Isophthalic polymer coated particles

The invention relates to use of a water dispersible isophthalic acid polymer as a dust free coating on particulates. The particles provide a timed release of the contents of the particle which allows for reduced amounts of active agents on the coatings and less interference between active agents in the coating or environment and the particulates.

FIELD OF THE INVENTION 
The invention relates to dried dust free particles. In particular the 
invention relates to particles which have been coated with a water 
dispersible coating of an isophthalic acid polymer. The particles are 
particularly useful for use as a coating with laundry detergent granules. 
BACKGROUND OF THE INVENTION 
When formulating dried particulate products such as would be made in a 
fluid bed dryer (e.g. particles for use in washing compositions), two 
problems normally occur. The first problem is that of dusting. The method 
of manufacturing particles can create very fine powders which cause 
dermatologic effects when the product contains sensitizing agents (e.g. 
enzymes in a detergent granule). The second problem relates to the need to 
incorporate relatively high amounts of ingredients such as enzyme 
protecting agents, masking agents and scavengers (e.g. chlorine 
scavengers) into products for the purpose of binding ions which can 
inactivate an active ingredient in the particle. It would be desirable to 
use less of these types of materials or to use them without interfering 
with enzymes that may be present. 
Many commercially useful enzymes are produced by microorganisms, 
particularly bacteria, yeast and filamentous fungi. These enzymes are 
especially useful in detergent and food applications. With the advent of 
biotechnology and recombinant DNA techniques, other enzymes from mammlian 
sources are produced recombinantly in microorganisms. When enzymes are 
produced in a microbial host they are usually either secreted directly 
into the fermentation both by the microorganism or released into the 
fermentation broth by lysing the cell. The enzyme can then be recovered 
from the broth in a soluble form by a number of techniques including 
filtration, centrifugation, membrane filtration, chromatography and the 
like. The dissolved enzyme can be converted to a dry form from a liquid 
using techniques such a precipitation, crystallization or spray-drying. A 
problem associated with dry enzyme preparations is that there is a high 
dust level associated with them, which can cause dermatologic distress to 
the manufacturer, consumer or any other person handling the enzyme. It has 
been a desire in the art to treat these dry enzymes so as to reduce the 
hazard of dusting. To control dusting and increase particle size, dry 
enzymes are often granulated by various means known by those skilled in 
the art. 
Various enzyme formulations and processes for these preparations have been 
developed in an effort to alleviate the dusting problem. For example, 
German Patent No. 21 37 042 discloses a process in which an 
enzyme-containing formulation is extruded through a die onto the revolving 
plate of a spheronizing device to form sperical particles of the 
enzyme-containing formulations which are optionally coated with a material 
designed to prevent dusting. 
In U.S. Pat. No. 4,087,368, there is disclosed an enzyme granule 
formulation in which rods or spheres of an enzyme in admixture with 
magnesium alkyl sulfate and ethylene oxide are provided. 
U.S. Pat. No. 4,016,040 discloses a method for the preparation of 
free-flowing substantially dust-free, spherical enzyme-containing beads 
prepared by blending a powdered concentrate of the enzyme with a binder in 
molten form and spraying droplets of the blend through a spray nozzle into 
cool air to solidify the droplets and form the beads. 
In U.S. Pat. No. 4,242,219, there is claimed a process for the preparation 
of enzyme-containing particles prepared by mixing the dry enzyme with a 
hydrophilic organic cohesive material, a building agent or a mixture 
regulating agent and mechanically dividing it into particles of the 
desired size and shape which are then coated with a water repellent 
material. 
Another type of granular enzyme formulation is described in U.S. Pat. No. 
4,009,076. This formulation is prepared by mixing the dry enzyme with a 
solid nonviable substance and optionally a cohesive organic material as 
binder to form an enzymatically active core. An enzyme slurry containing 
the cohesive organic material can be sprayed onto, for example, sodium 
tripolyphosphate in a mixer or an enzyme powder can be mixed with the 
sodium tripolyphosphate and the cohesive organic material sprayed onto it 
with subsequent extrusion through a die. The enzyme-containing granule is 
sprayed with an aqueous solution containing a plasticized organic resin, 
then dried. 
