WO1991006227A1 - Enduits comestibles a base de proteines - Google Patents

Enduits comestibles a base de proteines Download PDF

Info

Publication number
WO1991006227A1
WO1991006227A1 PCT/US1990/006441 US9006441W WO9106227A1 WO 1991006227 A1 WO1991006227 A1 WO 1991006227A1 US 9006441 W US9006441 W US 9006441W WO 9106227 A1 WO9106227 A1 WO 9106227A1
Authority
WO
WIPO (PCT)
Prior art keywords
prolamine
latex
zein
film
group
Prior art date
Application number
PCT/US1990/006441
Other languages
English (en)
Inventor
Stephen G. Haralampu
Stephen Sands
Akiva Gross
Original Assignee
Opta Food Ingredients, Inc.
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Opta Food Ingredients, Inc. filed Critical Opta Food Ingredients, Inc.
Publication of WO1991006227A1 publication Critical patent/WO1991006227A1/fr

Links

Classifications

    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K9/00—Medicinal preparations characterised by special physical form
    • A61K9/20—Pills, tablets, discs, rods
    • A61K9/28—Dragees; Coated pills or tablets, e.g. with film or compression coating
    • A61K9/2806—Coating materials
    • A61K9/2833—Organic macromolecular compounds
    • A61K9/2873—Proteins, e.g. gelatin
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23G—COCOA; COCOA PRODUCTS, e.g. CHOCOLATE; SUBSTITUTES FOR COCOA OR COCOA PRODUCTS; CONFECTIONERY; CHEWING GUM; ICE-CREAM; PREPARATION THEREOF
    • A23G3/00—Sweetmeats; Confectionery; Marzipan; Coated or filled products
    • A23G3/34—Sweetmeats, confectionery or marzipan; Processes for the preparation thereof
    • A23G3/343—Products for covering, coating, finishing, decorating
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K40/00—Shaping or working-up of animal feeding-stuffs
    • A23K40/30—Shaping or working-up of animal feeding-stuffs by encapsulating; by coating
    • A23K40/35—Making capsules specially adapted for ruminants
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23P—SHAPING OR WORKING OF FOODSTUFFS, NOT FULLY COVERED BY A SINGLE OTHER SUBCLASS
    • A23P20/00—Coating of foodstuffs; Coatings therefor; Making laminated, multi-layered, stuffed or hollow foodstuffs
    • A23P20/10—Coating with edible coatings, e.g. with oils or fats
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23G—COCOA; COCOA PRODUCTS, e.g. CHOCOLATE; SUBSTITUTES FOR COCOA OR COCOA PRODUCTS; CONFECTIONERY; CHEWING GUM; ICE-CREAM; PREPARATION THEREOF
    • A23G2200/00—COCOA; COCOA PRODUCTS, e.g. CHOCOLATE; SUBSTITUTES FOR COCOA OR COCOA PRODUCTS; CONFECTIONERY; CHEWING GUM; ICE-CREAM; PREPARATION THEREOF containing organic compounds, e.g. synthetic flavouring agents
    • A23G2200/10—COCOA; COCOA PRODUCTS, e.g. CHOCOLATE; SUBSTITUTES FOR COCOA OR COCOA PRODUCTS; CONFECTIONERY; CHEWING GUM; ICE-CREAM; PREPARATION THEREOF containing organic compounds, e.g. synthetic flavouring agents containing amino-acids, proteins, e.g. gelatine, peptides, polypeptides

