WO2009070011A1 - Procédé de fabrication de capsules à base de protéine - Google Patents

Procédé de fabrication de capsules à base de protéine Download PDF

Info

Publication number
WO2009070011A1
WO2009070011A1 PCT/NL2008/000265 NL2008000265W WO2009070011A1 WO 2009070011 A1 WO2009070011 A1 WO 2009070011A1 NL 2008000265 W NL2008000265 W NL 2008000265W WO 2009070011 A1 WO2009070011 A1 WO 2009070011A1
Authority
WO
WIPO (PCT)
Prior art keywords
protein
proteins
hydrophobic material
cross
dispersion
Prior art date
Application number
PCT/NL2008/000265
Other languages
English (en)
Other versions
WO2009070011A8 (fr
Inventor
Aart Cornelis Alting
Theodorus Arnoldus Gerardus Floris
Fanny Chantal Jacqueline Weinbreck
Jeroen Grandia
Original Assignee
Nizo Food Research B.V.
Van De Velde, Freddie
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 Nizo Food Research B.V., Van De Velde, Freddie filed Critical Nizo Food Research B.V.
Priority to EP08853315A priority Critical patent/EP2217088A1/fr
Publication of WO2009070011A1 publication Critical patent/WO2009070011A1/fr
Publication of WO2009070011A8 publication Critical patent/WO2009070011A8/fr

Links

Classifications

    • B—PERFORMING OPERATIONS; TRANSPORTING
    • B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
    • B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
    • B01J13/00—Colloid chemistry, e.g. the production of colloidal materials or their solutions, not otherwise provided for; Making microcapsules or microballoons
    • B01J13/02—Making microcapsules or microballoons
    • B01J13/06—Making microcapsules or microballoons by phase separation
    • B01J13/14—Polymerisation; cross-linking
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23D—EDIBLE OILS OR FATS, e.g. MARGARINES, SHORTENINGS, COOKING OILS
    • A23D7/00—Edible oil or fat compositions containing an aqueous phase, e.g. margarines
    • A23D7/005—Edible oil or fat compositions containing an aqueous phase, e.g. margarines characterised by ingredients other than fatty acid triglycerides
    • A23D7/0053—Compositions other than spreads
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23D—EDIBLE OILS OR FATS, e.g. MARGARINES, SHORTENINGS, COOKING OILS
    • A23D9/00—Other edible oils or fats, e.g. shortenings, cooking oils
    • A23D9/02—Other edible oils or fats, e.g. shortenings, cooking oils characterised by the production or working-up
    • A23D9/04—Working-up
    • A23D9/05—Forming free-flowing pieces
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K20/00—Accessory food factors for animal feeding-stuffs
    • A23K20/10—Organic substances
    • A23K20/142—Amino acids; Derivatives thereof
    • A23K20/147—Polymeric derivatives, e.g. peptides or proteins
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K20/00—Accessory food factors for animal feeding-stuffs
    • A23K20/10—Organic substances
    • A23K20/158—Fatty acids; Fats; Products containing oils or fats
    • 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
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L27/00—Spices; Flavouring agents or condiments; Artificial sweetening agents; Table salts; Dietetic salt substitutes; Preparation or treatment thereof
    • A23L27/70—Fixation, conservation, or encapsulation of flavouring agents
    • A23L27/72—Encapsulation
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
    • A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
    • A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
    • A23L33/115—Fatty acids or derivatives thereof; Fats or oils
    • 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
    • A23P10/00—Shaping or working of foodstuffs characterised by the products
    • A23P10/30—Encapsulation of particles, e.g. foodstuff additives
    • 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
    • A61K9/48—Preparations in capsules, e.g. of gelatin, of chocolate
    • A61K9/50—Microcapsules having a gas, liquid or semi-solid filling; Solid microparticles or pellets surrounded by a distinct coating layer, e.g. coated microspheres, coated drug crystals
    • A61K9/5005—Wall or coating material
    • A61K9/5021—Organic macromolecular compounds
    • A61K9/5052—Proteins, e.g. albumin