A process is described in GDR Patent 0 151 598 in which sodium 
tripolyphosphate is sprayed with an aqueous fermentation broth and 
agglomerated in a cyclone apparatus. The agglomerates are removed from the 
cyclone apparatus while still wet and placed in a mechanical blender with 
a drying detergent formulation and intensively mixed. 
In British Patent No. 1,483,591, there is described a process for coating 
water soluble or water dispersible particles, including enzyme particles, 
using a fluidized-bed reactor. This reference involves a dust-free coating 
technique for enzyme particles which have been granulated by other 
processes such as prilling or spheronizing. 
In U.S. Pat. No. 4,689,297, there is described a method for preparing 
dust-free enzyme involving dissolving or suspending dry enzyme in solution 
to make a slurry of at least 30% w/w of the solids enzymes, spraying it on 
a hydratable core and then coating it with macromolecular material. 
In PCT patent application 87/00057 there is described a detergent enzyme 
product with an enzyme core on which is an enteric coating. Such coatings 
are water soluble and dissolve readily at high pH's while resisting 
dissolution at low pH's. 
Oxidant scavengers or enzyme protecting agents or masking agents can be 
included in washing compositions to bind free ions, compounds or the like, 
which may inactivate the enzyme or decrease its efficacy or otherwise 
interfere with the ability of the detergent or enzyme preparation. 
It is desirable to produce improved dust free particles which can decrease 
or eliminate the need for scavengers, enzyme protecting agents, or masking 
agents and other such compounds or increase the effectiveness of enzymes 
in the presence of ions. 
SUMMARY OF THE INVENTION 
It has surprisingly been found that a dry dust-free particle can be 
produced which reduces the need for scavengers, protecting agents, or 
masking agents and/or improves the effectiveness of enzymes therein and 
additionally provides a particle with delayed dissolution times. The 
product comprises a particulate material to which has been applied a 
continuous layer of a non-water soluble isophthalic acid polymer or other 
warp size agent, preferably in the presence of a detergent. Particularly 
within the scope of this invention are enzyme and detergent particles 
prepared with a non-water soluble isophthalic acid polymer. In a preferred 
embodiment, a crosslinking agent consisting of a multivalent cation salt, 
such as aluminum sulfate, is incorporated into the particle.

DETAILED DESCRIPTION OF THE INVENTION 
"Warp size" as used herein refers to compositions, in this case isophthalic 
acid polymers, normally used in the textile industry. These agents are 
sprayed on thread during the weaving process to help protect them against 
damage (e.g. by abrasion). Normally the size material is removed by use of 
desizing agents prior to sale of the goods. Many such warp size agents are 
known to be readily dispersible in water, but not soluble, and such are 
ones suitable for the present invention. A preferred isophthalic acid 
polymer and warp size is available commercially as AQ-55 from Eastman 
Chemicals Co. but chemically is poly [82/18-isophthalic 
acid/S-sodiosulfoisophthalic acid-54/46 diethyleneglycol/1,4-cyclohexane 
dimethanol]. Other such agents are known in the prior art and/or could 
easily be synthesized. It has been discovered that where these agents are 
used to coat particles, they offer several advantages over the 
macromolecular films previously used to coat particles. They coat well, 
contain dust, and produce a nonfriable particle. They can be applied at 
high solids concentration from dispersions (typically 10-30% w/w solids, 
which entails reduced coating times), and are stable at high temperature 
and humidity. An important benefit of using these compounds is their 
ability to spread the release of the enzyme contents of the particle over 
about 1-3 minutes after addition to an aqueous detergent environment. This 
is useful when scavengers, protecting agents, etc., such as ammonium 
sulfate, are used which act to sequester or inactivate available chlorine 
or other oxidizing agents or components harmful to enzymes. Such enzyme 
protecting agents are disclosed in U.S. Ser. No. 07/642,619 now abandoned 
filed on even date with this application entitled "GRANULES CONTAINING 
BOTH AN ENZYME AND AN ENZYME PROTECTING AGENT AND DETERGENT COMPOSITIONS 
CONTAINING SUCH GRANULES". The delay in release allows the chlorine or 
other ions to be bound to available substrates other than the enzyme, 
prior to release of the enzyme, thus decreasing the need for scavengers, 
protecting agents, or masking agents. These other substrates, such as the 
proteinaceous stains on clothing and other amino or thiol compounds can 
often be present in the environment where enzyme granules might be used, 
such as a washing machine. Under some conditions the delay in release in 
itself may offer sufficient protection, and no added scavengers or 
protecting agents or masking agents may be needed. For example, in clothes 
washing detergent compositions the detergent and soiled clothing can be 
allowed to react with and bind the available chlorine after which the 
enzyme can be released in a more favorable environment eliminating or 
greatly reducing the need for a scavenger or protecting agent or masking 
agent. 