Definitions

  • Edible coatings are used in foods to minimize the migration of components within the food system or between the food and its surrounding environment. For example, such coatings prevent the diffusion of water, fats and/or oxygen into, out of, or within the food system. Of these, reducing moisture migration is the most important requirement in most cases. A change in either direction of moisture levels or water activity does not have to be very large to be very detrimental for the food quality. Moisture loss or uptake in a food can have dramatic effects on the texture, stability or yield of the food product. Moisture uptake can reduce or
  • Oxygen uptake by a food often results in deleterious reactions which affect its flavor, nutritional quality and acceptability.
  • the, migration of water or lipids within the food itself may have a detrimental effect on the perceived quality.
  • coatings may reduce the migration of a processing aid, i.e., fat, into the food.
  • barriers may be used to minimize the migration or loss of other additives, such as colors, flavors, preservatives, antioxidants, etc..
  • Edible coatings also can be used to impart structural integrity to the surface of a food, making it less susceptible to mechanical damage.
  • Kester and Fennema (“Edible Films and Coatings: a Review," Food Technology, (1986), 40(12):47-59) reviewed the use of edible films and coatings, and the current state-of-the-art coating compositions. The most common edible barrier materials, in the category of those which would not be readily
  • polysaccharides e.g., alginate, pectin, carrageenan, starch, starch hydrolysates and cellulose derivatives
  • lipids e.g., acetylated monoglycerides, natural waxes and surfactants
  • proteins e.g., gelatin, casein, serum albumin, ovalbumin, wheat gluten and zein, plus combinations of these.
  • shellac Another common edible barrier not encompassed in the above catagories is shellac. Films containing wheat gluten, which contains the wheat prolamine gliadin, and films containing zein have only received limited attention as edible coatings. Of the protein-based films, zein films have been found to possess relatively good water-barrier properties. (Guilbert,
  • Non-edible films based on prolamines have been described. Hansen (U.S. Patent 2,047,961) describes a non-edible prolamine-based film which is formed by reacting the protein in an aqueous-alcoholic
  • Veatch (U.S. Patent 2,194,337) also describes a non-edible zein film with improved grease resistance by
  • Patent 2,311,485 Sturken introduces the use of s orb itol and tr iethanolamine as plas ticiz ers for non-edible zein films deposited by evaporation from an ethanol solution.
  • Evans and Manley U.S. Patent 2,437,946 report that lactamides are excellent plasticizers for prolamine films, and that these may be hardened by reaction with an aldehyde.
  • U.S. Patent 2,285,758 Sturken discloses a process for treating a zein film to give it water resistance. In this process, a zein film is brought into direct contact with steam.
  • Solvent-based coating compositions containing zein in solution with relatively large amounts of water have a tendency to gel on standing.
  • Coleman U.S. Patent 2,185,123
  • an auxiliary solvent which is a lacquer solvent or a lacquer plasticizer, has been added.
  • Coleman further describes a substantially non-aqueous coating composition which resists gelation, wherein zein is dissolved in alcohol containing not more than 5% water.
  • Evans and Manley Stabilizing Zein Dispersions against Gelation," Industrial and
  • Meigs describes a derivatization of zein in which the zein is reacted together with formaldehyde and a secondary dialkyl- amine having less than nine carbon atoms.
  • the zein derivative is soluble in dilute aqueous acids and may be used in non-edible coating compositions.
  • James uses surfactants to disperse the zein in a predominantly aqueous phase.
  • Anker, Foster and Loader disclose a coating formulation for foods comprised of wheat gluten, and optionally zein or soy protein isolate, dispersed in an alkaline, aqueous alcohol and plasticized with glycerol.
  • zein provides a glossy surface
  • zein possessing both good lipid and moisture barrier protection.
  • the use of zein has been limited to the nut and confection industry, however, due to the need for organic solvents and/or extreme pH's.
  • the present invention relates to a method for providing a barrier to gases, water, water vapor and oil in a substrate by coating the substrate with a prolamine film.
  • the method involves applying a water-based prolamine latex which is substantially free of organic solvent to the substrate, which forms an edible coating or barrier on the substrate.
  • the water-based prolamine latex forms a continuous durable film when deposited on a surface and dried.
  • the properties of the coating or barrier can be modified with various additives to the latex, e.g., to increase its flexibility or barrier properties.
  • Edible coatings produced by the present method are clear films which are non-toxic since they are formed from a naturally-occurring, common food protein.
  • the present water-borne prolamine latex does not contain organic solvents or require extremepH's, thus, the residues of these undesirable elements are minimized or eliminated.
  • the prolamine films have excellent resistance to moisture, lipid and gas permeation.
  • Figure 1 is a graph illustrating the resistance of zein latex films measured at a transmembrane water vapor pressure of 0.79 psi and for a film area of 31 cm 2 .
  • Figure 2 is a graph illustrating the resistance of zein latex films measured at a transmembrane water vapor pressure of 0.34 psi and for a film area of 31 cm 2 .
  • Figure 3 is a graph comparing the permeability to water of zein latex films cured at 45°C and 105°C with coatings cast from a zein solution, beeswax, and agar-agar.
  • Figure 4 is a graph comparing the permeability to oil of a zein latex film cured at 105°C with films cast from agar-agar and a zein solution.
  • the present invention relates to a method of forming an edible barrier using an aqueous protein latex containing a prolamine suspended in an aqueous medium which is substantially free of organic solvent.
  • the prolamine coating provides a barrier to gases (such as oxygen) water, water vapor and oil.
  • gases such as oxygen
  • latex means a suspension of water-insoluble particles having a median volume diameter of about 20 microns or less in an aqueous medium.
  • aqueous medium refers to water or a water-based solution which medium contains at least 60% by weight water.
  • the prolamine latices used in the present method can be made by dissolving the prolamine in a solvent, such as ethanol, and combining the
  • prolamine solution with an aqueous medium under mixing conditions.
  • Prolamines are not soluble in the water-rich mixture, and precipitate, thereby forming a latex.
  • Substantially spherical particles are produced by this method. Prolamine latices and methods for making them are described in detail in co-pending U.S. patent application Serial No.
  • the resulting latex can then be treated, e.g., by evaporation or diafiltration, to reduce the amount of prolamine solvent.
  • prolamine latex is substantially free of organic solvent, that is, contains none or only trace amounts (e.g., less than 1% by weight) of organic solvent.
  • trace amounts e.g., less than 1% by weight
  • Another method of forming the aqueous prolamine latex is to mill the prolamine to a fine particle size (e.g., less than about 50 microns) and to disperse them in an aqueous medium using a fine particle size (e.g., less than about 50 microns) and to disperse them in an aqueous medium using a fine particle size (e.g., less than about 50 microns) and to disperse them in an aqueous medium using a
  • particles having an average particle size of less than about 15 microns are preferred.
