U.S. patent application number 10/630217 was filed with the patent office on 2004-02-12 for granule with hydrated barrier material.
Invention is credited to Becker, Nathaniel T., Christensen, Robert I. JR., Dale, Douglas A., Gaertner, Alfred L., Ghani, Mahmood M..
Application Number | 20040029756 10/630217 |
Document ID | / |
Family ID | 22082210 |
Filed Date | 2004-02-12 |
United States Patent
Application |
20040029756 |
Kind Code |
A1 |
Becker, Nathaniel T. ; et
al. |
February 12, 2004 |
Granule with hydrated barrier material
Abstract
A granule having high stability and low dust is described. The
granule includes a hydrated barrier material having moderate or
high water activity. Also described are methods of producing the
granules.
Inventors: |
Becker, Nathaniel T.;
(Burlingame, CA) ; Christensen, Robert I. JR.;
(Pinole, CA) ; Gaertner, Alfred L.; (San Bruno,
CA) ; Ghani, Mahmood M.; (Milpitas, CA) ;
Dale, Douglas A.; (Pacifica, CA) |
Correspondence
Address: |
JEFFERY D. FRAZIER
GENENCOR INTERNATIONAL, INC.
925 PAGE MILL ROAD
PALO ALTO
CA
94304
US
|
Family ID: |
22082210 |
Appl. No.: |
10/630217 |
Filed: |
July 30, 2003 |
Related U.S. Patent Documents
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Application
Number |
Filing Date |
Patent Number |
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10630217 |
Jul 30, 2003 |
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09581717 |
Jun 16, 2000 |
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6602841 |
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09581717 |
Jun 16, 2000 |
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PCT/US98/27214 |
Dec 21, 1998 |
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60068382 |
Dec 20, 1997 |
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Current U.S.
Class: |
510/226 ;
435/183; 510/320 |
Current CPC
Class: |
C12N 9/48 20130101; C11D
11/0088 20130101; C11D 3/38672 20130101 |
Class at
Publication: |
510/226 ;
510/320; 435/183 |
International
Class: |
C12N 009/00; C11D
003/386 |
Claims
1. A granule comprising an enzyme core and a barrier material,
wherein the barrier material comprises a hydrated barrier material
with moderate or high water activity.
2. The granule of claim 1, wherein the barrier material is a
salt.
3. The granule of claim 1, wherein the salt is selected from the
group consisting of magnesium sulfate heptahydrate, zinc sulfate
heptahydrate, copper sulfate pentahydrate, sodium phosphate dibasic
heptahydrate, magnesium nitrate hexahydrate, sodium borate
decahydrate, sodium citrate dihydrate and magnesium acetate
tetrahydrate.
4. The granule of claim 1, wherein the barrier-material is part of
the protein core.
5. The granule of claim 1, wherein the barrier material is coated
over the protein core.
6. The granule of claim 1, further comprising a layer of material
between the protein core and the barrier material.
7. The granule of claim 1, further comprising a layer of material
over the barrier layer and protein core.
8. The granule of claim 1, wherein the protein is an enzyme.
9. The granule of claim 1, wherein the water activity is greater
than 0.25.
10. A method of producing a granule comprising: a) providing a
protein core; b) coating a hydrated barrier material with moderate
or high water activity onto the protein core.
11. The method of claim 10, further comprising a coating over the
barrier material.
Description
BACKGROUND OF THE INVENTION
[0001] Recently the use of enzymes, especially of microbial origin,
has become more and more common. Enzymes are used in several
industries including, for example, the starch industry, the dairy
industry, and the detergent industry. It is well known in the
detergent industry that the use of enzymes, particularly
proteolytic enzymes, has created industrial hygiene concerns for
detergent factory workers, particularly due to the health risks
associated with dustiness of the available enzymes.
[0002] Since the introduction of enzymes into the detergent
business, many developments in the granulation and coating of
enzymes have been offered by the industry. See for example the
following patents relating to enzyme granulation:
[0003] U.S. Pat. No. 4,106,991 describes an improved formation of
enzyme granules by including within the composition undergoing
granulation, finely divided cellulose fibers in an amount of 2-40%
w/w based on the dry weight of the whole composition. In addition,
this patent describes that waxy substances can be used to coat the
particles of the granulate.