The term "non-water soluble" means that upon contact with water, the 
polymer does not solubilize (as, for example, in an enteric coating). 
"Delayed release" means that at least a portion of the particulate 
material is released into the surrounding water over a period of time such 
that at least about 90% of the enzyme or other selected component of the 
particulate material coated with the non-water soluble coating is released 
within 7 minutes, more preferably within about 2-4 minutes, but not more 
than 50% is released within 30 seconds. Release of the enzyme and other 
components underneath the polymer coating may take place by either polymer 
erosion, dispersion or diffusion through the polymer (for example, when 
the polymer swells upon contact with water), or by a combination of these 
or other mechanisms. Time of release of the enzyme and other components 
can be further delayed by crosslinking the polymer. Crosslinking is 
carried out by incorporating multivalent cation salts, such as Al.sub.2 
(SO.sub.4).sub.3 or MgSO.sub.4 beneath the polymer coating. Crosslinking 
may actually occur only once the granule is wetted. The degree of 
crosslinking will affect the rate of polymer erosion and enzyme release. 
These coatings are also effective in combination with powdered fillers 
such as TiO.sub.2 or talc. Besides serving as cosmetic whiteners, these 
powdered fillers aid in preventing agglomeration during the coating 
process. 
"Particulate material" refers to relatively small particles in the area of 
150-1500 microns. In a preferred embodiment the particle is a spray-coated 
particle with a soluble or dispersible core to which a spray coating has 
been applied. In the case of a detergent particulate material (a preferred 
particle), such particle would contain a core of a soluble or dispersible 
solid such as non pareil salt crystals to which has applied to it 
detergent, enzyme, scavenger, protecting agent, etc. in one or more coats. 
Coated particles of the present invention can be made in a fluidized-bed 
spray-coater. Typically, such devices comprise a fluidized-bed dryer 
consisting of a cylindrical product chamber that has a porous grid on the 
bottom and is open on the top to be put up against a conical shaped 
expansion chamber of a larger diameter than the cylindrical product 
chamber; a filter to collect dust and a fan to help air flow is placed at 
the far end of the expansion chamber and a spray nozzle is located within 
the chamber to apply the solution to the core material. In operation, as 
the velocity of air passing up through the chamber is increased, a point 
is reached where particles resting on the porous grid are suspended in the 
air flow as a fluid, hence the terms "fluidization" and "fluidized-bed 
dryer". The particles are lifted by the upward force of the air out of the 
product chamber into the expansion chamber where the air expands and the 
upward force per unit of area is reduced. This allows the particles to 
fall back into the product chamber and start the cycle over. 
The initial step in the method involves introducing a particulate, core 
material into the reaction chamber of the fluidized-bed dryer and 
suspending the particles therein on a stream of air. The core particles 
preferably are composed of a highly hydratable material, i.e. a material 
which is readily dispersible or soluble in water. The core material should 
either disperse (fall apart by failure to maintain its integrity) or 
dissolve by going into a true solution. Clays (bentonite, kaolin), non 
pareils and agglomerated potato starch are considered dispersible. Non 
pareils are spherical particles consisting of a solid sugar core that has 
been built up and rounded into a spherical shape by binding layers of 
sugar, starch and possibly other materials to the core in a rotating 
spherical container and are preferred. 
Salt particles (NaCl crystals, NaCl rock salt, NaHCO.sub.3) are considered 
soluble particles useful in the invention. More particularly, core 
particles can be non pareils with or without a final coat of dextrin or a 
confectionery glaze. Also suitable are agglomerated trisodium citrate, pan 
crystallized NaCl flakes, bentonite granules and prills, 
bentonite/kaolin/diatomaceous earth disk-pelletized granules and sodium 
citrate crystals. The core particle is of a material which is not 
dissolved during the subsequent spraying process and is preferably of a 
particle size from 150 to 2,000 microns (100 mesh to 10 mesh on the U.S. 