  • prolamines insolubility in water and solubility in aqueous alcohol (e.g., aqueous solutions of alcohol containing at least 40% alcohol), and by the presence in the protein of large amounts of hydrophobic amino acids, such as proline, glutamine and asparagine.
  • aqueous alcohol e.g., aqueous solutions of alcohol containing at least 40% alcohol
  • hydrophobic amino acids such as proline, glutamine and asparagine.
  • prolamines are found in high concentrations in various grains, such as corn, wheat, barley, rice and sorghum, and in other plants and animal sources.
  • Representative prolamines include, for example, zein, hordein, gliadin and kafirin.
  • the preferred prolamine for use in the present method is the alcohol-soluble protein-fraction of corn (Zea mays), named zein.
  • the potential yield of zein is about one pound per bushel of corn.
  • Zein can be readily obtained from corn gluten, which is a by-product of the corn wet milling industry. Both commercially available grades, with associated impurities, and purified forms of zein can be used.
  • the concentration of prolamine particles in suspensions made by the precipitation process described is generally up to about 5% by weight.
  • the suspension may be further concentrated to up to about 40% by weight, by ultrafiltration, evaporation or other appropriate technique, or reduced to a dry powder, using standard techniques such as flash drying, lyophilization or spray drying.
  • ultrafiltration using membranes having a cut-off of 300,000 NMWL (nominal molecular weight limit) or less is a preferred method of
  • the concentrated protein can be diafiltered to reduce the amount of residual
  • the diafiltration can be done continuously by staged addition of water or in a batch mode by constant volume batch diafiltration.
  • the concentrated suspension can, optionally, be dried to a powder. This can be accomplished by placing the suspension in a lyophilizer at an appropriate temperature (e.g., room temperature), at a pressure of less than about 100 millitorr (mtorr) until the water and other volatiles have been evaporated (to about 1-10% moisture content), and a fine powder remains.
  • Alternative forms of drying such as flash drying, fluid-bed drying, spray drying or vacuum drying can be used. This powder can then be stored and handled without refrigeration or other special handling procedures. Rehydration can be accomplished by adding the powder to water, or an aqueous medium, with agitation sufficient to
  • a suspension having a protein:water ratio of about 0.10 to about 0.25 by weight is preferred.
  • a suspension of prolamine in a predominantly aqueous medium can be made by milling the protein and mechanically
  • the protein may be milled to a fine particle size of preferably less than about 20 microns, and more preferably less than about 15 microns in an appropriate apparatus, e.g., a pin mill, or fluid energy mill optionally using a particle size classification device, such as a cyclone separator, to isolate the ultrafine particles.
  • the milled protein may be suspended in the aqueous medium in a manner similar to the rehydration of the dehydrated latex
  • suspension may be made by adding the milled protein to water, or an aqueous medium, with agitation sufficient to individualize and suspend the
  • Additives in the aqueous medium may be used to enhance the properties of the suspension, and/or the resultant film.
  • the properties of the suspension can be modified for a given application, for example, by chemically and/or enzymatically altering the
  • the functionality, surface properties and molecular weight distribution of the protein can be modified by hydrolysis with proteases, such as papain or chymotrypsin, to yield peptides having similar solubility characteristics as the untreated protein.
  • Enzymatic hydrolysis can be carried out prior to making the suspension. The degree of hydrolysis can be controlled by varying the amount of enzyme used, the temperature of the reaction mixture or the reaction time during which the protein is exposed to the enzyme.
  • Enzymatic hydrolysis of zein in 90% ethanol using a protease e.g., papain or chymotrypsin
  • Unmodified zein has a dimer molecular weight of about 38,000 daltons. More importantly, the hydrolysate retains the solubility characteristics of the protein, i.e., the polypeptides are still insoluble in water but soluble in aqueous alcohol having at least 60% alcohol.
  • the properties of the product can be influenced by chemical modification of the proteins.
  • modifications can include, for example, treating the proteins with an acid, base or other agent which alters the structure of one or more of the amino acid side chains, which, in turn, alters the
  • the high glutamine and asparagine content of prolamines, particularly zein provides a means for manipulating the charge characteristics of the protein by
  • the preferred deamidation method involves mild acid-catalyzed deamidation (at a pH of about 1) at elevated temperatures (e.g., 25-65°C) for a period of time sufficient to accomplish the desired level of deamidation.
  • the deamidation process may be followed by measuring the release of ammonia with an ammonia electrode.
  • Deamidation is controllable, and may be terminated by the addition of ammonium carbonate or other base.
  • Other examples of chemical modification include esterification of the protein with fatty alcohols, or acylation of the protein with fatty anhydrides.
  • Additives can be used to enhance certain properties of the films, such as the film barrier properties, film mechanical properties (e.g., tensile strength and flexibility), and to improve the flow and fusing of the latex particles to form a continuous film from the suspension.
  • waxes e.g., beeswax, carnauba wax, or paraffin wax
  • oils and/or surfactants e.g., acetylated glycerides, or diacetyl tartaric acid esters of mono- and di-glycerides (DATEM esters)
  • DATEM esters diacetyl tartaric acid esters of mono- and di-glycerides
  • Composite film structures with complex properties can be formed by using other polymeric or film-forming additives, such as other proteins (e.g., gelatin or casein), hydrocolloids (e.g., gum arabic, carrageenan or xanthan) or synthetic polymers (e.g., polyethylene glycol).
  • proteins e.g., gelatin or casein
  • hydrocolloids e.g., gum arabic, carrageenan or xanthan
  • synthetic polymers e.g., polyethylene glycol
  • Flavors, colors, anti-oxidants and/or preservatives can also add useful function to the films.
  • Additives which are soluble in water can be any suitable additive that are soluble in water.
  • Additives which are insoluble in water may be dispersed by surfactants and added as an emulsion or latex, or incorporated in the zein microparticles during the precipitation process.
  • Water insoluble additives can be incorporated in the microparticles by dissolving or dispersing the additive in the alcoholic prolamine solution prior to the precipitation process in which the latex is formed.
  • the additive when incorporated in the prolamine microspheres, can be either evenly distributed throughout the sphere, in the center of the sphere or on the surface of the sphere,
  • the additive may form microspheres or droplets separate from the protein microspheres.
  • the properties of the prolamine can be enhanced by crosslinking the prolamine prior to forming the latex by the addition of an enzyme which catalyzes intra- and/or intermolecular crosslinking of the protein, such as transglutaminase, or protein disulfide isomerase.
  • an enzyme which catalyzes intra- and/or intermolecular crosslinking of the protein such as transglutaminase, or protein disulfide isomerase.
  • Transglutaminase and protein disulfide isomerase cause inter- and intramolecular crosslinking of the protein through glutamine and cysteine, respectively.
  • Transglutaminase catalyzes an acyl transfer reaction, in which the amide group of the amino acid glutamine is the acyl donor.
  • the present prolamine based suspensions can be used in various applications in the food and pharmaceutical industries, including as edible coatings or barriers in foods or for drugs, e.g., for tablets, such as aspirin.
