[go: up one dir, main page]

WO1989010960A1 - Procede de modification de proteines, peptides et/ou lipides au moyen d'enzymes provenant d'euphauciaces - Google Patents

Procede de modification de proteines, peptides et/ou lipides au moyen d'enzymes provenant d'euphauciaces Download PDF

Info

Publication number
WO1989010960A1
WO1989010960A1 PCT/SE1989/000235 SE8900235W WO8910960A1 WO 1989010960 A1 WO1989010960 A1 WO 1989010960A1 SE 8900235 W SE8900235 W SE 8900235W WO 8910960 A1 WO8910960 A1 WO 8910960A1
Authority
WO
WIPO (PCT)
Prior art keywords
krill
enzymes
modification consists
protein
modification
Prior art date
Legal status (The legal status 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 status listed.)
Ceased
Application number
PCT/SE1989/000235
Other languages
English (en)
Inventor
Viggo Mohr
Lars Hellgren
Jan Vincent
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Pfizer Health AB
Original Assignee
Pharmacia AB
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 Pharmacia AB filed Critical Pharmacia AB
Publication of WO1989010960A1 publication Critical patent/WO1989010960A1/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

Links

Classifications

    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12PFERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P7/00Preparation of oxygen-containing organic compounds
    • C12P7/64Fats; Fatty oils; Ester-type waxes; Higher fatty acids, i.e. having at least seven carbon atoms in an unbroken chain bound to a carboxyl group; Oxidised oils or fats
    • C12P7/6409Fatty acids
    • C12P7/6418Fatty acids by hydrolysis of fatty acid esters
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/16Hydrolases (3) acting on ester bonds (3.1)
    • C12N9/18Carboxylic ester hydrolases (3.1.1)
    • C12N9/20Triglyceride splitting, e.g. by means of lipase
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
    • C12N9/64Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6402Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12PFERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00Preparation of peptides or proteins
    • C12P21/06Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products