Standard Sieve Series) in its longest dimension. 
Enzymes and other agents, including any optional metallic salts, pigments, 
solubilizers, activators, antioxidants, dyes, inhibitors, binders, 
plasticizers, fragrances, etc. are applied to the surface of the 
particulate material by fluidizing the particles in a flow of air 
whereupon a broth containing the enzyme and other solutes or suspended 
material is then atomized and sprayed into the expansion chamber of the 
spray-coater. The atomized droplets contact the surface of the particles 
leaving a film of the solids adhering to the surface of the particles when 
the water and other volatiles are evaporated. 
Airflow is maintained upwards and out the top of the expansion chamber 
through a filter. The filter may be located inside or outside of the unit, 
or may be substituted for by a scrubber or cyclone. This filter or 
scrubber or cyclone traps fine dried particles which contribute to dust. 
Fluidized-bed spray-coaters that have this filter typically have automatic 
shakers which shake the filter to prevent excessive restriction of the air 
flow. 
When sufficient enzyme or other solids are applied to the core particles to 
provide the desired size particles, while still suspended in the reaction 
chamber of the coater or later reintroduced therein, the particles are 
coated with a layer of the isophthalic acid polymer of the invention with 
the scavenger or other desired ingredient and optional fillers. 
Optionally, a solution or suspension containing a crosslinking agent, 
typically a multivalent cation salt, can be sprayed onto the particulate 
material prior to applying the isophtalic acid polymer. (Actually, 
crosslinking may not occur until the particle is subsequently wetted and 
the crosslinking agent can diffuse into the polymer layer.) This is 
accomplished in a manner similar to that used for application of the 
enzyme/solids coating. The isophthalic acid polymer should be roughly 
1-15% w/w of the entire particle and roughly 10-100% of the final coating. 
The dust-free enzyme particles containing enzymes of the present invention 
can be used wherever enzymes or other agents are needed in a dry form. 
Thus, they can be used as additives to dry detergent formulations, for 
removing gelatin coatings on photographic films, to aid in silver 
recovery, in the digestion of wastes from food processing plants for 
nitrogen recovery, in denture cleansers for removing protein bound stains 
in food preparation, in textile applications such as desizing and a 
processing aid in waste water treatment. In general, they can be used 
anywhere it is desirable to delay the release of an enzyme or other agent. 
The following outlines ingredients, other than enzymes, which could be 
present in the coated particulate material: 
ENZYME PROTECTING AGENTS AND SCAVENGERS 
The enzyme protecting agents employed herein refer to those compounds 
which, when incorporated in the granules at a sufficient concentration, 
will prevent significant loss of enzyme activity over time when these 
granules are added to a detergent wash medium. Suitable enzyme protecting 
agents include 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. 
The concentration of the enzyme protecting agent employed in combination 
with the enzyme in the granule is an amount effective to retard the loss 
of enzymatic activity in the detergent wash medium, i.e., provide 
resistance to enzymatic activity degradation in the detergent wash medium. 
It is believed that oxidizing moieties in the detergent wash medium are 
responsible for oxidizing the amine, ammonium and sulhydryl 
functionalities of amine, ammonium and/or sulhydryl containing amino acids 
in the enzyme and that this oxidation accounts for at least part of the 
loss of enzymatic activity. It is further believed that enzyme protecting 
agents containing functional groups such as --NH.sub.3, --NH.sub.4.sup.+, 
--SH and the like protect the enzyme from enzymatic activity degradation 
by offering alternative sites for oxidation by the oxidizing moieties. 
That is to say that the presence of a large number of these 
functionalities in the detergent wash medium will result in enzyme 
protection because, by sheer number of such functionalities, oxidizing 
agents present in the wash medium will preferentially oxidize these 
functionalities rather than oxidizing oxidizable functionalities on the 
enzyme. Accordingly, such functional groups are described herein as enzyme 
protecting functional groups. 