[0004] U.S. Pat. No. 4,689,297 describes enzyme containing
particles which comprise a particulate, water dispersible core
which is 150-2,000 microns in its longest dimension, a uniform
layer of enzyme around the core particle which amounts to 10%-35%
by weight of the weight of the core particle, and a layer of
macro-molecular, film-forming, water soluble or dispersible coating
agent uniformly surrounding the enzyme layer wherein the
combination of enzyme and coating agent is from 25-55% of the
weight of the core particle. The core material described in this
patent includes clay, a sugar crystal enclosed in layers of corn
starch which is coated with a layer of dextrin, agglomerated potato
starch, particulate salt, agglomerated trisodium citrate, pan
crystallized NaCl flakes, bentonite granules or prills, granules
containing bentonite, Kaolin and diatomaceous earth or sodium
citrate crystals. The film forming material may be a fatty acid
ester, an alkoxylated alcohol, a polyvinyl alcohol or an
ethoxylated alkylphenol.
[0005] U.S. Pat. No. 4,740,469 describes an enzyme granular
composition consisting essentially of from 1-35% by weight of an
enzyme and from 0.5-30% by weight of a synthetic fibrous material
having an average length of from 100-500 micron and a fineness in
the range of from 0.05-0.7 denier, with the balance being an
extender or filler. The granular composition may further comprise a
molten waxy material, such as polyethylene glycol, and optionally a
colorant such as titanium dioxide.
[0006] U.S. Pat. No. 5,254,283 describes a particulate material
which has been coated with a continuous layer of a non-water
soluble, warp size polymer. U.S. Pat. No. 5,324,649 describes
enzyme-containing granules having a core, an enzyme layer and an
outer coating layer. The enzyme layer and, optionally, the core and
outer coating layer contain a vinyl polymer.
[0007] WO 91/09941 describes an enzyme containing preparation
whereby at least 50% of the enzymatic activity is present in the
preparation as enzyme crystals. The preparation can be either a
slurry or a granulate.
[0008] WO 97/12958 discloses a microgranular enzyme composition.
The granules are made by fluid-bed agglomeration which results in
granules with numerous carrier or seed particles coated with enzyme
and bound together by a binder.
[0009] However, even in light of these developments offered by the
industry (as described above) there is a continuing need for
low-dust enzyme granules which have additional beneficial
characteristics. Additional beneficial characteristics needed in
the enzyme granulation industry are low-residue granule
formulations (where low residue is defined as a reduced tendency to
leave noticeable undissolved residues on clothes or other
material), and improved stability formulations. Accomplishing all
these desired characteristics simultaneously is a particularly
challenging task since, for example, many delayed release or
low-dust agents such as fibrous cellulose or warp size polymers
leave behind insoluble residues.
[0010] Therefore, it is an object of the present invention to
provide low-dust, low residue, highly soluble enzyme granules
having increased stability. It is another object of the present
invention to provide processes which afford the formation of such
improved granules.
SUMMARY OF THE INVENTION
[0011] One embodiment of the present invention is a granule that
includes a protein core and a hydrated barrier material with
moderate or high water activity. The hydrated barrier material can
be in one or more layers and/or can be included in the protein
core.
[0012] A further embodiment of the present invention is a granule
that includes an enzyme core and a hydrated barrier material with
moderate or high water activity. The hydrated barrier material can
be in one or more layers and/or can be included in the enzyme
core.
[0013] Another embodiment is a method of producing the above
granule.
DETAILED DESCRIPTION OF THE INVENTION
[0014] The present invention provides a granule with improved
stability having low dust. The granule includes a protein core and
a hydrated barrier material with moderate or high water
activity.
[0015] A "protein core" or an "enzyme core" can be homogenous such
as that described in U.S. patent application Ser. No. 08/995,457 or
layered as described in U.S. Pat. No. 5,324,649.
[0016] Proteins that are within the scope of the present invention
include pharmaceutically important proteins such as hormones or
other therapeutic proteins and industrially important proteins such
as enzymes.