Definitions

  • the present invention relates to novel applications of enzymes in the area of production technology.
  • the invention specifies how preparations of active enzymes or enzyme systems selected from animals belonging to the order Euphauciaceae can be used in a novel way in industrial processes.
  • the unique properties of the enzymes of this order of animals are utilized in a way which opens up new perspectives in the area of enzyme technology.
  • the invention explicitly documents how the preparations of said enzymes can be applied in clearly defined processes and with the purpose of manufacturing specific products..
  • the krill have developed an unusually effective digestive apparatus which secures that food, when available, is quickly digested and deposited as storage lipid.
  • the digestive enzymes of this apparatus are of considerable interest therapeutically and industrially.
  • krill are also unusual in another sense. Few other groups of animals are adapted to life at such low temperatures as Antarctic- and Arctic krill which may frequently experience temperatures approaching that of freezing sea water (-1.9 oC). Thus, the enzyme systems of krill are designed to exhibit activity at such low temperatures. When studied in vitro, activity can be observed at even lower temperatures, provided that freezing is prevented by the addition of antifreeze agents.
  • krill are characterized by having not only an unusually high level of digestive enzymes, but the enzymes are also adapted to function effectively at low temperatures. At present few, if any enzyme systems with such characteristics are generally available commercially, despite the fact that enzymes of this type would open up a completely new field of considerable commercial importance, namely low temperature enzyme technology.
  • the present invention makes a systematic contribution to this area by pointing out specific industrial applications which depend on the unique properties of the enzymes of krill, and which utilize the unusual effectiveness of these enzymes and/or their particular temperature relationships.
  • Krill contain an array of enzymes required to break down the polymeric substances making up the food of the animals.
  • enzymes Of particular interest in the context of industrial application are the peptide hydrolases and the lipolytic enzymes of krill.
  • the peptide hydrolases of krill have been studied in considerable detail, and it has been shown that krill rely on a system of both endo- and exopeptidases to degrade protein.
  • the krill peptide hydrolases include three trypsin-like enzymes, two carboxypeptidase A-type of enzymes, two carboxypeptidase B-type of enzymes and one aminopeptidase (Osnes & Mohr, 1985a; Osnes & Mohr, 1985b; Osnes & Mohr, 1986). These enzymes seem to originate almost exclusively from the digestive tract of the krill, and thus seem to constitute enzymes of the digestive apparatus of the animals.
  • the peptide hydrolases give rise to a rapid autolyses of the krill tissues post mortem, resulting in the production of large amounts of free amino acids (Ellingsen & Mohr, 1987; Saether, Ellingsen S. Mohr, 1987). Other work has shown that the krill peptide hydrolases have a similar effect on milk and meat proteins (Osnes, Ellingsen & Mohr, 1986), and on the protein constituents of necrotic wounds (Hellgren, Mohr & Vincent, 1986).
  • the krill peptide hydrolases possess yet another property which is highly valuable and essential for the use of the mixture of krill enzymes for practical purposes.
  • Krill are animals which are characterized by having a simple digestive system, in which the different endo- and exopeptidases apparently act together in the digestive tract. This contrasts the situation in higher animals, in which the individual digestive enzymes operate in anatomically distinct portions of the digestive system.
  • krill In addition to peptide hydrolases, krill contain a number of other enzyme systems required for breaking down polymeric substances in the food ingested. Of these enzymes upases and phosholipases are of particular interest from an industrial point of view.
  • the present invention specifies procedures which utilize the unique properties of specific enzyme systems of krill in industrial processes in a completely novel way. Compared with enzyme processes previously known, the effectiveness of the procedures based on krill enzymes is striking and surprising.
  • the procedures specified in the invention utilize one or more of the following properties of the krill enzymes:
  • compositions of active krill enzymes may be carried out using several different types of compositions of active krill enzymes.
  • the simplest procedure is to utilize the krill enzymes as they occur in situ, i.e., to let whole krill autolyse under proper conditions with the formation of e.g. free amino acids and free fatty acids.
  • Another method may depend on using macerated, whole krill as a source of enzymes in the process or, alternatively, an aqueous extract of krill which should preferably be defatted, and if necessary, also concentrated.
  • the appropriate enzyme systems of krill or, alternatively, specific enzymes of the animals may be isolated and purified by methods well known to the specialist, for instance by procedures based on differences in molecular size, electric charge, types of active sites etc (Osnes & Mohr, 1985a; Osnes S. Mohr, 1985b; Osnes & Mohr, 1986; Osnes et al., 1986).
  • the peptide hydrolases of krill can be used as a very effective means of manufacturing protein concentrates from suitable raw materials of either microbial-, plant- or animal origin.
  • the objective is to anchieve removal of unwanted parts of the raw material, and at the same time secure a concentration of protein and other desirable constituents. It is often an objective to obtain a protein concentrate which is water-soluble.
  • Enzyme technology has been applied to a certain extent within this area, and usually in the form of a partial hydrolysis using proteolytic enzymes of mammalian-, plantor microbial origin (Mohr, 1978; Mohr, 1980).
  • Krill peptide hydrolases hold particular promise in this context, and in particular as regards production of protein concentrates from cheap fish or from fish- or abbatoir by-products.
  • Dietary protein hydrolysates represent a small, but important market segment. Such preparations are used for postoperative patients or for individuals with an impaired digestive system.
  • the hydrolysates may be administered as comparatively crude preparations per os (Clegg, 1978), or as highly purified mixtures of amino acids for intravenous administration.
  • Enzyme hydrolysates of milk proteins have been applied as dietary preparations.
  • conventional enzymes of either microbial-, plant- or animal origin serious problems are encountered, both because the yield of free amino acids may be low, and because a large amount of bitter peptides are formed (Clegg, 1978).
  • Dietary protein hydrolysates made by the application of krill peptide hydrolases represent an important, new area, both due to the high yield of amino acids obtained in the process, and because a very limited amount of bitter peptides is produced.
  • the peptide hydrolases of krill may be applied in effective processes for the manufacture of free amino acids from cheap protein sources.
  • the free amino acids produced in the process may either be prepared as a crude mixture, or further separated into the individual amino acids or groups of individual amino acids by methods well known to the specialist.