It is believed that normally an initially very high concentration of the 
enzyme protecting agent in the microenvironment of the enzyme prevents any 
significant oxidation of the enzyme by those oxidizing groups found in the 
detergent wash medium. In contrast, if the enzyme and enzyme protecting 
agent are merely combined into the detergent composition as separate 
components, this high concentration of enzyme protection agent in the 
microenvironment of the enzyme cannot form and accordingly, significantly 
less protection is accorded to the enzyme. Whereas in the present 
invention, the coating allows for a reduction in the amount of protecting 
agent needed. 
In view of the above, the concentration of the enzyme protecting agent 
necessary to impart protection to the enzyme in the detergent wash medium 
is related to the number of enzyme protecting functional groups present on 
the protecting agent molecule, and to the delay in release of enzyme, and 
to the agent being protected against. 
In general, the concentration of the enzyme protecting agent employed is an 
amount effective to retard the loss of enzymatic activity of the enzyme in 
the wash medium. Preferably, the enzyme protecting agent is selected so as 
to provide at least about 1.0 micromols/liter of the enzyme protecting 
functional groups in the detergent wash medium. More preferably, the 
concentration of the enzyme protecting agent is selected so as to provide 
at least about 5 micromols of enzyme protecting functional groups per 
liter of detergent wash medium, and even more preferably, at least about 
10 micromols of enzyme protecting functional groups per liter of detergent 
wash medium. 
While the enzyme protecting agents employed herein include some of the same 
components heretofore employed as chlorine scavengers, the amount of 
concentration of enzyme protecting agent which imparts improved resistance 
to loss of enzyme activity in the detergent wash medium is preferably 
greater than that required to scavenge chlorine. That is to say that such 
use is an improvement over such previous uses of chlorine scavengers 
insofar that when used at a higher concentration in the detergent wash 
medium, these scavengers additionally remove other oxidizing moieties 
which thereby improves the enzymatic activity degradation resistance in 
the detergent wash medium. 
SURFACTANTS 
Suitable anionic surfactants for use in the detergent composition of this 
invention include linear or branched alkylbenzenesulfonates; alkyl or 
alkenyl ether sulfates having linear or branched alkyl groups or alkenyl 
groups; alkyl or alkenyl sulfates; olefinsulfonates; alkanesulfonates and 
the like. Suitable counter ions for anionic surfactants include alkali 
metal ions such as sodium and potassium; alkaline earth metal ions such as 
calcium and magnesium; ammonium ion; and lakanolamines having 1 to 3 
alkanol groups of carbon number 2 or 3. 
Ampholytic surfactants include quaternary ammonium salt sulfonates, 
betaine-type ampholytic surfactants, and the like. Such ampholytic 
surfactants have both the positive and negative charged groups in the same 
molecule. 
Nonionic surfactants generally comprise polyoxyalkylene ethers, as well as 
higher fatty acid alkanolamides or alkylene oxide adduct thereof, fatty 
acid glycerine monoesters, and the like. 
Suitable surfactants for use in this invention are disclosed in British 
Patent Application No. 2 094 826A, the disclosure of which is incorporated 
herein by reference. 
The surfactant is generally employed in the detergent compositions of this 
invention in a cleaning effective amount. Preferably, the surfactant is 
employed in an amount from about 1 weight percent to about 95 weight 
percent of the total detergent composition and more preferably from about 
5 weight percent to about 45 weight percent of the total detergent 
composition. 
In addition to the enzyme, and the coating, the detergent compositions of 
this invention can additionally contain the following components: 
CATIONIC SURFACTANTS AND LONG-CHAIN FATTY ACID SALTS 
Such cationic surfactants and long-chain fatty acid salts include saturated 
or unsaturated fatty acid salts, alkyl or alkenyl ether carboxylic acid 
salts, .alpha.-sulfofatty acid salts or esters, amino acid-type 
surfactants, phosphate ester surfactants, quaternary ammonium salts 
including those having 3 to 4 alkyl substituents and up to 1 phenyl 
substituted alkyl substituents. Suitable cationic surfactants and 
long-chain fatty acid salts are disclosed in British Patent Application 
No. 2 094 826 A, the disclosure of which is incorporated herein by 
reference. The composition may contain from about 1 to about 20 weight 
percent of such cationic surfactants and long-chain fatty acid salts. 