Definitions

  • the present invention concerns a method for encapsulating a hydrophobic core using a protein-based encapsulation matrix.
  • Encapsulated particles thus provided are suitable ingredients for various products, in particular food products.
  • Encapsulation techniques have been developed to protect components against the detrimental effects of e.g. oxygen, moisture, heat, light or chemical reactions and further to control the release of encapsulated components under conditions of use.
  • Acceptable encapsulating agents must be safe and non-hazardous to the consumer's health.
  • Suitable encapsulation agents for food applications include natural gums, carbohydrates, fats and waxes and some proteins. Whereas gum Arabic is one of the most widely used encapsulation agent in food applications the use of proteins is limited.
  • the main protein that has been evaluated for encapsulation is gelatin. Gelatin has been successfully applied as encapsulation agent in the pharmaceutical industry.
  • US 5,601,760 discloses a method for microencapsulation of a volatile or a nonvolatile core material in an encapsulation agent consisting essentially of a whey protein. It is described that whey protein isolate and whey protein concentrate, optionally in combination with milk-derived or non-milk derived carbohydrates, and also ⁇ - lactoglobulin and mixtures of ⁇ -lactoglobulin and ⁇ -lactalbumin were used in a spray- drying encapsulation process.
  • One example describes encapsulation of anhydrous milk fat in whey protein isolate that has been heated at 80 0 C for 30 minutes. This treatment results in denaturation of whey proteins.
  • EP-A 1042960 describes a cappuccino creamer with advantageous foaming properties.
  • the creamer is prepared by spray-drying a slurry that includes as essential constituents protein, lipid and carrier.
  • the protein is partly denatured whey protein (concentrate or isolate).
  • the product is said to contain buoyant, hydrated, insoluble, non-colloidal, irregularly shaped whey protein particles of approximately 10-200 microns in size, with an average particle size of about 60 microns.
  • US 6,841,181 B2 describes the encapsulation of active food components using spray-drying technology.
  • the process consists of mixing active ingredients with non- activated proteins and polysaccharides which are spray-dried to form a capsule.
  • the capsules are 1 - 200 ⁇ m and up to 90% core material.
  • the inventors have discovered that the aforementioned objective can be realized by using a method for encapsulating particles containing hydrophobic material, involving the use of activated protein aggregates, allowing these aggregates to form layers around the hydrophobic material while being dispersed in aqueous phase, and cross-linking the activated protein aggregates by means of disulfide cross- links afterwards.
  • the inventors have discovered that in a suspension comprising a dispersed hydrophobic phase and activated protein aggregates, the protein aggregates will spontaneously form a layer around the hydrophobic droplets and/or particles. Conveniently, encapsulation is initiated already at an early stage, whilst the components stay in aqueous environment. Thus, it is possible to encapsulate the hydrophobic droplets and/or particles in situ by cross-linking the protein aggregates in the interfacial layer.
  • Cross-linkages enhance the ability of the protein-based matrix to protect the encapsulated material against atmospheric oxygen. The ability improves if a protein is utilized that is capable of forming a plurality of disulfide cross-links per molecule.
  • the cross-linking can be achieved by subjecting the suspension to a heat treatment or ultra high pressure. Alternatively, cross-linking may be brought about by contacting the activated aggregates in the interfacial layer with an oxidizing agent. Activation of protein particles is a special form of protein denaturation and is crucial for the formation of disulphide cross- links during subsequent encapsulation steps.
  • the activated protein aggregates are formed by irreversible denaturation of dissolved protein molecules, resulting in exposure of thiol groups that have the ability and accessibility to form disulfide bridges.
  • the reactive thiol groups of denatured protein molecules react together to form disulfide bridges.
  • aggregates comprising a multitude of cross- linked protein molecules are formed.
  • Activated protein aggregates can be prepared by various methods, such as heating, high pressure treatment etc..
  • the resulting protein reactivity is determined by the overall treatment conditions (shear, protein concentration, type of protein, protein composition, type and concentration of salts, pH, other ingredients such as sugars and polysaccharides, fats).
  • the activated aggregates used in the method of the invention exhibit a reactivity of at least 5.0 ⁇ mol thiol groups per gram of activated protein aggregates, as determined in the Ellman's assay (Ellman, G.L. Tissue sulfhydryl groups. Arch. Biochem. Biophys. 1959, 82, 70-77). Methods for achieving activation of the proteins will be detailed below.
  • Proteins that can suitably be cross-linked by disulfide links include proteins that contain amino acid residues with a thiol-group, notably cystein. Provided these cystein groups have been 'activated' in a suitable manner, cystein groups in different protein molecules can react with each other, thereby cross-linking these protein molecules by a disulfide cross-link. Not only cystein residues that have free thiol groups can participate in these cross-linking reactions, but also cystein residues that together form a disulfide bridge can react with a thiol group under the formation of a new disulfide bridge and the release of another free thiol group.
  • ⁇ -lactoglobulin can suitably be used as a cross-linkable protein even though this protein normally contains two pairs of cystein residues that form disulfide bridges and only one cystein residue that contains a free thiol group.
  • proteins that are capable of forming disulfide cross- links include whey proteins, egg proteins, soy proteins, lupine proteins, rice proteins, pea proteins and wheat proteins.
  • the protein-based encapsulates of the present invention are produced by cross-linking activated protein aggregates in a "wet procedure" comprising the steps of:
  • microcapsules are formed in situ in the dispersion.
  • the resulting dispersion of microcapsules can be employed as such in the preparation of e.g. a foodstuff, a beverage or a nutritional supplement or animal feed. Alternatively, the dispersion may be dried to yield a dry encapsulate.
  • the above makes it clear that particles are already formed before any drying step is performed.
  • the flexibility and control of the "wet procedure" allows different types of encapsulated hydrophobic droplets and/or particles to be made. The particle size and properties can be controlled easily.
  • the method of the present invention provides means for controlling the water-solubility of the particles to any extent desired, thus making it possible to distinguish from untreated reference material exhibiting 100 % water-solubility.
  • the particles are water-insoluble.
  • the invention thus pertains to a method of manufacturing microcapsules containing a hydrophobic core and a protein-based shell, said method comprising the steps of: a) preparing a dispersion of hydrophobic material in a continuous aqueous phase containing activated protein aggregates, said preparation comprising: al) providing an aqueous solution or suspension of a protein that is capable of forming disulfide cross-links; a2) submitting said aqueous solution or suspension to a protein activation treatment to produce an aqueous suspension of activated protein aggregates, said suspension having a reactivity of at least 5.0 ⁇ mol thiol groups per gram of protein as determined in the Ellman's assay; wherein the aqueous solution or suspension provided in step al) contains a dispersed phase of hydrophobic material and/or wherein hydrophobic material is dispersed throughout the suspension of activated protein aggregates in or after step a2), in any event prior to step b); b) allowing the activated protein aggregate
  • the present method consists of the subsequent steps a) - c).
  • encapsulate and "microcapsule” as used herein are interchangeable, and refer to the particulate or droplets of hydrophobic material obtained by the method of the present invention.
  • the individual particles within the encapsulate can consist of clearly identifiable discrete particles, but they can also consists, for instance, of a cluster of (micro-)particles, e.g. as a result of agglomeration.