  • the coating should impart neither significant flavor nor color, so that it does not substantially alter the flavor or appearance of the food or the drug product.
  • Some commercial preparations of prolamines may impart a yellow color to the protein suspension or may have an objectionable odor and/or flavor.
  • the proteins may be decolorized and/or deflavored. Decolorizing can be done prior to making the suspension. Decolorizing can be accompushed by known techniques for removing selected substances, such as extraction with organic solvents (e.g., acetone, hexane or methanol). Decolorizing can also be effected by passing the protein feed solution through a column, or other appropriate container, packed with an adsorbent, such as activated charcoal or a polymeric resin. For this
  • non-polar, neutral, macroporous polymeric beads having a high surface area e.g. from about 100 to about 1000 square meters per gram
  • Macroporous polystyrene or styrene-divinylbenzene copolymer beads having a pore size from about 10 to about 200 angstroms are preferred.
  • the prolamine is dissolved in alcohol at a concentration of about 2 to about 40% and run through a column containing polystyrene beads at a space velocity of 2 1/hr per gm of beads. This procedure removes the color from the protein and passes the protein with a recovery of over 95%.
  • Deflavoring the protein removes the "grassy” or "grainy” flavor and/or odor which may be present in some proteins.
  • One deflavoring method is to extract the dried protein with solvents such as ethanol, methanol, acetone, hexane or mixtures thereof. The solvent can then be removed from the prolamine by filtration and drying. Deflavoring can also can be accomplished by ultrafiltration. For this purpose, membranes having a pore size less than about 30,000 NMWL can be used.
  • the protein suspension is deflavored by filtering the suspension through a 30,000 NMWL hollow fiber filter cartridge. Protein microparticles treated with ultrafiltration exhibited reduced odor and flavor.
  • the edible coating or barrier can be applied to the substrate of choice by any suitable method, e.g., dipping, spraying, brushing, etc.
  • the prolamine latex is applied to the substrate and dried under moderate heat to evaporate the water, and cause the microparticles to fuse or coalesce into a continuous film.
  • a temperature of at least 40°C is generally used.
  • Quickly raising the temperature of the film composition to above about 75oC, for example, has the effect of driving off the water and of causing the protein microparticles to flow and fuse into a continuous, transparent film.
  • Heat is applied to the surface, preferably via a radiant source, such as a high intensity lamp establishing a surface temperature of about 75°C or above.
  • the film may be cured directly in the baking process.
  • the film may also be cured by high temperature bulk heating of the food or by application to a hot substrate.
  • the important feature of the curing process is to drive off the moisture at a sufficiently high temperature to allow the protein microparticles to flow into a continuous film while there is enough moisture remaining in the film to allow for plastic flow. If a zein
  • dispersion were to be dried at a low temperature, e.g., room temperature, and then subjected to heat, establishing a surface temperature of about 100°C, a continuous, transparent film would not form.
  • the present method using a water-based
  • prolamine latex has several advantages: the latex can be dried to form a stable dry product which can be readily reconstituted with water, or other aqueous medium, prior to use.
  • the prolamine latex is stable under conditions of mild pH (e.g., about 2 to about 10).
  • the preferred pH range for food applications is from about pH 5 to about pH 7.
  • the latex forms a continuous, durable film upon curing which is colorless, odorless, bland to the taste and non-toxic.
  • the film can be applied to foods to form an edible barrier to moisture, lipid, gases, and/or other additives, such as colors, flavors,
  • the edible coating is particularly useful in prepared foods which are stored for a period of time prior to use.
  • frozen pizza presents many problems to the manufacturer.
  • Different components of the product, such as pizza crust, tomato sauce, cheeses and toppings must be discretely maintained under storage conditions.
  • Tomato sauce in particular must be kept from seeping into the crust rendering it soggy, and kept from imparting unwanted color to the cheeses and other toppings.
  • Coating the crust with the present protein coating prior to applying the tomato sauce puts an effective barrier between these phases.
  • the present prolamine coating can be used in other food systems where it is desirable prevent migration of components such as keeping moisture from escaping or migrating within the systems, or preventing colors and/or flavors from blending.
  • a prolamine coating can be applied to tablets for oral ingestion, for example, to provide a barrier between the drug and air or moisture.
  • the present film properties of the prolamine coating can be modified by controlling the
  • concentration of prolamine in the latex the mode of application and the number of layers applied. For example, where a thicker coating is desired, either a latex having a higher prolamine concentration or multiple layers can be applied.
  • the film formed from the present prolamine latex is superior to solvent-cast prolamine films.
  • zein was purified by extraction with acetone.
  • An 800 g portion of dry zein (regular grade, F-4000; Freeman Industries, Inc., Tuckahoe, NY) which had been milled to less than 150 microns in a Micronizer, fluid energy mill (Sturtevant, Inc., Boston, MA) was blended with 2 liters of dry acetone at about 45°C for about 15 minutes. This slurry was then filtered in a coarse sintered glass funnel. The dry solids were resuspended in an additional 2 liters of dry acetone and extracted in a similar manner. A total of 6 extraction steps were made. The filtered solids were then placed in a tray and allowed to air dry overnight, yielding about 780 g of the purified material.
  • a zein solution was prepared by dissolving 630 g of the purified zein, 4.96 g soybean oil (Crisco Brand, The Procter and Gamble Company, Cincinnati, OH) and 2.12 g of a DATEM ester (Myvatem 30, Kodak Company, Rochester, NY) in 9 liters of 90% ethanol (8.1 liters ethanol, 200 proof, and 0.9 liters water). This solution was heated to about 50°C.
  • Another solution was prepared which contained 35 g medium viscosity carboxymethyl cellulose (Sigma Chemical Co., St. Louis, MO) and 35 g gum arable (TIC Gums, Inc., Belcamp, MD) in 36 liters of water. This solution was also heated to about 50°C.
  • the two solutions were combined in a flow through mixing apparatus.
  • the mixing chamber was 65 mm in diameter by 27 mm long.
  • the chamber was mechanically agitated via a 50 mm, 6-bladed turbine rotating at 500 rpm.
  • the two solutions were pumped into the cell, with the aqueous solution being introduced at the base of the cell, and the
  • ethanolic zein solution being introduced through a 0.125 inch, Teflon ® tube, located near the tip of the impeller.
  • the pumping rate allowed for an approximate residence time in the mixing apparatus of about 20 seconds.
  • a precipitated zein latex was formed and removed by displacement at the top of the cell.
  • the resulting suspension was comprised of particles with a median volume diameter of 0.93 microns (80% of the particles were between 0.38 and 2.38 microns) as measured on a Microtrac Small
  • the zein latex was concentrated by ultrafiltration in a 5 ft 2 Pellicon System (Millipore, Inc.,
  • the latex was finally concentrated to about 9.5 liters (approximately 7% solids). The concentrate was then loaded into trays in an approximately 1 cm thick layer, and frozen at -70°C. The latex was freeze-dried in a Virtis shelf drier (Model
  • the zein latex was coated onto glass slides and cured into a film using radiant heat.