BUILDERS 
A. Divalent sequestering agents. 
The detergent composition may contain from about 0 to about 50 weight 
percent of one or more builder components selected from the group 
consisting of alkali metal salts and alkanolamine salts of the following 
compounds: phosphates, phosphonates, phosphonocarboxylates, salts of amino 
acids, aminopolyacetates high molecular elecrolytes, non-dissociating 
polymers, salts of dicarboxylic acids, and aluminosilicate salts. Suitable 
divalent sequestering agents are disclosed in British Patent Application 
No. 2 094 826 A, the disclosure of which is incorporated herein by 
reference. 
B. Alkalis or inorganic electrolytes 
The detergent composition may contain from about 1 to about 50 weight 
percent, preferably from about 5 to about 30 weight percent, based on the 
composition of one or more alkali metal salts of the following compounds 
as the alkalis or inorganic electrolytes: silicates, carbonates and 
sulfates as well as organic alkalis such as triethanolamine, 
diethanolamine, monoethanolamine and triisopropanolamine. 
ANTIREDEPOSITION AGENTS 
The detergent composition may contain from about 0.1 to about 5 weight 
percent of one or more of the following compounds as antiredeposition 
agents: polyethylene glycol, polyvinyl alcohol, polyvinylpyrrolidone and 
carboxymethylcellulose. 
Among them, a combination of carboxymethyl-cellulose or/and polyethylene 
glycol with the cellulase composition of the present invention provides 
for an especially useful dirt removing composition. 
For removing the decomposition of carboxymethyl-cellulose by the cellulase 
in the detergent, it is desirable that carboxymethylcellulose is 
granulated or coated before the incorporation in the composition. 
BLEACHING AGENTS 
The use of certain enzymes, e.g., cellulase, in combination with a 
bleaching agent such as sodium percarbonate, sodium perborate, sodium 
sulfate/hydrogen peroxide adduct and sodium chloride/hydrogen peroxide 
adduct or/and a photosensitive bleaching dye such as zinc or aluminum salt 
of sulfonated phthalocyanine further improves the deterging effects. 
BLUING AGENTS AND FLUORESCENT DYES 
Various bluing agents and fluorescent dyes may be incorporated in the 
composition, if necessary. Suitable bluing agents and fluorescent dyes are 
disclosed in British Patent Application No. 2 094 826 A, the disclosure of 
which is incorporated herein by reference. 
CAKING INHIBITORS 
The following caking inhibitors may be incorporated in the powdery 
detergent: p-toluenesulfonic acid salts, xylenesulfonic acid salts, acetic 
acid salts, sulfosuccinic acid salts, talc, finely pulverized silica, 
clay, calcium silicate (such as Micro-Cell of Johns Manville Co.), calcium 
carbonate and magnesium oxide. 
MASKING AGENTS FOR FACTORS INHIBITING THE CELLULASE ACTIVITY 
Certain enzymes, e.g., cellulase are deactivated in some cases in the 
presence of copper, zinc, chromium, mercury, lead, manganese or silver 
ions or their compounds. Various metal chelating agents and 
metal-precipitating agents are effective against these inhibitors. They 
include, for example, divalent metal ion sequestering agents as listed in 
the above item with reference to optional additives as well as magnesium 
silicate and magnesium sulfate. 
In regard to the enzymes, certain components can act as inhibitors. For 
example, with cellulase, it is known that cellobiose, glucose and 
gluconolactone act sometimes as the inhibitors. It is preferred to avoid 
the co-presence of these inhibitors with the enzyme as far as possible. In 
the event that co-presence is unavoidable, it is necessary to avoid the 
direct contact of the inhibitors with the enzyme by, for example, coating 
them. 
Long-chain-fatty acid salts and cationic surfactants can act as the 
inhibitors of some enzymes, e.g., cellulase, in some cases. However, the 
co-presence of these substances with the enzyme is allowable if the direct 
contact of them is prevented by some means such as tableting or coating. 
The above-mentioned masking agents and methods may be employed, if 
necessary, in the present invention. 
ENZYME-ACTIVATORS 
Certain enzymes, e.g. cellulase, are known to be activated by the presence 
of materials referred to as activators. For cellulase, the activators vary 
depending on variety of the cellulases. In the presence of proteins, 
cobalt and its salts, magnesium and its salts, and calcium and its salts, 
potassium and its salts, sodium and its salts or monosaccharides such as 
mannose and xylose, the cellulases are activated and their deterging 
powers are improved remarkably. 