  • step al) Aqueous solution/suspension of a protein capable of forming disulfide cross- links
  • a protein is added to an aqueous solution, such as for example water.
  • aqueous solution of protein that is capable of forming disulfide cross-links can also contain non-dissolved protein and other non- dissolved components. Therefore, step al) results in a solution or suspension containing proteins which may be activated in subsequent steps.
  • the text refers to "the aqueous solution containing a protein capable of forming disulfide cross- links"
  • protein refers to a polymer made of amino acids arranged in a chain and joined together by peptide bonds between the carboxyl and amino groups of adjacent amino acid residues. Typically, the protein contains at least 10 amino acid residues.
  • the protein employed in accordance with the present invention can be, for instance, an intact naturally occuring protein, a protein hydrolysate or a synthesised protein. The protein is preferably food-grade.
  • Protein hydro lysates refers to a mixture of proteins and/or peptides obtained by (partial) breakage of peptide bonds, e.g. through enzymatic hydrolysis or other treatments.
  • Suitable isolated proteins may be obtained from various sources. They may be extracted or purified from natural sources, such as plants, animal milk, animal tissue, microorganism, etc. using known methods or they may be obtained commercially. Suitable proteins or protein compositions (i.e. mixtures of different types of proteins and/or proteins from different sources) include for example total milk proteins, individual milk proteins, such as one or more whey proteins, e.g. ⁇ -lactoglobulin, ⁇ - lactalbumin, bovine serum albumin, etc., and/or one or more caseins such as ⁇ -caseins, ⁇ -caseins, ⁇ -caseins and ⁇ -caseins or total caseins or total whey proteins. Total whey proteins can for example be obtained from Davisco Foods, USA (e.g. BiPROTM).
  • a protein in its native form comprises at least three cystein residues per molecule, even more preferably at least 4, most preferably at least 5 cystein residues per molecule.
  • the whey proteins ⁇ -lactoglobulin and ⁇ -lactoglobulin contain 5 and 8 cystein residues per molecule, respectively.
  • cystein residue in native form refers to the natural state of the protein in the material it is sourced from.
  • cystein residue also encompasses cystein residues that are bound to other cystein residues by means of a disulfide bond.
  • the protein preferably comprises at least about 1 or even
  • the average molecular weight of the protein capable of forming disulfide cross-links is preferably at least 5, 10, 15, 20, 50, 100, 200, 250 or more kDa as determined by SDS-PAGE analysis.
  • the protein employed in step al) advantageously contains at least 30 amino acid residues, more preferably at least 50 amino acid residues and most preferably at least 60 amino acid residues.
  • animal proteins such as bovine serum albumin, one or more blood proteins and/or one or more egg proteins may be used.
  • certain microbial proteins such as one or more bacterial proteins and/or fungal proteins (including yeast proteins) can be used.
  • the aqueous phase provided in step al) preferably contains one or more proteins selected from one or more of the group consisting of whey proteins, egg proteins, soy proteins, lupine proteins, rice proteins, pea proteins, wheat proteins and combinations thereof. Even more preferably, said cross-linked protein is selected from the group consisting of whey proteins, soy proteins and combinations thereof. Most preferably, the protein is a whey protein or a combination of whey proteins. Most preferably, all proteins provided in step al) fall within the aforementioned ranges.
  • the dispersion of hydrophobic material further containing activated protein aggregates submitted to step b) contains preferably 0.1 - 50 wt%, more preferably 0.2- 25 wt%, most preferably 0.5 - 15 wt% of protein(s) capable of forming disulfide cross- links, based on the weight of the continuous aqueous phase.
  • the weight of any dispersed hydrophobic material is not incorporated in these numbers.
  • Step a2) activation treatment the aqueous protein solution/suspension is submitted to a protein activation treatment.
  • the nature of this treatment is not essential, provided that the protein becomes sufficiently activated for further use.
  • the activation treatment is preferably a heat treatment
  • other methods may also be suitable for achieving the same degree of protein activation, such as application of high pressure, shear forces, etc.
  • suitable methods for achieving adequate protein reactivity are microwave treatment, high pressure, shear, unfolding with urea, and combinations thereof. The skilled person can easily determine whether the treatment results in sufficiently activated (reactive) protein aggregates.
  • the temperature and time required for obtaining the minimum reactivity depends on the types of protein used and other conditions, such as applied shear, pH of the solution, salts, etc.
  • heat treatment of a solution of 9%wt. whey proteins (BiPROTM; Davisco, USA) in demineralized water for 30 minutes holding time at 90 0 C in a water bath without stirring resulted in a reactivity of more than 15 ⁇ mol per gram of protein.
  • Heat treatment preferably involves a period of 0.1 sec to 24 hour. It is particularly preferred that the heating time ranges from 10 s - 1 hour, more preferably from at least 10 minutes. The preferred corresponding minimum and maximum temperatures may be calculated from the above formulae.
  • the treatment should be sufficient to result in protein aggregates having a reactivity of at least 5.0 ⁇ mol thiol groups per gram of protein.
  • the reactivity achieved is at least 10 ⁇ mol/g, more preferably at least 15 ⁇ mol/g, even more preferably at least 20 ⁇ mol/g and most preferably at least 25 ⁇ mol/g.
  • the activated protein aggregates submitted to step b) have a volume- weighted average diameter in the range of 1-1000 nanometers, more preferably in the range of 2 - 250 nanometers, even more preferably in the range of 2 - 100 nanometers.
  • the treatment should be sufficient to result in protein aggregates having a reactivity of at least 5 ⁇ mol thiol groups per gram of protein.
  • the reactivity achieved is at least 10 ⁇ mol/g, more preferably at least 15 ⁇ mol/g, even more preferably at least 20 ⁇ mol/g and most preferably at least 25 ⁇ mol/g.
  • the activated protein aggregates submitted to step b) have a volume- weighted average diameter in the range of 1-1000 nanometers, more preferably in the range of 2 - 250 nanometers, even more preferably in the range of 2 - 100 nanometers. Ellman's assay
  • the aforementioned reactivity can suitably be determined at pH 7 according to the Ellman's assay (Ellman,1959 vide supra).
  • the absorbance is measured at 20-25 0 C.
  • the value after 30 minutes of incubation with DTNB is taken to calculate the reactivity.
  • the reactivity is measured by determining the concentration of thiol groups (in mM) in a 2 wt% protein solution. The numbers on the molar amount of thiol groups per gram protein as used throughout the text can easily be calculated there from.
  • suspension of activated protein aggregates is subjected to cooling to preferably lower than 30 °C, more preferably ambient conditions prior to any subsequent steps.
  • the aqueous solution/suspension is provided with one ore more hydrophobic materials.
  • the hydrophobic materials may be provided to the aqueous solution/suspension before adding the cross- linkable proteins, after adding but before activating the cross-linkable proteins, or even after activating the cross-linkable proteins.
  • the hydrophobic material should at least be dispersed throughout the aqueous solution/suspension prior to step b).
  • the hydrophobic material is added as a dispersed phase in the aqueous solution after the activation step a2), as a step a3).
  • hydrophobic material stands for all components incorporated in the dispersed phase. It includes oils, waxes, oil-soluble vitamins, fatty acids (e.g. PUFAs), lipophilic drugs, active pharmaceutical ingredients (APIs), oil-soluble flavors, oil- soluble colorants, peptides, minerals, vitamins, bioactive components, hormones etc.
  • any component preferably food-grade, which benefits from protection against the environment, such as oxygen, moisture, acid conditions, interaction with food matrix, temperature etc. may be used as well as any other component that is to be separated from its environment simply to prevent the escape thereof, e.g. volatile components as well as gases, in particular air.