[0017] Any enzyme or combination of enzymes may be used in the
present invention. Preferred enzymes include those enzymes capable
of hydrolyzing substrates, e.g. stains. These enzymes are known as
hydrolases which include, but are not limited to, proteases
(bacterial, fungal, acid, neutral or alkaline), amylases (alpha or
beta), lipases, cellulases and mixtures thereof. Particularly
preferred enzymes are subtilisins and cellulases. Most preferred
are subtilisins such as described in U.S. Pat. No. 4,760,025, EP
Patent 130 756 B1 and EP Patent Application WO 91/06637, which are
incorporated herein by reference, and cellulases such as Multifect
L250.TM. and Puradax.TM., commercially available from Genencor
International. Other enzymes that can be used in the present
invention include oxidases, transferases, dehydratases, reductases,
hemicellulases and isomerases.
[0018] As noted, the barrier material can be coated over the
protein core in one or more layers or made part of the protein core
in order to insulate or to impede transport of water and
inactivating substances to the protein. When the barrier material
is part of the protein core, it can be dispersed throughout the
core or as a layer in the core.
[0019] Suitable hydrated barrier materials with moderate or high
water activity can include salts of an inorganic or organic acid,
sugars, polysaccharides, lipids, proteins or synthetic polymers;
preferably salts.
[0020] The term "water activity", symbolized a.sub.w, refers to the
fractional relative humidity of an atmosphere in equilibrium with a
solid or liquid phase material, i.e., the ratio of the partial
pressure of water vapor to that present above pure water at the
same temperature. In all phases between which water distribution
has reached equilibrium, it is by definition equal. The term
"relative humidity" is generally used to describe the water in the
atmosphere or gas phase in equilibrium with the solid, and is
expressed as a percentage, with 100% as the relative humidity of
pure water in a closed system. Thus, for any water activity value,
there is a corresponding relative humidity given by %
RH=100*a.sub.w.
[0021] Water activity can be readily measured by methods known in
the art, typically by placing a sample of the material inside the
temperature-controlled chamber of a water activity meter, such as
the Water Activity System Model D2100 available from Rotronic
Instrument Corp. (Huntington, N.Y.), and allowing the measurement
to reach equilibrium as indicated on the display.
[0022] A "hydrated" barrier material contains water in a free or
bound form, or a combination of the two. The water of hydration can
be added either during or after the coating process. The degree of
hydration will be a function of the material itself and the
temperature, humidity and drying conditions under which it is
applied.
[0023] "Moderate or high" water activity includes a water activity
of at least 0.25, preferably greater than 0.30, most preferably
greater than 0.35. The water activity referred to herein is that of
the granule itself once it has the barrier material--but no further
coatings--coated onto it. Further coatings may mask accurate
measurement of the water activity of the barrier material as a
distinct layer.
[0024] Without wishing to be bound by theory, it is expected that
materials with a water activity greater than 0.25 will have a
reduced driving force for picking up water under storage conditions
in which the relative humidity is greater than 25%. Most climates
have relative humidities above 25%. Many detergents have water
activities in the range of about 0.3 to 0.4. If the water activity
of the granule is actually higher than that of the surrounding
detergent or storage climate, the driving force for pick up of
water by the granule should be eliminated, and in fact water may be
given up by the granule to its surroundings. Even if the water
activity of the granule is lower than that of the detergent or the
corresponding relative humidity, the water present in the barrier
layer would act as a shield limiting the amount of water and hence
in activating substances being picked up by the granule and
affecting the protein core.
[0025] In the case of salt hydrates, the hydrated material is a
crystalline salt hydrate with bound water(s) of crystallization.
The hydrate should be chosen and applied in a manner such that the
resulting coated granule will have a water activity in excess of
0.25, or as high as possible while still providing a granule which
is dry to the touch. By applying a salt hydrate, or any other
suitable hydrated barrier material, in such a manner, as noted
above, one expects that this would eliminate any driving force for
further uptake of water by the granule. As an important
consequence, the driving force for transport of substances which
may be detrimental to enzyme activity, such as perborate or
peroxide anion, is removed. Without water as a vehicle, these
substances are less likely to penetrate the enzyme core. Empirical
data demonstrates that enzyme activity in the granule is
substantially enhanced by coating the enzyme core with stable salt
hydrates.
[0026] Preferred salts include magnesium sulfate heptahydrate, zinc
sulfate heptahydrate, copper sulfate pentahydrate, sodium phosphate
dibasic heptahydrate, magnesium nitrate hexahydrate, sodium borate
decahydrate, sodium citrate dihydrate and magnesium acetate
tetrahydrate.