ANTIOXIDANTS 
The antioxidants include, for example, tert-butyl-hydroxytoluene, 
4,4'-butylidenebis(6-tert-butyl-3-methylphenol), 
2,2'-butylidenebis(6-tert-butyl-4-methylphenol), monostyrenated cresol, 
distyrenated cresol, monostyrenated phenol, distyrenated phenol and 
1,1-bis(4-hydroxy-phenyl)cyclohexane. 
SOLUBILIZERS 
The solubilizers include, for example, lower alcohols such as ethanol, 
benzensulfonate salts, lower alkylbenzensulfonate salts such as 
p-toluenesulfonate salts, glycols such as propylene glycol, 
acetylbenzenesulfonate salts, acetamides, pyridinedicarboxylic acid 
amides, benzoate salts and urea. 
The detergent composition of the present invention can be used in a broad 
pH range of from acidic to alkaline pH. Preferably, the detergent 
composition is employed in a neutral/alkaline pH and more preferably in a 
neutral/alkaline pH of from pH 7 to 10. 
Aside from the above ingredients, perfumes, buffers, preservatives, dyes 
and the like can be used, if desired, with the detergent compositions of 
this invention. 
When the detergent composition is added to an aqueous solution so as to 
produce a cleaning effective concentration of a surface active agent, the 
resulting aqueous solution is sometimes referred to herein as a "detergent 
wash medium". 
When a detergent base used in the present invention is in the form of a 
powder, it may be one which is prepared by any known preparation methods 
including a spray-drying method and a granulation method. The detergent 
base obtained particularly by the spray-drying method and/or spray-drying 
granulation method are preferred. The detergent base obtained by the 
spray-drying method is not restricted with respect to preparation 
conditions. The detergent base obtained by the spray-drying method is 
hollow granules which are obtained by spraying an aqueous slurry of 
heat-resistant ingredients, such as surface active agents and builders, 
into a hot space. The granules have a size of from 50 to 2000 micrometers. 
After the spray-drying, perfumes, enzymes, bleaching agents, inorganic 
alkaline builders may be added. With a highly dense, granular detergent 
base obtained such as by the spray-drying-granulation method, various 
ingredients may also be added after the preparation of the base. 
The following examples are representative and not intended to be limiting. 
One skilled in the art could choose other enzymes, cores, particles, 
methods and coating agents based on the proportions and ingredients taught 
herein. 
The following examples were prepared using techniques similar to those 
described in co-pending U.S. application Ser. No. 07/429,881 incorporated 
herein by reference as a spray-coating. The following example procedure 
used for all the examples. 
EXAMPLE 1 
A Uni-Glatt laboratory fluidized-bed spray-coater was charged with 1210 
grams of non pareils cores or seeds having a diameter of 425 to 850 
microns. A 1.05 liter aqueous cellulase concentrate (cellulase available 
as Cytolase 123 from Genencor International, 180 Kimball Way, South San 
Francisco, Calif. 94080) containing 170 grams/liter protein and 25% total 
solids was sprayed onto the fluidized cores at a spray rate of about 10 
ml/min with an inlet temperature of 45.degree. to 62.degree. C. and an 
outlet temperature of 38.degree. to 46.degree. C. At the end of the enzyme 
application, 1466 grams of granules were recovered, representing a 21.2% 
weight gain over the non pareil core. The resulting granules were screened 
to provide granules between 425 and 1180 microns, a total of 1411 grams. 
The recovery of protein in the 425 and 1180 microns granules was 87.0% of 
the protein occurring in the cellulase concentrate applied. The protein 
content of these granules was determined to be 110 grams/kilogram. These 
granules are hereinafter referred to as "Granule A". 
Granule A (706 grams) was then charged into a Uni-Glatt 
fluidized-bed-spray-coater and coated with 37 grams of ammonium sulfate 
dissolved in 100 mls final volume of deionized water. The ammonium sulfate 
solution was sprayed onto the fluidized granules at around 10 mls/min with 
an inlet temperature of 50.degree. to 60.degree. C. and an outlet 
temperature of 40.degree. to 45.degree. C. Subsequently, a solution 
containing 15% AQ-55 polymer solids and 15% suspended titanium dioxide was 
spray-coated onto the granule in a similar fashion, and enough was applied 
to result in 4% net dry weight percentage of each TiO.sub.2 and AQ-55. 