  • a method as defined herein before is thus provided, wherein a component is encapsulated, said component being selected from the group consisting of vitamins, minerals, peptides, polyphenols, fatty acids, oils, drugs, bioactive components, flavors, colorants, fibres, gas and combinations thereof and combinations thereof.
  • the hydrophobic material may be present in liquid or in solid form, or as a mixture thereof, thus forming an emulsion or suspension, respectively, containing hydrophobic material dispersed in water.
  • the aqueous phase provided in step a) may contain as much hydrophobic material as possible, provided that the aqueous phase thus formed remains the continuous phase, and the hydrophobic material stays dispersed therein. It is preferred that the aqueous phase, submitted to step b), contains 1-50 wt%, more preferably 5 - 45 wt%, most preferably 10 - 40 wt% of the dispersed hydrophobic material, based on the total weight of the dispersion submitted to step b).
  • the ratio (w/w) of hydrophobic material to protein in the aqueous dispersion submitted to step b) is preferably comprised between 1:8 to 200:1, preferably in a weight ratio of 1 :4 to 10:1.
  • the hydrophobic material comprises one or more oils, preferably at least 60 wt%, more preferably at least 70 wt% of the hydrophobic material dispersed in the aqueous phase submitted to step b). It is preferred that less than 80 wt% of the hydrophobic phase is represented from oils.
  • oils are often used in the art to characterise fats which are in liquid form at room temperature, in the context of the invention the terms “fat” and “oil” are considered interchangeable. Both fats and oils may be applied, thus resulting in oil droplets or fat particles, or combinations thereof.
  • oil as used herein encompasses any lipid substance that contains one or more fatty acid residues.
  • oil encompasses, for instance, triglycerides, diglycerides, monoglycerides, free fatty acids and phospholipids. Not all need be present necessarily.
  • the oil employed in accordance with the present invention can be a solid, a liquid or a mixture of both.
  • fatty acid as used herein encompasses free fatty acids as well as fatty acid residues. Whenever reference is made herein to a weight percentage of fatty acids, this weight percentage includes free fatty acids as well as fatty acid residues (e.g. fatty acid residues contained in triglycerides).
  • the oil droplets/particles consist of an oil having a melting point of less than 40 0 C, more preferably of less than 30 0 C and most preferably of less than 15 0 C.
  • the oil droplets/particles of the dispersed phase preferably contain at least 50 wt%, more preferably at least 70 wt% and most preferably at least 80 wt% of a lipid material selected from the group consisting of triglycerides, diglycerides and mixtures thereof.
  • the oil comprises one or more flavor oils.
  • Any fat or oil may be suitable, in particular food-grade fats or oils, such as plant derived oil (e.g. sunflower oil, canola oil, palm oil, soybean oil, flax oil, safflower oil, peanut oil, maize oil, olive oil, pumpkin oil, etc.). They may also be processed fats and oils or synthesized fats and oils which are subjected to hardening, fractionation, interesterif ⁇ cation and the like.
  • oils and fats rich in poly unsaturated fatty acids are used.
  • polyunsaturated fatty acid encompasses any fatty acid containing 2 or more double bonds in the carbon chain.
  • the advantageous properties of the present encapsulates are particularly pronounced in case the dispersed hydrophobic phase contains high levels of PUFAs. Accordingly, in a preferred embodiment, the dispersed hydrophobic phase contains at least 5 wt%, more preferably at least 10 wt%, most preferably at least 20 wt% of PUFAs.
  • the dispersed hydrophobic phase submitted to step b) contains at least 3 wt%, more preferably at least 5 wt% and most preferably at least 10 wt% of one or more PUFAs selected from the group consisting OfC 18 -C 24 ⁇ 3- fatty acids, C 18 -C 24 ⁇ 6-fatty acids and combinations thereof, based on the total weight of the hydrophobic phase.
  • the latter PUFAs are selected from the group consisting of docosahexaenoic acid (DHA), eicosapentaenoic acid (EPA), arachidonic acid, gamma-linoleic acid, conjugated linoleic acid (CLA) and combinations thereof.
  • DHA docosahexaenoic acid
  • EPA eicosapentaenoic acid
  • CLA conjugated linoleic acid
  • the PUFAs are selected from the group consisting of DHA, EPA, CLA and combinations thereof.
  • the PUFA in the dispersed hydrophobic phase may suitably be provided by a vegetable oil or a marine oil. Examples of such oils include fish oil, algae oil and linseed oil.
  • the present invention also encompasses encapsulates in which the oil droplets/particles comprise a blend of a high PUFA oil and one or more other lipid components.
  • one or more (food-grade) additives may be added to the aqueous solution, either before the activation treatment and/or after the activation treatment, but prior to the cross-linking treatment.
  • the additives are not reactive towards the activated protein aggregates, i.e. non-cross-linkable by forming disulfide bonds, e.g. the additives do not react with free thiol groups as this would interfere with subsequent cross-linking of the protein.
  • cross- linkers which will assist in cross-linking the activated protein aggregates, as addressed below.
  • Suitable additives are e.g. carbohydrates (e.g. fibers, inulin, maltodextrin, lactose, sucrose, glucose, galactose), hydrocolloids (e.g. gum Arabic, alginate, pectin, starch, xanthan gum, carrageenan, guar gum, locust bean gum, tara gum, gellan gum), polyols (e.g. glycerol, xylitol), plasticizers (e.g. glyceryl triacetate and/or di-(2- ethylhexyl)adipate) and proteins that are not able to form disulfide cross-links (e.g. gelatin).
  • carbohydrates e.g. fibers, inulin, maltodextrin, lactose, sucrose, glucose, galactose
  • hydrocolloids e.g. gum Arabic, alginate, pectin, starch, xanthan gum, carrage
  • Step b) Layer formation in wet conditions
  • the activated protein aggregates form a layer at the interface of the dispersed phase of hydrophobic material and the aqueous phase. Although the layer forms spontaneously, the process may be promoted by mechanical agitation, e.g. stirring or homogenization.
  • the protein layer formed at the interface of the hydrophobic phase with the continuous aqueous phase preferably has a thickness in the range of 0.01 - 50 ⁇ m, more preferably 0.01 - 25 ⁇ m, even more preferably 0.01 - 5 ⁇ m.
  • the dispersed phase containing hydrophobic material thus obtained preferably has a mass-weighted average diameter of 0.1 - 5000 ⁇ m. If the dispersed phase involves hydrophobic droplets, it is preferred that the mass-weighted average diameter is preferably 1 - 500 ⁇ m, most preferably 1 - 100 ⁇ m.
  • microcapsules or encapsulates are ultimately formed by forming disulfide crosslinks between the activated protein aggregates contained in the interface layer by heating, pressurization and/or contacting the activated protein aggregates with an oxidizing agent.
  • cross-linking is to be achieved by heating, it should involve heating to a temperature of a least 40 0 C for at least 5 milliseconds and/or by pressurizing the suspension droplets to a pressure of at least 50 MPa. More preferably said step comprises heating the suspension droplets to a temperature within the range of 50-150 0 C, most preferably within the range of 60-120 0 C, preferably for 1-86,000 seconds, more preferably for 20-86,000 seconds.
  • cross-linking may be established by pressurization to a pressure within the range of 50-1000 MPa, most preferably within the ranges of 100-600 MPa. Said pressures may typically be applied for at least 0.1 second, preferably for 1-7200 seconds.
  • Yet another method of cross-linking the activated protein aggregates at the interface of the dispersed droplets in the emulsion is by oxidizing, using an oxidizing agent.
  • the oxidizing agent according to the invention has the ability to oxidize the free thiol groups in the protein aggregates to form disulfide cross-links. Any oxidizing agent having this ability may be used in accordance with the invention.
  • the oxidizing agent is selected from the group consisting of salts, oxides or ligands of transition metals, reactive oxygen compounds (e.g. hydrogen peroxide) and oxidizing enzymes (oxidoreductases) and combinations thereof.
  • transition metals that can be used in the form of salts or ligands in the present method are selected from the group consisting of copper, iron, manganese, zinc, ruthenium, cobalt and combinations thereof. Most preferably, the transition metal is selected from the group consisting of copper (Cu(II)), iron (Fe(III)), manganese, nickel, zinc and combinations thereof. According to another preferred embodiment, the present method employs a salt of a transition metal, e.g. a transition metal oxide or a transition metal halide. The term "salt" as used herein also encompasses the use of dissociated salts.