[0027] The granules of the present invention can also comprise one
or more coating layers. For example, such coating layers may be one
or more intermediate coating layers, or such coating layers may be
one or more outside coating layers or a combination thereof.
Coating layers may serve any of a number of functions in a granule
composition, depending on the end use of the granule. For example,
coatings may render the protein resistant to oxidation by bleach,
bring about the desirable rates of dissolution upon introduction of
the granule into an aqueous medium, or provide a barrier against
ambient moisture in order to enhance the storage stability of the
enzyme and reduce the possibility of microbial growth within the
granule.
[0028] Suitable coatings include polyvinyl alcohol (PVA), polyvinyl
pyrrolidone (PVP), cellulose derivatives such as methylcellulose,
hydroxypropylmethyl cellulose, hydroxycellulose, ethylcellulose,
carboxymethyl cellulose, hydroxypropyl cellulose, polyethylene
glycol, polyethylene oxide, chitosan, gum arabic, xanthan,
carrageenan, latex polymers, and enteric coatings. Furthermore,
coating agents may be used in conjunction with other active agents
of the same or different categories.
[0029] Suitable PVAs for incorporation in the coating layer(s) of
the granule include partially hydrolyzed, fully hydrolyzed and
intermediately hydrolyzed PVAs having low to high degrees of
viscosity. Preferably, the outer coating layer comprises partially
hydrolyzed PVA having low viscosity. Other vinyl polymers which may
be useful include polyvinyl acetate and polyvinyl pyrrolidone.
Useful copolymers include, for example, PVA-methylmethacrylate
copolymer and PVP-PVA copolymer.
[0030] The coating layers of the present invention may further
comprise one or more of the following: plasticizers, extenders,
lubricants, pigments, and optionally additional enzymes. Suitable
plasticizers useful in the coating layers of the present invention
are plasticizers including, for example, polyols such as sugars,
sugar alcohols, or polyethylene glycols (PEGs), urea, glycol,
propylene glycol or other known plasticizers such as triethyl
citrate, dibutyl or dimethyl phthalate or water. Suitable pigments
useful in the coating layers of the present invention include, but
are not limited to, finely divided whiteners such as titanium
dioxide or calcium carbonate or colored pigments or dyes or a
combination thereof. Preferably such pigments are low residue
pigments upon dissolution. Suitable extenders include sugars such
as sucrose or starch hydrolysates such as maltodextrin and corn
syrup solids, clays such as kaolin and bentonite, and talc.
Suitable lubricants include nonionic surfactants such as Neodol,
tallow alcohols, fatty acids, fatty acid salts such as magnesium
stearate and fatty acid esters.
[0031] The outer coating layer of the present invention preferably
comprises between about 1-25% by weight of the coated granule.
[0032] Adjunct ingredients may be added to the granules of the
present invention. Adjunct ingredients may include: metallic salts;
solubilizers; activators; antioxidants; dyes; inhibitors; binders;
fragrances; enzyme protecting agents/scavengers such as ammonium
sulfate, ammonium citrate, urea, guanidine hydrochloride, guanidine
carbonate, guanidine sulfamate, thiourea dioxide, monoethanolamine,
diethanolamine, triethanolamine, amino acids such as glycine,
sodium glutamate and the like, proteins such as bovine serum
albumin, casein and the like etc.; surfactants including anionic
surfactants, ampholytic surfactants, nonionic surfactants, cationic
surfactants and long-chain fatty acid salts; builders; alkalis or
inorganic electrolytes; bleaching agents; bluing agents and
fluorescent dyes and whiteners; and caking inhibitors.
[0033] The granules described herein may be made by methods known
to those skilled in the art of enzyme granulation, including
pan-coating, fluid-bed coating, fluid-bed agglomeration, prilling,
disc granulation, spray drying, extrusion, centrifugal extrusion,
spheronization, drum granulation, high shear agglomeration, or
combinations of these techniques.
[0034] The following examples are representative and not intended
to be limiting. One skilled in the art could choose other proteins,
protein cores, enzymes, enzyme cores, seed particles, methods and
coating agents based on the teachings herein.