  • the freezedried latex prepared in Example A was rehydrated by adding the appropriate amount of cold water to the dry powder and homogenizing the mixture, over an ice bath, using a Polytron homogenizer (Brinkmann
  • the zein latex was reconstituted to three different concentrations, as outlined in Table 1.
  • Example C The film formed from latex III included some bubbles due to the viscous nature of the latex and the formation of bubbles in the latex during homogenization.
  • Zein films were formed on filter paper from the reconstituted latices described in Example B.
  • Filter disks (type 2, 4.25 cm, Whatman International Ltd. , Maidstone, England) were coated by dipping in the latex, and allowing the excess to freely drain off.
  • the disks were placed on a Teflon ® sheet and cured under the heat lamp, located 17 cm above the film for 15 minutes. The heat lamp gave a curing temperature of about 100°C.
  • the coatings were uniform, and the amount of zein incorporated in the films was essentially linearly related to the concentration of the latex solution in which the filters were dipped.
  • Ethanolic solutions of zein were prepared by dissolving 5.02, 10.00 and 15.01 g of zein (regular grade, F-4000, Freeman Industries, Inc., Tuckahoe, NY) in 95, 90 and 85 ml, respectively, of 75% (v/v) ethanol.
  • Example B Films were formed on 7.0 cm Whatman No. 40 filter paper by dipping for 2 minutes, draining and curing under the heat lamp, located 17 cm above the film, for 10 minutes.
  • Control films were prepared by treating filter paper with water or with 75% ethanol. An untreated filter paper control was also tested.
  • the film permeabilities were measured using a modified ASTM procedure. Approximately 20-25 g of 9 mesh anhydrous calcium sulfate (CaSO 4 ) dessicant (W.A. Hammond Drierite Company, Xenia, OH) was placed in a 63 x 17.5 mm aluminum weighing pan
  • the permeabilities of the zein films were measured in a manner similar to that described in Example D, however the packages were stored at 32% relative humidity rather than at 75%, maintaining a 0.34 psi transmembrane differential water vapor pressure. This test describes the effects of moisture level on the barrier properties of the zein film.
  • Example D A series of films was made as described in Example D.
  • a film was formed from milled zein.
  • Zein regular grade, F-4000
  • a Micronizer fluid energy mill to median volume particle diameter of 29 microns.
  • a 15% (w/w) milled zein dispersion in water was prepared into which the filter paper was dipped and the film was cured as described in Example D.
  • the films were used to seal aluminum weighing pans containing dessicant, as described in Example D, however these pans contained 35-36 g of dessicant.
  • the packages were stored at
  • Example D subtracting out the effect of the appropriate control barrier and quantifying the additional moisture barrier properties observed due to the presence of the zein film. None of the controls varied from one another, i.e., water and alcohol treatment had no effect on the barrier properties of the untreated filter paper. The results are given in Figure 2, and show that the latex-based films give superior performance over the solution-based films. The milled zein also forms an effective barrier with performance similar to the solution- based film. The high external relative humidity used in Example D had little or no effect on the resistance of the film (when corrected for the driving force across the membrane, i.e., the
  • Example F Barrier Properties of the Zein Film in a Food System
  • the barrier properties of the latex, milled dispersion, and solution based zein films were quantified in a food system.
  • the 15% solid latex formulation described in Example B, the 15% zein solution described in Example D, and the 15% solid dispersion of milled zein described in Example E were used to coat Unsalted Tops Premium Crackers (Nabisco Brands Inc., East Hanover, NJ). Each coating formulation was painted onto the surface of the cracker using a soft round No. 7 artist's brush.
  • the film was then cured for 10 minutes by placing the cracker under the infrared heat lamp set at 17 cm above the cracker surface. Untreated, water, and alcohol coated controls were run. Each sample was run In duplicate. After coating, the crackers were stored overnight at ambient temperature over dessicant .
  • the crackers were stored at about 38°C and 75% relative humidity (over saturated NaCl), and the moisture uptake was measured gravimetrically. The initial water uptake rate was determined. The Initial water uptake rates of the coated crackers were compared to the controls to establish the relative water uptake shown in Table 2. All of the coatings formulations were equivalently effective barriers with the milled zein dispersion in water being the most effective barrier.
  • Barrier films were prepared on filter paper for quantification of the moisture barrier properties.
  • Dispersions of 2.5%, 10%, 15% and 20% of the dry zein latex (prepared according to the procedure described in Example A) in distilled water were prepared by stirring the powder into water and sonicating for 5 minutes to maximize dispersion.
  • Filter papers, 6 cm in diameter, were immersed in the dispersions and allowed to equilibrate for a few minutes.
  • One set of treated papers was dried in an oven at 45°C for 16 hours, while a second set was dried at 105°C for 2 days.
  • the water barrier properties were measured in a model system with films cast on filter paper.
  • the method employed measured gravimetrically the passage of water through the barrier film into an absorbant filter paper stack.
  • a stack of between 10 and 15 filter papers (6 cm in diameter) was first accurately weighed.
  • a treated paper was placed on top of the stack and the whole stack was clamped into an open-ended brass cylinder with the treated paper uppermost.
  • Approximately 5ml of a commercially bottled spaghetti sauce (Dolmio Spaghetti Sauce) was placed on top of the treated paper and covered with a glass plate to prevent evaporation.
  • latex-based film were measured in a manner similar to the one described in Example G.
  • the barrier films were prepared as described in Example G, and were analyzed in the same apparatus described in
  • Example G except about 5 ml of corn oil were pl ac ed on the treated filter paper ins tead of the spaghetti sauce.
  • the zein latex-based fims formed at 45°C and 105°C were compared to agar-agar, beeswax and zein (cast from an ethanol solution) treated filter papers. There were no discernable differences in the barrier properties of the zein lateax-based film cured at 45°C and the beeswax film when compared to the untreated control.
  • Figure 4 shows the rate of oil uptake for the remaining films tested.
  • a latex-based coating formulation was made using zein, as in Example A, along with a beeswax additive to impart greater resistance to water vapor permeation.
  • a solution was made by dissolving 4.97 g beeswax (Aldrich Chemical Company) in a hot mixture of 90 ml absolute ethanol and 10 ml water. To this solution, 7.00 g zein (Freeman Industries, Lot F4000 848C) and 0.96 g 70% acetylated
  • the latex was formed by rapidly
  • Example A combining the alcohol solution with an aqueous gum solution containing 0.50 gum arable and 0.47 g CMC in 400 ml water in the mixing apparatus described in Example A.
  • the latex was concentrated by first filtering through a coarse cheese cloth to remove any large particles, follwed by concentration of the latex via microfiltration using a regenerated cellulose, 300K NMWL membrane (PLMK, Millipore
  • the ethanol was removed from the concentrate by diafiltration with three volumes of water.
  • the final latex concentrate was 14.4% solid.
  • the latex formulation was used to form films on 7.0 cm diameter filter paper as described in Example D.
  • the film water vapor permeability was measured as described in Example D. Control fims of the zein latex, and of a zein solution in ethanol, as