  • the protein aggregates are contacted with the one or more transition metals in an aqueous medium containing at least 0.001 mM of the said transition metals, more preferably 0.001-500 mM, most preferably 0.01-100 mM.
  • said transition metals are contained in the aqueous medium in the form of cations having a valency of at least 2.
  • Oxidoreductases i.e. enzymes classified under the Enzyme Classification number E.C. 1 (Oxidoreductases) in accordance with the Recommendations (1992) of the Interantional Union of Biochemistry and Molecular Biology (IUBMB)
  • Suitable examples include laccases or related enzymes which act on molecular oxygen and yield water; oxidases, which act on molecular oxygen and yield peroxide; and peroxidases which act on peroxide and yield water.
  • the oxidizing agent is an enzyme selected from the group consisting of oxidases, peroxidases, laccases and combinations thereof. More preferably the oxidizing enzyme is selected from the group consisting of glutathione peroxidase, horseradish peroxidase, microperoxidase, coprinus cinereus oxidase, chloroperoxidase, lactoperoxidase, manganese peroxidase and combinations thereof. Most preferably, the oxidizing enzyme is selected from the group consisting of glutathione peroxidase, horseradish peroxidase, coprinus cinereus oxidase, manganese peroxidase and combinations.
  • the present invention also encompasses the formation of encapsulates in which protein in the protein-based matrix has not only been cross-linked by disulfide bonds, but in which additional cross-linking mechanisms have been used to cross- link the protein molecules.
  • Examples of alternative cross- linking techniques include the aforementioned use of gluteraldehyde and/or transglutaminase as cross- linking agents.
  • the method of the only involves disulfide cross-linking.
  • the aforementioned characteristics of the protein layer thickness and the volume- weighted average diameter of the dispersed phase formed in step b) are not expected to change significantly during cross-linking.
  • Dispersion of protein-based encapsulated particles/droplets Also provided are a dispersion of hydrophobic particles and/or droplets in a continuous aqueous phase, as obtainable by the method.
  • the protein coating formed has unique properties, as do the particles and droplets themselves.
  • the dispersed hydrophobic phase is enclosed by a protein-based layer containing at least 10 wt% of a protein that has been cross-linked by means disulfide cross-links. It is preferred that at least 50 wt% of this cross-linked protein dissolves when dithiothreitol (DTT) is incorporated in the aqueous phase in a concentration of 2% by weight of water.
  • DTT dithiothreitol
  • the dispersion formed in step c) of the present method can be either an o/w- emulsion or an aqueous suspension, depending on the state of the dispersed material. Numbers on amounts of proteins and hydrophobic material, and the relative weight ratio of oil to protein as provided in steps al) and a) are also applicable here.
  • the size of the hydrophobic particles and droplets in the encapsulates formed in step c) can vary within a wide range. According to a large estimate, the encapsulates have a volume-weighted average size of 0.1 - 5000 microns. If the encapsulates contains hydrophobic droplets, these are preferably characterized by a volume- weighted averaged size within the range of 0.1 - 1000 ⁇ m, especially within the range of 1 - 500 ⁇ m, particularly ranging 1-100 ⁇ m. According to a particularly preferred embodiment, the averaged particle size is equal to or below 50 ⁇ m in diameter, such as equal to or less than 25, 20, 15, 10 or 5 ⁇ m. Size and shape can be analyzed using microscopy (e.g.
  • the particles Preferably at least 80%, 85%, 90% or more of the particles have a diameter of 50 ⁇ m or less, such as 40, 30, 25, 15, 10 ⁇ m or less.
  • the volume- weighted diameter of the oil droplets is preferably within the range of 0.1 - 10 ⁇ m, most preferably 0.2 - 5 ⁇ m.
  • the numbers in the foregoing paragraph apply to the mass- weighted average size.
  • the particle (droplet) size distribution of the encapsulate can suitably be determined in a manner well known to a skilled person using a set of sieves with different well-defined mesh sizes.
  • the average number of hydrophobic droplets/particles per encapsulate can vary widely, e.g. from 1.0 tolO 9 .
  • the encapsulate contains 1.0 to 10 6 of hydrophobic droplets/particles per encapsulate.
  • the encapsulation matrix contains at least 20 wt%, most preferably at least 40 wt%, even more preferably at least 60 wt% of a protein that has been cross- linked by means of disulfide cross- links, based on the weight of total protein in protective protein-based matrix
  • the protein that has been cross-linked by disulfide cross-links exhibits a number weighted average degree of polymerisation of at least 500 more preferably of at least and most preferably of at least 1000.
  • the degree of polymerisation equals the total number of protein molecules that are linked together in a single cross-linked macromolecule.
  • encapsulates may be prepared in which the proteins have not been cross-linked in any other way than by disulfide cross-links.
  • water can be removed in an optional step d) to yield a free flowing powder. It is preferred that the dried encapsulates contain less than 20 wt%, preferably less than 15 wt% of water. Even more preferably the water content does not exceed 10 wt%.
  • the coated particles/droplets obtained in step c) may be subjected to an additional step of spray-drying, resulting in a dried powder comprising the encapsulates.
  • Spray-drying can be carried out as known in the art, for example as described in US 6,223,455 or the "Spray Drying Handbook", K. Masters, 5th ed.,
  • the encapsulates are sprayed and dried using e.g. fluidized bed or spouted bed equipment.
  • fluidized bed or spouted bed equipment Such equipment is available in the art, see e.g. Fluid bed coater GPCG 1.1 with Wurster insert (Glatt GmbH).
  • the encapsulates may be subjected to additional coating steps.
  • the present encapsulates contain at least on coating layer that contains at least 60 wt% of one or more components selected from the group consisting of lipids (including waxes and low PUFA fats), polyols (such as: glycerol, xylitol), menthol, glyceryl triacetate, di-(2-ethylhexyl) adipate, plasticizers (such as glycerol, glyceryl triacetate and/or di-(2-ethylhexyl) adipate, or others), or mixtures of two or more plasticizers; sugars (such as for example: lactose, sucrose, glucose, galactose), hydrocolloids (such as for example: gum Arabic, al
  • additional outer layers may be provided for using any suitable coating method known in the art.
  • the ranges given throughout the text apply to the core and the first protein-based shell layer in direct contact therewith only, obtainable by the method involving steps a) - c) as explained above, unless stated otherwise.
  • the protein-based encapsulates are characterized in that they exhibit a low amount of hydrophobic material at the surface, since the method of the invention ensures that the hydrophobic phase is completely enveloped by the protein-based matrix.
  • the surface hydrophobic content of the encapsulate is less than 10%, more preferably less than 5% and most preferably less than 2%. This may be determined by weighing 10 gram powder and adding 10OmL tetrachloromethane, at room temperature. After 15 minutes of contact time, the mixture is filtered using 502 Schleicher & Schuell filter. 50 mL filtrate is weighed and subsequently the tetrachloromethane is evaporated by drying. After drying the dry amount is weighed again. Form these measurements the amount of unbound hydrophobic material, particularly oil, can be determined.
  • the protein-based hydrophobic encapsulates according to the present invention exhibit the special property that the protein contained in the protein-based matrix exhibits very poor water solubility as a result of the disulfide cross-linking. Without these cross-links the protein-based matrix normally has a much higher water solubility. This poor water solubility is also apparent within a broad pH range at near ambient conditions.
  • the protein-based matrix is characterized in that less than 70 wt.%, more preferably less than 40 wt.% and most preferably less than 25 wt.% of the protein contained in the protein-based matrix can be dissolved when 75 mg of the encapsulate is dispersed in 50 ml distilled water having a temperature of 25 0 C at any pH within the range of 3.0-7.0.