These granules were screened to provide granules between 425 and 1180 
microns, a total of 727 grams. The recovery of protein in the granules 
between 425 to 1180 microns was 98.1% of the protein occurring in the 
Granule A material charged into the fluidizied-bed spray-coater. The 
protein content of these granules was determined to be 105 grams/kilogram. 
These granules are hereinafter referred to as "Granule B". 
A fully formulated commercially available powdered laundry detergent was 
separately formulated into two separate compositions. The first 
composition contained a sufficient amount of Granule A so as to provide 
0.1 weight percent of cellulase (hereinafter "Composition A"); whereas the 
second composition contained a sufficient amount of Granule B so as to 
provide the same weight percent of cellulase (hereinafter "Composition 
B"). The same amount of Composition A and Composition B were added to 
separate washing machines each of which contained 17 gallons of water at 
37.degree. C. Immediately after addition, a 20 ml aliquot of each solution 
was withdrawn and the enzymatic activity was measured, i.e., the zero 
point measurement. Additional aliquots were withdrawn at 3 minute 
intervals and the activity was measured for these samples as well. 
EXAMPLE 2 
The following results were achieved by varying the general amounts of 
coating and protecting agents. 
By a similar method to that described in Example 1, a series of samples of 
spray-coated subtilisin were produced incorporating varying levels of 
ammonium sulfate and AQ-55 polymer. In all samples, the following 
procedure was approximately constant: A Uni-Glatt laboratory fluidized-bed 
spray-coater was charged with 600 and 950 grams of non pareil seeds having 
a diameter of 425 to 850 microns. The weight of non pareils was varied 
based on the desired target concentrations of ammonium sulfate and AQ-55 
polymer to be added, in order to achieve an approximately constant final 
product weight and enzyme concentration. An enzyme concentrate containing 
from 10 to 20% w/v total solids and a subtilisin concentration of from 1.0 
to 3.0% w/v was sprayed onto the fluidized seeds at a rate of about 10 
ml/min and an atomization air pressure of 3.5 bar, with an inlet 
temperature of 45.degree. C. to 62.degree. C. and an outlet temperature of 
34.degree. C. to 48.degree. C. Enough of an aqueous solution of ammonium 
sulfate at a 40% w/v concentration was sprayed on to provide the net dry 
weight percentage indicated in the table below for each sample. An aqueous 
suspension was prepared containing 15% AQ-55 polymer solids and 15% 
suspended titanium dioxide, and enough was applied to provide the net dry 
weight percentage of AQ-55 indicated in Table 1 (i.e., titanium dioxide is 
present at an equal proportion as the polymer). Final produce, at 
approximately 1000 to 1100 grams weight, was harvested from the fluidized 
bed, and screened between 16 and 50 mesh screens to remove fines and 
agglomerates. 
The ten samples prepared had polymer and ammonium sulfate compositions 
indicated by the non-empty cells in Table 1. (The combinations represented 
by the empty cells were not produced or tested). These samples were then 
tested for wash performance in washing machines, using a proprietary 
detergent in a 12 minute cycle at 95.degree. F. Standard stain swatches 
were evaluated for cleaning benefit by single-blind subjective tests and 
assigned a relative rating. In the following table, performance ratings 
are scaled between 0.0 and 2.0, with a higher rating representing a 
subjectively cleaner swatch. 
TABLE 1 
______________________________________ 
Cleaning Performance of Detergent Protease 
Granules Coated the Ammonium Sulfate and AQ-55 Polymer 
Percent Percent Ammonium Sulfate 
AQ-55 Polymer 0 5 10 15 
______________________________________ 
0 0.3 
2 0.7 1.2 
3 1.6 
4 0.5 1.0 1.5 1.8 
6 1.2 1.5 
______________________________________ 
The swatch cleaning ratings on Table 1 indicate an additive performance 
benefit for combinations of increased polymer levels and increased 
ammonium sulfate levels. Thus, it is apparent that good cleaning 
performance can be maintained at low levels of chlorine scavenger by 
compensating with increased levels of AQ-55 polymer.