EXAMPLES
Example 1
[0035] Stability of Maqnesium Sulfate Coated Protease Granules
[0036] A. In a Deseret 60 fluidized bed coater, 54.1 kg of
sucrose/starch non pareil seeds were charged and fluidized. Onto
these cores, 75.8 kg of protease UF concentrate containing 62.9
g/kg subtilisin protease were sprayed under the following
conditions. (Ranges indicate initial and final values over the
course of the specified ramp time):
1 Ramp time: 80 minutes Fluid feed rate 0.6-1.0 liter/min
Atomization pressure 75 psi Inlet air temperature 85-92 degrees C.
Outlet air temperature 50 degrees C. Fluidization air rate 18
m3/min
[0037] A solution of magnesium sulfate was prepared by adding 22.2
kg of magnesium sulfate heptahydrate into 22.2 kg of water, and
this was sprayed onto the enzyme-coated cores under the following
conditions in order to provide that 20% of the final granule would
be magnesium sulfate heptahydrate, with care being taken to keep
the bed temperature close to, but slightly below, 50 degrees
C.:
2 Ramp time: 40 minutes Fluid feed rate 0.6-1.7 liter/min
Atomization pressure 45 psi Inlet air temperature 70-84 degrees C.
Outlet air temperature 48-50 degrees C. Fluidization air rate 18
m3/min
[0038] Finally, a polymer coating solution was prepared by
dissolving 6.35 kg of Elvanol 51-05 polyvinyl alcohol, 7.94 kg
titanium dioxide and 1.59 kg Neodol 23-6.5T nonionic surfactant in
50.12 kg water and spraying over the salt-coated enzyme cores under
the following conditions:
3 Ramp time: 10 min, then constant for 100 min Fluid feed rate 0.6
liter/min Atomization pressure 75 psi Inlet air temperature 50
degrees C. Outlet air temperature 75-80 degrees C. Fluidization air
rate 18 m3/min
[0039] The harvested granules had an enzyme concentration of
approximately 40 g/kg.
[0040] B. Accelerated Stability Test
[0041] The stability of many enzyme granules formulated into
bleach-containing detergents is generally excellent, showing
generally no more than about 10 to 20% loss in activity over 6
weeks storage at 30 to 37.degree. C. and 70% to 80% R.H. However,
to aid in the development and screening of granular formulations,
it is desirable to have an accelerated means of determining
relative granule stability. The conditions of the accelerated
stability test (AST) are far more severe than enzyme granules or
detergents would ever encounter in realistic storage or transport.
The AST is a "stress test" designed to discriminate differences
between formulations which would otherwise not be evident for weeks
or months.
[0042] In this test, a test detergent base was made from the
following ingredients:
4 72% WFK-1 detergent base (WFK, Forschunginstitut fuer
Reinigungstechnologie e.V., Krefeld, Germany) 25% sodium perborate
monohydrate (Degussa Corp., Allendale Park, New Jersey.) 3% TAED
bleach activator (Warwick International,
(=tetraacetylethylenediamine) Mostyn, UK)
[0043] For each enzyme sample to be tested, three identical tubes
were prepared by adding 1 gram of the test base and 30 mg of enzyme
granules to a 15 ml conical tube and mixed by inverting the capped
tube 5-8 times by hand. A hole was drilled in the tube cap with a
{fraction (1/16)} inch drill bit. One of the three tubes was
assayed immediately and the other two were stored in a humidity
chamber set at 50.degree. C. and 70% R.H. One of the two stored
tubes was assayed after 1 day of storage; the second, after 3 days
of storage. Storage stability was reported for Day 1 and Day 3 by
dividing the remaining activity by the original activity at Day 0,
expressed as a percentage.
[0044] The enzyme activity was determined by adding to each tube 30
ml of 0.25M MES pH 5.5 buffer containing 20 .mu.l Catalase HP L5000
(Genencor International, Rochester, N.Y.) and incubating for 40
minutes to inactivate the perborate. After this, the enzyme was
assayed by adding 10 .mu.l of the test tube mixture and 10 .mu.l of
sAAPF protease substrate to 980 .mu.l of 0.1 M Tris pH 8.6, then
incubating at 25.degree. C. over 3 minutes, and measuring the
optical absorbance at 410 nm. The slope of the absorbance vs. time
was then multiplied by the dilution factor and the known extinction
coefficient for the specific protease to obtain an enzyme activity
as concentration in mg/ml.