  • the weight percentage of the protein that can be dissolved is at least a factor 1.3 higher when in the aforementioned procedure the distilled water is replaced by an aqueous solution of 2 wt.% dithiothreitol (DTT).
  • the protein-based matrix is characterised in that: i.
  • less than 40 wt.%, more preferably less than 25 wt.% of the protein contained in the protein-based matrix can be dissolved when 75 mg of the encapsulate is dispersed in 50 ml distilled water having a temperature of 25 0 C at any pH within the range of 3.0-7.0; ii. the weight percentage of the protein that can be dissolved is at least a factor 2 higher when in the aforementioned procedure the distilled water is replaced by an aqueous solution of 2 wt.% DTT.
  • the protein-based matrix is characterized in that less than 40 wt.%, more preferably less than 25 wt.% of the protein-based matrix can be dissolved when 75 mg of the encapsulate is dispersed in 50 ml distilled water having a temperature of 25 0 C at any pH within the range of 1.0-8.0.
  • the protein-based matrix is characterised in that: i. less than 40 wt.%, more preferably less than 25 wt.% of the protein contained in the protein-based matrix can be dissolved when 75 mg of the encapsulate is dispersed in 50 ml distilled water having a temperature of 25 0 C at any pH within the range of 1.0-8.0; ii. the weight percentage of the protein that can be dissolved is at least a factor 2 higher when in the aforementioned procedure the distilled water is replaced by an aqueous solution of 2 wt.% DTT.
  • solubility tests the pH of the distilled water or the DTT solution is adjusted with the help of HCl and solubility is measured 16 hours after the encapsulate was dispersed in the liquid. During this period the mixture is continuously gently stirred in order to prevent 'clumping' of the encapsulate particles.
  • solubility test i) and ii) pH is adjusted to achieve maximum protein solubility within the pH range of 3.0-7.0.
  • the invention also encompasses a further step of combining the microcapsules formed by the method of the present invention, either in dispersion as obtained after step c), or concentrated or dried after an optional step d), with one or more other edible ingredients, to produce a food, a beverage, a nutritional supplement or animal feed, that is subsequently packaged.
  • the protein-based encapsulates of the present invention can for instance advantageously be employed as a vehicle for delivering biologically active ingredients to an animal or a human.
  • protein-based encapsulates that are stable under gastric conditions may suitably be used to deliver biologically active ingredients that are not stable under gastric conditions.
  • one aspect of the invention relates to the of use the present protein-based encapsulates in therapeutic or prophylactic treatment, said treatment comprising oral administration of the protein-based encapsulates.
  • the protein encapsulated particles are orally administered in an amount of 0.1 to 40 g per administration event.
  • the biologically active ingredient may be a pharmaceutically active ingredient or a nutrient (including micronutrients such as vitamins).
  • Another aspect of the present invention relates to a foodstuff, a beverage, a nutritional supplement or animal feed containing from 0.3-80 wt.% of a dried or concentrated encapsulate as defined herein before (as obtained in step d) or from 0.5-98 wt.% of the dispersion as obtained in step c) of the method of the invention.
  • the invention also pertains to a method of these applications, involving combining the dried microcapsules of step d) or the dispersion of step c) of the present method with conventional ingredients, to obtain the aforesaid numbers.
  • Food products comprising the particles include for example the following: cold or warm drinks, such as coffee, chocolate, tea, fruit or vegetable juices; soups; sauces; spreads, batters, ready-to-eat meals, dairy products (milk, milk-based drinks, yoghurt, cheese, butter, margarine, ice cream), pasta, fruit or vegetable products, meat or fish products, meat replacers, bread, pastries, deserts, sweets, candy-bars, confectionary, food- or drink- additives (such as coffee or tea creamers, sweeteners), powders such as instant coffee or tea, milk-powder, soup powder, ice-cream, etc.
  • Feed products include any type of animal feed, such as feed for farm animals (cows, horses, pigs, chicken, etc.), pets (dogs, birds, fish, cats, rabbits, rodents, etc), wild animals, etc.
  • the invention relates to the use of encapsulates obtainable by the method of the present invention in pharma applications and cosmetic products.
  • Example 1 preparation of spray-dried orange oil capsules Protein solution was prepared by mixing 54 g of whey protein isolate (Bipro; Davisco,
  • Reactive protein aggregates were prepared by heating the whey protein isolate solution at 68.5 0 C during 2 hours in a water bath. The solution was further cooled down in ice and then brought to room temperature. The reactivity of the particles was determined using the DTNB-method as described before. The reactivity was about 17 ⁇ mol thiol groups per gram protein.
  • a pre-emulsion was prepared by mixing 128 g of demineralized water and 400 g of a solution of 9% of reactive protein aggregates and 72 g of orange oil (lot nr 04723BC-137 Sigma Aldrich) using an Ultra-turrax (2 min at power 9.5). The mixture was then homogenized using a two-stage high pressure homogenizer (Model NSlOOlL - PANDA, Niro Soavia S.P.A., Italy; flow 10 L/h) (400/40 bar). The suspension of orange oil capsules with activated protein aggregates was subsequently heated for at 90 0 C during 30 minutes hours in a water bath. The emulsion was further cooled down in ice and then brought to room temperature.
  • the emulsion was spray-dried using a Buchi lab-scale spray- dryer (inlet temperature 160 0 C, outlet temperature 90 0 C). By spray-drying a powder was obtained.
  • Example 2 Measurement of the payload of the spray-dried orange oil capsules: Spray-dried orange oil capsules were prepared as described in example 1. The payload of the oil contained in the powder after spray drying was measured using nucleic magnetic resonance (NMR, Brucker Minispec MQ20 NMR analyser). The maximum payload based on the solid content of the suspension before spray drying is 33 %wt. of the orange oil contained in the powder after spray drying of capsules.
  • the capsules prepared with reactive protein aggregates and subsequent cross- linking showed a payload of 25 %.
  • Example 3 preparation of an aqueous suspension of fish oil capsules with activated protein aggregates
  • Protein solution was prepared by mixing 54 g of whey protein isolate (Bipro; Davisco, USA) in 546 g of demineralized water at room temperature (stirred for 2 h).
  • Reactive protein aggregates were prepared by heating the whey protein isolate solution at 68.5°C during 2 hours in a water bath. The solution was further cooled down in ice and then brought to room temperature. The reactivity of the particles was determined using the DTNB-method as described before. The reactivity was about 17 ⁇ mol thiol groups per gram protein.
  • a pre-emulsion was prepared by mixing 128 g of demineralized water and 400 g of a solution of 9% of reactive protein aggregates and 72 g of fish oil (batch 116kl837 Sigma Aldrich) using an Ultra-turrax (2 min at power 9.5). The mixture was then homogenized using a two-stage high pressure homogenizer (Model NSlOOlL - PANDA, Niro Soavia S.P.A., Italy; flow 10 L/h) (400/40 bar). The suspension of fish oil capsules with activated protein aggregates was subsequently heated for at 9O 0 C during 30 minutes hours in a water bath. The emulsion was further cooled down in ice and then brought to room temperature.
  • Example 4 Measurement of oxidation products of fish oil capsules
  • the aqueous suspension of fish oil capsules was prepared as described in example 3.
  • the aqueous suspension of fish oil capsules was stored in an open container at ambient conditions during 5 weeks.
  • An open container containing the fish oil used for the preparation of the suspension of the fish oil capsules was used a reference and stored on the conditions described for the capsules.
  • the amounts of oxidation products of fish oil were measured in the capsules and the free fish oil sample using gas chromatography.
  • the amount of the oxidation products measured for the aqueous suspension of fish oil capsules were expressed as the percentage of the amount of oxidation products measured for the free fish oil (Table 1).
  • Table 1 Relative amount of fish oil oxidation products measured after 5 weeks of ambient storage.

