in Table 7 demonstrate that the
transglutaminase-treated Cheddar cheese (0.25% ACTIVA TG-TI) would
contribute .about.20.48 to 28.36% firmness increase in the
processed cheese formula studied. The data also demonstrates that
the transglutaminase-treated UF cheese (0.25% ACTIVA TG-TI) would
provide .about.5.39% to 12.28% firmness increase in the processed
cheese formula studied. The impact of both transglutaminase-treated
Cheddar cheese (0.25% ACTIVA TG-TI) and UF cheese (0.25% ACTIVA
TG-TI) resulted in even greater firmness increase (.about.35.28%)
in the processed cheese formula studied.
EXAMPLE 5
Commercial Scale Production of Processed Cheese Containing the
Transglutaminase-Treated UF Cheese (Example 3)
[0081] The UF cheese from Example 3, (containing approximately
0.25% ACTIVA TG-TI) and a conventional Cheddar cheese were ground
and blended with the other ingredients according to the following
formulation (Table 8). A control batch of processed cheese was made
using the control UF cheese from Example 3. TABLE-US-00009 TABLE 8
Cheese/Ingredient Weight (lbs) UF Cheese (Example 3) 3147 Young
Cheddar 3560 Medium Cheddar 173 Sodium Citrate 297 Concentrated
Milk Fat 594 Non-Fat Dry Milk 495 Whey Powder 100 Carotenal Color
8.6 Salt 127 Sorbic 20 Water 1702 10223.6
[0082] Blend 1 contained the control UF cheese (0.25% maltodextrin,
Example 3).
[0083] Blend 2 contained the transglutaminase-treated UF cheese
(0.25% ACTIVA TG-TI, Example 3). All other cheese/ingredients in
blends 1 and 2 were the same.
[0084] The ground cheese and other ingredient mixture was blended
for 30 minutes before being fed continuously into a commercial size
swept surface cooker with indirect steam jacket heating. The blend
mixture was cooked to 190.degree. F. and discharged with a molten
plastic homogeneous body. The molten process cheese was quickly
cooled down to below 60.degree. F. The finished process cheese was
further cooled down (<40.degree. F.) inside the final packages
during distribution.
[0085] The proximate composition, melt properties and Instron
firmness of the finished process cheeses are shown in Table 9.
TABLE-US-00010 TABLE 9 % Instron Mettler Instron Firmness Process
Cheese Melt Firmness Increase Blend ID UF Cheese Type % H.sub.2O %
Fat % Salt pH SFI Melt (.degree. F.) kgf* ** 1 Control 39.16 30.0
2.64 5.99 3+ 146 2.388 -- 2 Transglutaminase 38.95 31.0 2.44 6.00 4
156 2.605 9.08 treated(.about.0.25% ACTIVA TG-TI) *Instron firmness
corrected to 40% moisture ** .times. 2.605 - 2.388 2.388 100 = 9.08
.times. % ##EQU6##
[0086] The higher Instron firmness results in Table 9 compared to
Table 6 reflect the fact that processed cheese made in commercial
scale equipment is generally firmer than processed cheese made in
pilot plant equipment, and the fact that the cheese used in Example
5 had a younger average age than the cheese used in Examples 1-4.
The test results reported in Table 9 demonstrate that the
transglutaminase-treated UF cheese (0.25% ACTIVA TG-TI) provided
9.08% firmness increase in the processed cheese formula
studied.
[0087] An increased firmness in processed cheese has numerous
benefits. A firmer product can be packaged at higher rates of
speed. Manufacturing steps are also easier to perform when the
processed cheese is firm. The packaged product maintains its shape,
resisting cold flow. The moisture content of the product can be
increased (resulting in a lower product cost) if the firmness of
the product can otherwise be maintained. The preferred embodiment
of the present invention provides a mechanism whereby the firmness
of the processed cheese can be improved without adding
significantly to the time required to make the processed cheese,
and while maintaining acceptable melt properties. Further, the
amount of transglutaminase required to improve the firmness is
minimized by using it in a concentrated protein composition.
[0088] It should be appreciated that the method and products of the
present invention are capable of being incorporated in the form of
a variety of embodiments, only a few of which have been illustrated
and described above. The invention may be embodied in other forms
without departing from its spirit or essential characteristics. For
example, while the transglutaminase was mixed with the cheese blend
in the cooker in Example 1, commercial use of that embodiment of
the invention would likely involve mixing the transglutaminase with
the cheese blend in a different vessel, such as a blender, and
later placing the mixture into the cooker, with the time for the
cross-linking reaction occurring in the blender, the cooker or even
in an intermediate vessel.
[0089] As noted above, the other processed cheese ingredients,
particularly the emulsifying agents, are preferably added after the
cross-linking reaction has progressed. Alternatively, these other
ingredients could be added before the time for the cross-linking
reaction has elapsed. Also, if a preheating step were not used in
the UF cheese-making process, the transglutaminase could be added
at an earlier point in the process, even to the initial milk after
it was pasteurized, because the transglutaminase would be retained
with the milk proteins in the ultrafiltration and diafiltration
steps. Also, the UF cheese could be made by direct acidification
rather than fermentation, and rennet may be added to the retentate
prior to the fermentation or not used at all.
[0090] The above examples use Cheddar and UF cheese, but other
cheeses can be used, particularly other American-type cheeses and
pasta filata-type cheeses. The described embodiments are thus to be
considered in all respects only as illustrative and not
restrictive, and the scope of the invention is, therefore,
indicated by the appended clams rather than by the foregoing
description. All changes that come within the meaning and range of
equivalency of the claims are to be embraced within their
scope.
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