Landscapes

  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Polymers & Plastics (AREA)
  • Health & Medical Sciences (AREA)
  • Food Science & Technology (AREA)
  • Epidemiology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Zoology (AREA)
  • Medicinal Chemistry (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Animal Behavior & Ethology (AREA)
  • General Health & Medical Sciences (AREA)
  • Public Health (AREA)
  • Veterinary Medicine (AREA)
  • General Preparation And Processing Of Foods (AREA)
  • Manufacture Of Macromolecular Shaped Articles (AREA)
  • Medicinal Preparation (AREA)

Abstract

Un latex protéique aqueux peut être appliqué à un produit alimentaire ou à un autre substrat afin de former un enduit ou couche de protéines ayant d'excellentes propriétés de blocage. La couche protéinique peut former une barrière entre des couches du produit alimentaire ou entre le produit alimentaire d'une part et l'air, l'humidité ou l'huile d'autre part.
PCT/US1990/006441 1989-11-06 1990-11-06 Enduits comestibles a base de proteines WO1991006227A1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US43298889A 1989-11-06 1989-11-06
US432,988 1989-11-06

Publications (1)

Publication Number Publication Date
WO1991006227A1 true WO1991006227A1 (fr) 1991-05-16

Family

ID=23718397

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/US1990/006441 WO1991006227A1 (fr) 1989-11-06 1990-11-06 Enduits comestibles a base de proteines

Country Status (1)

Country Link
WO (1) WO1991006227A1 (fr)