Landscapes

  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Polymers & Plastics (AREA)
  • Engineering & Computer Science (AREA)
  • Food Science & Technology (AREA)
  • Health & Medical Sciences (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Zoology (AREA)
  • Organic Chemistry (AREA)
  • Nutrition Science (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Animal Husbandry (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Veterinary Medicine (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Epidemiology (AREA)
  • Animal Behavior & Ethology (AREA)
  • General Health & Medical Sciences (AREA)
  • Public Health (AREA)
  • Medicinal Chemistry (AREA)
  • Dispersion Chemistry (AREA)
  • Mycology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Cosmetics (AREA)
  • General Preparation And Processing Of Foods (AREA)
  • Manufacturing Of Micro-Capsules (AREA)
  • Fodder In General (AREA)

Abstract

La présente invention concerne des microcapsules contenant un noyau hydrophobe et une enveloppe à base de protéine. L'invention concerne également un procédé de préparation de capsules à base de protéine comprenant les étapes suivantes : la formation par des agrégats de protéines activées dans une solution aqueuse contenant un matériau hydrophobe d'une couche à l'interface de la phase dispersée, et la réticulation des agrégats de protéines activées. Les particules encapsulées de protéine sont particulièrement appropriées pour des applications alimentaires, d'alimentation pour animaux, cosmétiques et pharmaceutiques.
PCT/NL2008/000265 2007-11-29 2008-12-01 Procédé de fabrication de capsules à base de protéine WO2009070011A1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
EP08853315A EP2217088A1 (fr) 2007-11-29 2008-12-01 Procédé de fabrication de capsules à base de protéine

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
EP07121892 2007-11-29
EP07121892.9 2007-11-29

Publications (2)

Publication Number Publication Date
WO2009070011A1 true WO2009070011A1 (fr) 2009-06-04
WO2009070011A8 WO2009070011A8 (fr) 2010-03-04

Family

ID=40451078

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/NL2008/000265 WO2009070011A1 (fr) 2007-11-29 2008-12-01 Procédé de fabrication de capsules à base de protéine

Country Status (2)

Country Link
EP (1) EP2217088A1 (fr)
WO (1) WO2009070011A1 (fr)

Cited By (13)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2011008097A1 (fr) 2009-07-17 2011-01-20 Friesland Brands B.V. Procédé pour l'encapsulation d'une huile comestible, compositions comprenant une huile comestible et leur utilisation
EP2201842A3 (fr) * 2008-12-24 2012-05-02 Zeelandia H. J. Doeleman B.V. Améliorant de boulangerie
WO2012109694A1 (fr) * 2011-02-18 2012-08-23 Sai Ying Ko Procédé pour la préparation de produits comprenant des actifs stabilisés et compositions les comprenant
CN104672919A (zh) * 2015-02-09 2015-06-03 南京农业大学 一种利用热稳定性重组漆酶制备乳清蛋白膜的方法
WO2016022532A1 (fr) * 2014-08-05 2016-02-11 Advanced Bionutrition Corporation Encapsulation de composés biologiquement actifs hydrophobes
WO2018206856A1 (fr) * 2017-05-12 2018-11-15 Myllyn Paras Finland Oy Composante de graisse alimentaire, son procédé de production et ses utilisations
RU2702690C2 (ru) * 2015-08-13 2019-10-09 БИОЛИНГУС АйПи ЛЛСи Способ получения продуктов, содержащих стабилизированные активные вещества, и композиций, содержащих таковые
EP3256002B1 (fr) * 2015-02-09 2020-09-23 FrieslandCampina Nederland B.V. Procédé de préparation d'une dispersion aqueuse d'une protéine végétale faiblement dispersible
FR3102912A1 (fr) * 2019-11-07 2021-05-14 Huddle Corp Aliment ou complément alimentaire pour animaux d’élevage
EP4035655A1 (fr) * 2021-02-01 2022-08-03 Oxford University Innovation Limited Articules immunomodulatrices
KR20230049123A (ko) * 2020-08-18 2023-04-12 푸드사이언스, 엘엘씨 중합된 유청 단백질 캡슐화된 항산화제 화합물 및 이를 제조하기 위한 프로세스
WO2023111039A1 (fr) * 2021-12-17 2023-06-22 Firmenich Sa Microcapsules à noyau-enveloppe de polydisulfure
WO2024068235A1 (fr) * 2022-09-26 2024-04-04 Xampla Limited Microcapsules biodégradables et leur procédé de préparation

Citations (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5601760A (en) * 1994-09-01 1997-02-11 The Regents Of The University Of California, A California Corporation Milk derived whey protein-based microencapsulating agents and a method of use
WO2006115420A1 (fr) * 2005-04-26 2006-11-02 Massey University Encapsulation de lipides
WO2007064225A1 (fr) * 2005-12-01 2007-06-07 Tine Ba Compositions comprenant des proteines et des lipides de lactoserum et procedes pour leur preparation
WO2007136263A1 (fr) * 2006-05-22 2007-11-29 Nizo Food Research B.V. Particules encapsulées par une protéine
WO2008119482A1 (fr) * 2007-03-30 2008-10-09 Dsm Ip Assets B.V. Hydrocolloïde protecteur pour des ingrédients actifs
WO2008143507A2 (fr) * 2007-05-21 2008-11-27 Nizo Food Research B.V. Produits d'encapsulation à base de protéine réticulée par oxydation
WO2008157629A1 (fr) * 2007-06-19 2008-12-24 Martek Biosciences Corporation Compositions pour microencapsulation, leurs procédés de fabrication et d'utilisation et produits obtenus à partir de celles-ci

Patent Citations (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5601760A (en) * 1994-09-01 1997-02-11 The Regents Of The University Of California, A California Corporation Milk derived whey protein-based microencapsulating agents and a method of use
WO2006115420A1 (fr) * 2005-04-26 2006-11-02 Massey University Encapsulation de lipides
WO2007064225A1 (fr) * 2005-12-01 2007-06-07 Tine Ba Compositions comprenant des proteines et des lipides de lactoserum et procedes pour leur preparation
WO2007136263A1 (fr) * 2006-05-22 2007-11-29 Nizo Food Research B.V. Particules encapsulées par une protéine
WO2008119482A1 (fr) * 2007-03-30 2008-10-09 Dsm Ip Assets B.V. Hydrocolloïde protecteur pour des ingrédients actifs
WO2008143507A2 (fr) * 2007-05-21 2008-11-27 Nizo Food Research B.V. Produits d'encapsulation à base de protéine réticulée par oxydation
WO2008157629A1 (fr) * 2007-06-19 2008-12-24 Martek Biosciences Corporation Compositions pour microencapsulation, leurs procédés de fabrication et d'utilisation et produits obtenus à partir de celles-ci