[0045] The process described in A above was repeated three more
times, the only difference being that the outlet air temperature
was controlled at a setpoint of 40, 60 and 70 degrees C. in each of
the three separate runs. Samples were removed from all four batches
after the magnesium sulfate barrier coating had been applied, and
water activities of the granules were measure in a Rotronic Water
Activity System, as reported in Table 1. Two of the granules, after
application of the final polymer coating, were placed in WFK-1
detergent formula and stored in tubes with drilled caps for three
days at 50 degrees C. and 70% relative humidity, according to the
accelerated stability test method described above. Tubes were
withdrawn from the humidity chamber and assayed after 1 day and 3
days. The percent retained activities are reported in Table 1. The
results indicate the granules in which magnesium sulfate was coated
at 50 degrees C. outlet temperature are significantly more stable
than those coated at 70 degrees C., and that the more stable
granules had a water activity above 0.35, while the less stable
granules had a significantly lower water activity.
5TABLE 1 Stability of Magnesium Sulfate Coated Enzyme Granules
A.sub.w of MgSO4 Outlet Coated Percent Retained Activity of Temp
Protease Granules Stored in Bleach Detergent (C) Cores 0 days 1 day
3 days 40 0.374 50 0.409 100% 108% 97% 60 0.140 70 0.165 100% 94%
63%
Example 2
[0046] Stability of Sodium Citrate Coated Protease Granules
[0047] A. In a Vector 60 coater, 25 kg of sucrose/starch nonpareil
seeds were fluidized and 30.9 kg of subtilisin protease concentrate
with a concentration of 65.9 g/L and 18.3% total solids were
sprayed onto the fluidized cores under the following
conditions:
6 Ramp time: 55 minutes Fluid feed rate 0.5-0.9 liter/min
Atomization pressure 75 psi Inlet air temperature 60-95 degrees C.
Outlet air temperature 50 degrees C. Fluidization air rate 24
m3/min
[0048] A solution of trisodium citrate was prepared by adding 13.2
kg of trisodium citrate dihydrate into 19.7 kg of water, and this
was sprayed onto the enzyme-coated cores under the following
conditions in order to provide that 25% of the final granule would
be trisodium citrate dihydrate, with care being taken to keep the
bed temperature close to 50 degrees C:
7 Ramp time: 23 minutes Fluid feed rate 0.6-1.9 liter/min
Atomization pressure 75 psi Inlet air temperature 60-95 degrees C.
Outlet air temperature 50 degrees C. Fluidization air rate 24
m3/min
[0049] Finally, a polymer coating solution was prepared by
dissolving 2.94 kg Methocel HPMC, 0.98 kg polyethylene glycol,
molecular weight 600, 2.06 kg titanium dioxide and 0.59 kg Neodol
23-6.5T nonionic surfactant in 55.88 kg water and spraying over the
salt-coated enzyme cores under the following conditions:
8 Ramp time: 10 min, then 80 minutes constant Fluid feed rate
0.5-0.7 liter/min Atomization pressure 75 psi Inlet air temperature
75-80 degrees C. Outlet air temperature 60 degrees C. Fluidization
air rate 18 m3/min
[0050] The harvested granules had a weight of 49.5 kg and an enzyme
concentration of approximately 40 g/kg.
[0051] B. The above process was repeated under the same conditions,
but the outlet air temperature was controlled at a setpoint of 70
degrees C. Samples were removed from both batches after the sodium
citrate barrier coating had been applied, and water activities of
the granules were measure in a Rotronic Water Activity System, as
reported in Table 2. The two granules, after application of the
final polymer coating, were placed in an automatic dish detergent
base and stored in sealed tubes for 84 days at 37 degrees C. Tubes
were withdrawn from the humidity chamber and assayed after 14, 42
and 84 days. The percent retained activities are reported in Table
2. The results indicate the granules in which sodium citrate was
coated at 50 degrees C. outlet temperature are significantly more
stable than those coated at 70 degrees C., and that the more stable
granules had a water activity above 0.25, while the less stable
granules had a significantly lower water activity.
9TABLE 2 Stability of Sodium Citrate Coated Enzyme Granules A.sub.w
of Na3 Citrate Outlet Coated Percent Retained Activity of Temp
Protease Granules Stored in Bleach Detergent (C) Cores 0 days 14
days 42 days 84 days 55 0.272 100% 90% 89% 87% 70 0.059 100% 86%
81% 75%
* * * * *