Cited By (21)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1992015208A1 (fr) * 1991-03-01 1992-09-17 Opta Food Ingredients, Inc. Pellicles comestibles servant de barriere contre l'huile pour aliments cuits dans une friture
US5217736A (en) * 1991-03-01 1993-06-08 Opta Food Ingredients, Inc. Potato and other food products coated with edible oil barrier films
WO1993012670A1 (fr) * 1991-12-24 1993-07-08 Deutsche Gelatine-Fabriken Stoess Ag Dispositif de preparation d'aliments frits
WO1993015619A1 (fr) * 1992-02-06 1993-08-19 Griffith Laboratories Worldwide, Inc. Aliments frits enrobes en beignet et panes
EP0585688A2 (fr) * 1992-08-13 1994-03-09 Euro-Celtique S.A. Dispersions aqueuses de zéine et revêtements formés à partir de ces dispersions à libération contrôlée
EP0593123A1 (fr) * 1992-10-16 1994-04-20 Latenstein Zetmeel B.V. Procédé pour la fabrication d'une feuille ou d'une composition de revêtement, basée sur des protéines insolubles dans l'eau
WO1994013160A1 (fr) * 1992-12-16 1994-06-23 Pfizer Inc. Composition d'enrobage d'aliments, contenant un constituant hydrohobe et filmogene
EP0620730A1 (fr) * 1991-12-31 1994-10-26 Abbott Laboratories Enrobages de prolamine pour masquer le gout de medicaments s'administrant par voie orale
WO1995030340A1 (fr) * 1994-05-10 1995-11-16 HER MAJESTY THE QUEEN IN RIGHT OF CANADA, represented by THE MINISTER OF AGRICULTURE AND AGRI-FOOD Produits alimentaires proteges
WO1996034538A1 (fr) * 1995-05-02 1996-11-07 Opta Food Ingredients, Inc. Dispersions colloidales derivees de gluten et enrobages comestibles tires de celles-ci
US5599556A (en) * 1991-12-31 1997-02-04 Abbott Laboratories Prolamine coatings for taste masking
EP0862907A2 (fr) * 1997-03-07 1998-09-09 Dragoco Gerberding & Co Aktiengesellschaft Extrait protéinique de gluten de céréale
EP0869718A1 (fr) * 1995-12-26 1998-10-14 McArdle, Blaise Composition pour conservation des aliments et procedes d'utilisation associes
EP0988801A1 (fr) * 1996-10-04 2000-03-29 SHOWA SANGYO Co., Ltd. Agent de gla age pour aliments possedant une excellente aptitude au revetement
US6174559B1 (en) 1998-12-24 2001-01-16 Opta Food Ingredients, Inc. Gluten-derived colloidal dispersions and edible coatings therefrom and method of making
US6197353B1 (en) 1998-12-24 2001-03-06 Opta Food Ingredients, Inc. Gluten-derived colloidal dispersions, edible coatings therefrom and method of making
WO2002043706A2 (fr) * 2000-12-01 2002-06-06 Labopharm Inc. Compositions a liberation prolongee et compositions a liberation retardee, a base de prolamines
WO2006002346A2 (fr) 2004-06-23 2006-01-05 University Of Maine System Board Of Trustees Compositions barrieres et articles produits a partir de ces compositions
ES2293802A1 (es) * 2005-10-28 2008-03-16 Fomesa Fruitech, S.L. Recubrimiento para la capa superior de fruta encajada.
WO2009118282A2 (fr) * 2008-03-25 2009-10-01 Novozymes A/S Encapsulation de composés labiles par oxydation
CN111655047A (zh) * 2018-03-27 2020-09-11 日清食品株式会社 带面衣油炸食品及其制造方法以及油炸用食品原材料的制造方法

Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US3653925A (en) * 1969-09-18 1972-04-04 Gen Mills Inc Method of preparing gluten containing films and coatings
FR2117506A5 (fr) * 1970-12-11 1972-07-21 Kyowa Hakko Kogyo Kk
WO1980000659A1 (fr) * 1978-10-02 1980-04-17 Purdue Research Foundation Composition de revetement alimentaire et pharmaceutique, methode de preparation et produit ainsi enrobe
WO1989005589A1 (fr) * 1987-12-18 1989-06-29 Wm. Wrigley Jr. Company Chewing-gum contenant un edulcorant tres puissant enrobe de zeine, et procede de production
WO1990003123A2 (fr) * 1988-09-19 1990-04-05 Enzytech, Inc. Micro-particules de proteine hydrophobe et leur preparation

Patent Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US3653925A (en) * 1969-09-18 1972-04-04 Gen Mills Inc Method of preparing gluten containing films and coatings
FR2117506A5 (fr) * 1970-12-11 1972-07-21 Kyowa Hakko Kogyo Kk
WO1980000659A1 (fr) * 1978-10-02 1980-04-17 Purdue Research Foundation Composition de revetement alimentaire et pharmaceutique, methode de preparation et produit ainsi enrobe
WO1989005589A1 (fr) * 1987-12-18 1989-06-29 Wm. Wrigley Jr. Company Chewing-gum contenant un edulcorant tres puissant enrobe de zeine, et procede de production
WO1990003123A2 (fr) * 1988-09-19 1990-04-05 Enzytech, Inc. Micro-particules de proteine hydrophobe et leur preparation