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
ELLMAN ET AL: "Tissue sulfhydryl groups", ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, ACADEMIC PRESS, US, vol. 82, no. 1, 1 May 1959 (1959-05-01), pages 70 - 77, XP024815603, ISSN: 0003-9861, [retrieved on 19590501] *

Cited By (23)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP2201842A3 (fr) * 2008-12-24 2012-05-02 Zeelandia H. J. Doeleman B.V. Améliorant de boulangerie
US9649611B2 (en) 2009-07-17 2017-05-16 Friesland Brands B.V. Method for encapsulation of an edible oil, compositions comprising edible oil and the use thereof
WO2011008097A1 (fr) 2009-07-17 2011-01-20 Friesland Brands B.V. Procédé pour l'encapsulation d'une huile comestible, compositions comprenant une huile comestible et leur utilisation
WO2012109694A1 (fr) * 2011-02-18 2012-08-23 Sai Ying Ko Procédé pour la préparation de produits comprenant des actifs stabilisés et compositions les comprenant
US8951566B2 (en) 2011-02-18 2015-02-10 Sai Ying Ko Process for preparing products comprising stabilised actives and compositions comprising same
US10369539B2 (en) 2011-02-18 2019-08-06 Biolingus Ip Llc Process for preparing products comprising stabilised actives and compositions comprising same
CN106659230B (zh) * 2014-08-05 2020-11-13 英特维特国际股份有限公司 疏水性生物活性化合物的包封
WO2016022532A1 (fr) * 2014-08-05 2016-02-11 Advanced Bionutrition Corporation Encapsulation de composés biologiquement actifs hydrophobes
US20160038428A1 (en) * 2014-08-05 2016-02-11 Advanced Bionutrition Corp. Encapsulation of hydrophobic biologically active compounds
US10117839B2 (en) 2014-08-05 2018-11-06 Intervet Inc. Encapsulation of hydrophobic biologically active compounds
CN106659230A (zh) * 2014-08-05 2017-05-10 高级生物营养公司 疏水性生物活性化合物的包封
CN104672919A (zh) * 2015-02-09 2015-06-03 南京农业大学 一种利用热稳定性重组漆酶制备乳清蛋白膜的方法
EP3256002B1 (fr) * 2015-02-09 2020-09-23 FrieslandCampina Nederland B.V. Procédé de préparation d'une dispersion aqueuse d'une protéine végétale faiblement dispersible
RU2702690C2 (ru) * 2015-08-13 2019-10-09 БИОЛИНГУС АйПи ЛЛСи Способ получения продуктов, содержащих стабилизированные активные вещества, и композиций, содержащих таковые
CN111065276A (zh) * 2017-05-12 2020-04-24 麦林帕拉斯芬兰公司 食品脂肪组分、其生产方法和其用途
WO2018206856A1 (fr) * 2017-05-12 2018-11-15 Myllyn Paras Finland Oy Composante de graisse alimentaire, son procédé de production et ses utilisations
FR3102912A1 (fr) * 2019-11-07 2021-05-14 Huddle Corp Aliment ou complément alimentaire pour animaux d’élevage
WO2021089972A1 (fr) * 2019-11-07 2021-05-14 Huddle Corp Aliment ou complément alimentaire pour animaux d'élevage
KR20230049123A (ko) * 2020-08-18 2023-04-12 푸드사이언스, 엘엘씨 중합된 유청 단백질 캡슐화된 항산화제 화합물 및 이를 제조하기 위한 프로세스
KR102651539B1 (ko) 2020-08-18 2024-03-29 푸드사이언스, 엘엘씨 중합된 유청 단백질 캡슐화된 항산화제 화합물 및 이를 제조하기 위한 프로세스
EP4035655A1 (fr) * 2021-02-01 2022-08-03 Oxford University Innovation Limited Articules immunomodulatrices
WO2023111039A1 (fr) * 2021-12-17 2023-06-22 Firmenich Sa Microcapsules à noyau-enveloppe de polydisulfure
WO2024068235A1 (fr) * 2022-09-26 2024-04-04 Xampla Limited Microcapsules biodégradables et leur procédé de préparation

Also Published As

Publication number Publication date
WO2009070011A8 (fr) 2010-03-04
EP2217088A1 (fr) 2010-08-18

Similar Documents

Publication Publication Date Title
WO2009070011A1 (fr) Procédé de fabrication de capsules à base de protéine
US20090238885A1 (en) Protein encapsulated particles
US20110045147A1 (en) Protein-based oil encapsulates
Kaushik et al. Microencapsulation of omega-3 fatty acids: A review of microencapsulation and characterization methods
McClements et al. Structural design principles for delivery of bioactive components in nutraceuticals and functional foods
DK180325B1 (en) Encapsulation of hydrophobic biologically active compounds
JP5923443B2 (ja) 生物活性物質のマイクロカプセル化及びその製造方法
AU2008205325B2 (en) Vegetarian microcapsules
Yan et al. Coacervation processes
Santos et al. Interpolymeric complexes formed between whey proteins and biopolymers: Delivery systems of bioactive ingredients
RU2592572C2 (ru) Композиция и способ повышения стабильности добавок к пищевым продуктам
NZ253679A (en) Microencapsulated oil or fat product, the oil or fat dispersed, as particles or drops having an average diameter of less than or equal to 2 micrometers, in a matrix comprising caseinate
Augustin et al. Use of milk proteins for encapsulation of food ingredients
CA2670772A1 (fr) Procede destine a preparer des huiles en poudre
Sanguansri et al. 12 Microencapsulation and Delivery of Omega-3 Fatty Acids
AU2003303023A1 (en) Complex coacervate encapsulate comprising lipophilic core
WO2008143507A2 (fr) Produits d'encapsulation à base de protéine réticulée par oxydation
EP1925211A1 (fr) Procédé de préparation d'huiles poudrées
ZA200603305B (en) Nutritional composition with unsaturated fatty acids and trace elements
Li et al. Functionality of dairy proteins and vegetable proteins in nutritional supplement powders: a review.
JP2007501628A (ja) 満腹感増強性食品
Cittadini et al. Encapsulation techniques to increase lipid stability
Anbudhasan et al. Development of omega 3 fatty acid enriched stable functional foods: Challenges and options
Thies Microencapsulation methods based on biopolymer phase separation and gelation phenomena in aqueous media
Masum et al. Use of milk proteins for encapsulation of food ingredients

Legal Events

Date Code Title Description
121 Ep: the epo has been informed by wipo that ep was designated in this application

Ref document number: 08853315

Country of ref document: EP

Kind code of ref document: A1

DPE1 Request for preliminary examination filed after expiration of 19th month from priority date (pct application filed from 20040101)
DPE1 Request for preliminary examination filed after expiration of 19th month from priority date (pct application filed from 20040101)
WWE Wipo information: entry into national phase

Ref document number: 2008853315

Country of ref document: EP

NENP Non-entry into the national phase

Ref country code: DE