Cited By (33)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5217736A (en) * 1991-03-01 1993-06-08 Opta Food Ingredients, Inc. Potato and other food products coated with edible oil barrier films
WO1992015208A1 (fr) * 1991-03-01 1992-09-17 Opta Food Ingredients, Inc. Pellicles comestibles servant de barriere contre l'huile pour aliments cuits dans une friture
WO1993012670A1 (fr) * 1991-12-24 1993-07-08 Deutsche Gelatine-Fabriken Stoess Ag Dispositif de preparation d'aliments frits
US5599556A (en) * 1991-12-31 1997-02-04 Abbott Laboratories Prolamine coatings for taste masking
EP0620730A1 (fr) * 1991-12-31 1994-10-26 Abbott Laboratories Enrobages de prolamine pour masquer le gout de medicaments s'administrant par voie orale
EP0620730A4 (fr) * 1991-12-31 1995-05-17 Abbott Lab Enrobages de prolamine pour masquer le gout de medicaments s'administrant par voie orale.
US5609909A (en) * 1991-12-31 1997-03-11 Abbott Laboratories Prolamine coatings for taste masking
WO1993015619A1 (fr) * 1992-02-06 1993-08-19 Griffith Laboratories Worldwide, Inc. Aliments frits enrobes en beignet et panes
EP0585688A2 (fr) * 1992-08-13 1994-03-09 Euro-Celtique S.A. Dispersions aqueuses de zéine et revêtements formés à partir de ces dispersions à libération contrôlée
EP0585688A3 (fr) * 1992-08-13 1994-08-03 Euro Celtique Sa
EP0593123A1 (fr) * 1992-10-16 1994-04-20 Latenstein Zetmeel B.V. Procédé pour la fabrication d'une feuille ou d'une composition de revêtement, basée sur des protéines insolubles dans l'eau
WO1994013160A1 (fr) * 1992-12-16 1994-06-23 Pfizer Inc. Composition d'enrobage d'aliments, contenant un constituant hydrohobe et filmogene
WO1995030340A1 (fr) * 1994-05-10 1995-11-16 HER MAJESTY THE QUEEN IN RIGHT OF CANADA, represented by THE MINISTER OF AGRICULTURE AND AGRI-FOOD Produits alimentaires proteges
WO1996034538A1 (fr) * 1995-05-02 1996-11-07 Opta Food Ingredients, Inc. Dispersions colloidales derivees de gluten et enrobages comestibles tires de celles-ci
US5705207A (en) * 1995-05-02 1998-01-06 Opta Food Ingredients, Inc. Method of making gluten colloidal dispersions and edible coatings therefrom
US5736178A (en) * 1995-05-02 1998-04-07 Opta Food Ingredients, Inc. Colloidal dispersions of gluten, method of making and use therefor
EP0869718A1 (fr) * 1995-12-26 1998-10-14 McArdle, Blaise Composition pour conservation des aliments et procedes d'utilisation associes
EP0869718A4 (fr) * 1995-12-26 2000-04-05 Blaise Mcardle Composition pour conservation des aliments et procedes d'utilisation associes
EP0988801A4 (fr) * 1996-10-04 2000-04-19 Showa Sangyo Co Agent de gla age pour aliments possedant une excellente aptitude au revetement
EP0988801A1 (fr) * 1996-10-04 2000-03-29 SHOWA SANGYO Co., Ltd. Agent de gla age pour aliments possedant une excellente aptitude au revetement
EP0862907A2 (fr) * 1997-03-07 1998-09-09 Dragoco Gerberding & Co Aktiengesellschaft Extrait protéinique de gluten de céréale
EP0862907A3 (fr) * 1997-03-07 2000-05-17 Dragoco Gerberding & Co Aktiengesellschaft Extrait protéinique de gluten de céréale
US6174559B1 (en) 1998-12-24 2001-01-16 Opta Food Ingredients, Inc. Gluten-derived colloidal dispersions and edible coatings therefrom and method of making
US6197353B1 (en) 1998-12-24 2001-03-06 Opta Food Ingredients, Inc. Gluten-derived colloidal dispersions, edible coatings therefrom and method of making
WO2002043706A2 (fr) * 2000-12-01 2002-06-06 Labopharm Inc. Compositions a liberation prolongee et compositions a liberation retardee, a base de prolamines
WO2002043706A3 (fr) * 2000-12-01 2003-03-27 Labopharm Inc Compositions a liberation prolongee et compositions a liberation retardee, a base de prolamines
WO2006002346A2 (fr) 2004-06-23 2006-01-05 University Of Maine System Board Of Trustees Compositions barrieres et articles produits a partir de ces compositions
EP1781114A2 (fr) * 2004-06-23 2007-05-09 The University of Maine Board of Trustees Compositions barrieres et articles produits a partir de ces compositions
EP1781114A4 (fr) * 2004-06-23 2010-06-02 Univ Maine Sys Board Trustees Compositions barrieres et articles produits a partir de ces compositions
ES2293802A1 (es) * 2005-10-28 2008-03-16 Fomesa Fruitech, S.L. Recubrimiento para la capa superior de fruta encajada.
WO2009118282A2 (fr) * 2008-03-25 2009-10-01 Novozymes A/S Encapsulation de composés labiles par oxydation
WO2009118282A3 (fr) * 2008-03-25 2009-12-17 Novozymes A/S Encapsulation de composés labiles par oxydation
CN111655047A (zh) * 2018-03-27 2020-09-11 日清食品株式会社 带面衣油炸食品及其制造方法以及油炸用食品原材料的制造方法

Similar Documents

Publication Publication Date Title
US5182130A (en) Method for producing an edible prolamine coating from an aqueous latex
WO1991006227A1 (fr) Enduits comestibles a base de proteines
Cuq et al. Proteins as agricultural polymers for packaging production
US5705207A (en) Method of making gluten colloidal dispersions and edible coatings therefrom
Nesterenko et al. Vegetable proteins in microencapsulation: A review of recent interventions and their effectiveness
Weller et al. Edible bilayer films from zein and grain sorghum wax or carnauba wax
Debeaufort et al. Lipid-based edible films and coatings
Gennadios et al. Mechanical and barrier properties of egg albumen films
Sothornvit et al. Plasticizers in edible films and coatings
US5977312A (en) Modified wheat glutens and use thereof in fabrication of films
US5126152A (en) Method of coating foods with an edible oil barrier film and product thereof
US5567438A (en) Shellac dispersions and coatings, and method of forming aqueous-based shellac dispersions and coatings
WO1990003123A2 (fr) Micro-particules de proteine hydrophobe et leur preparation
CA2739561C (fr) Procede de production de proteines microparticulaires
AU2006294639A1 (en) Encapsulated emulsions and methods of preparation
US5217736A (en) Potato and other food products coated with edible oil barrier films
US20090136641A1 (en) Method of fractionating gliadin from wheat gluten protein and fabrication of edible film therefrom
CA1208068A (fr) Amidon pregelatinise enrobe et procede de production
AU2004281560B2 (en) Method for preparing film coatings and film coating
Lazko et al. Microcapsules based on glycinin–sodium dodecyl sulfate complex coacervation
WO2006132909A1 (fr) Compositions de barriere contre l'humidite comestibles et procedes de preparation de celles-ci
AU682680B2 (en) Crumb coating composition
JP2003093000A (ja) 食品用腸溶性皮膜、腸溶性食品及びその製法
Taylor Preparation, characterisation and functionality of kafirin microparticles
McHugh Effects of chemical properties and physical structure on mass transfer in whey protein-based edible film systems

Legal Events

Date Code Title Description
AK Designated states

Kind code of ref document: A1

Designated state(s): CA JP

AL Designated countries for regional patents

Kind code of ref document: A1

Designated state(s): AT BE CH DE DK ES FR GB GR IT LU NL SE

NENP Non-entry into the national phase

Ref country code: CA