  • the present process provides a new alternative to amino acid production by fermentation, and should hold considerable promise, both because the process economy is favourable, and because the process yields the entire range of free amino acids.
  • the essential amino acids are of particular interest in this context, but also other amino acids, e.g. glutamic acid and others, may be of considerable commercial interest.
  • Partial hydrolysis of proteinaceous feed- or foodstuffs can lead to significant improvements in either their digestibility or functional properties. Such improvements are of considerable importance from a practical point of view, for instance in the aquaculture industry.
  • Partial enzymic hydrolysis of suitable feedstuffs can make several protein raw materials suitable as a "start feed” for fish fry.
  • Enzymes from krill are particularly well suited for this application.
  • a particularly interesting aspect of this application is the fact that the krill enzymes can be added to the feed and allowed to act during low-temperature storage at chill temperatures.
  • Partial hydrolyses of protein constituents can also confer improved functional properties to feed- and foodstuffs, by increasing water solubility, emulsifying capacity, foaming ability or texture. In such cases the conditions of hydrolyses have to be specifically adapted to achieve the desired effects. 6. Tenderizing of muscle foods
  • Enzymic tenderization of muscle foods, and in particular meat represents a large market segment, which is presently dominated by plant proteases and certain microbial enzymes. Enzymic maturation and tenderization of fish muscle is also of considerable importance in many countries (Mohr, 1980). Krill enzymes provide an interesting alternative to present enzymic practices within this area.
  • a particularly interesting aspect of krill proteases is the ability of the former to act at temperatures down to freezing. This opens the possibility of achieving artificial tenderizing of meat or fish during chill storage, which is a completely new concept, which has so far not been explored due to the lack fo suitable enzymes.
  • bitter peptides As mentioned above (Clegg, 1978).
  • the bitter peptides occurring in protein hydrolysates may represent a considerable practical problem, as is the case e.g. during the ripening of different types of cheese and in the production of dietary protein hydrolysates.
  • bitterness of hydrolysates is usually due to particular peptides, and expecially those which contain a high proportion of hydrophobic amino acids. Bitterness can be effectively reduced by complete or partial hydrolyses of the bitter peptides.
  • the natural mixture of krill peptide hydrolases, and in particular the exopeptidases of such mixtures, are excellently suited to remove bitter peptides from hydrolysates.
  • debittering based on krill enzymes can also be carried out at low temperature.
  • Protein precipitates may present a considerable problem in certain products such as e.g. beer, because the precipitate causes the product to be hazy. In beer the haziness arises when soluble proteins precipitate during chill storage of the beer.
  • Reduction of the viscosity by partial enzymic hydrolyses of the protein constituents can provide a very effective solution to such problems.
  • One example is the treatment of the stickwater during fishmeal production with proteolytic enzymes. Due to the presence of both endo- and exopeptidases the digestive enzymes of krill can provide a far more efficient viscosity reduction than the bacterial proteases which are presently used for this purpose. Furthermore, the fact that the enzymic step can be carried out at low temperatures offers yet another interesting possibility in the case of the krill enzymes.
  • Peptide hydrolases from krill are particularly interesting in this respect because of their high activity at low temperature. This is particularly important since many of the products in question do not tolerate elevated temperatures because of the adverse effect of heating on sensory properties and hygienic standard.
  • the release of oil from fatty tissues can be significantly improved if the walls of the cells storing the fat are weakened or punctured prior to pressing or extraction. Enzymic treatment constitutes such a method.
  • the application of the effective endo- and exopeptidases of krill is of particular interest.
  • the enzymes should be added to the macerated fatty raw material, and allowed to act for a comparatively short time at low temperature in order to cause a weakening of the cell walls, but without causing extensive hydrolysis of the protein phase, in which case problems may be encountered in the pressing stage. 14. Production of free fatty acids
  • Antarctic krill as well as krill species in the North Atlantic, are characterized by containing high proportions of lipids, including phospholipids.
  • the phospholipids of krill have an unusually high proportion of long-chain w-3 fatty acids (Ellingsen, 1982; Saether et al., 1986b).
  • krill possess a very efficient enzyme apparatus for degrading lipids to free fatty acids.
  • krill lipases and phospholipases presents a highly interesting, new method for producing free fattyacids, either by a process based on controlled autolysis of krill itself, or by letting purified preparations of krill lipases and phospholipases act on a suitable lipid raw material.
  • Such processes present a new, competitive avenue to the manufacture of highly concentrated preparations of fatty acids, and it particular the w-3 fatty acids from marine organisms.
  • Frozen Antarctic krill (Euphausia superba) were thawed, and subsequently treated in a partly thawed state for two periods of each 30 s in a MSE Homogeniser.
  • the macerated krill was used as a source of enzymes according to the invention. Such material will be referred to as "macerated krill”.
  • Frozen Antarctic krill (Euphausia superba) were thawed and macerated as described above. 25 g of the macerated krill were mixed with 50 ml of water, homogenised and centrifuged in the cold (0 °C) for 30 min at 12 500 g. The sediment was resuspended in 50 ml water, homogenised and centrifuged as described above.
  • the combined extracts were added 20 ml of tetrachloromethane and homogenised in the cold. The mixture was centrifuged for 15 min at 2 500 g. The water-phase was removed and extracted once more with tetrachloromethane and centrifuged.
  • the combined, defatted aqueous extracts were freeze dried and used as an enzyme preparation according to the invention.
  • freeze dried krill extract Such preparations will be referred to as "freeze dried krill extract”.
  • Example 1A 25 g of macerated krill (Example 1A) were mixed with 25 ml deionised water and incubated at 50 °C for 20 h at the natural pH of the homogenate. During incubation a major proportion of the krill proteins are broken down, leaving the digestive enzymes intact.
  • the mixture was centrifuged at 13 000 g for 40 min in the cold.
  • the aqueous phase was removed and subjected to ultrafiltration using an Amicon Diaflo Ultrafilter type PM 10.
  • the filter effects retention of material with a molecular weight exceeding 10 000.
  • the high - molecular weight fraction after ultrafiltration containing the digestive enzymes including peptide hydrolases was concentrated, freeze dried and used according to the claims of the invention.
  • the present preparation will be referred to as "purified krill enzymes".
  • the elution profile was monitored spectrophotometrically at 280 nm. Fractions were collected and enzymatically active fractions pooled, dialysed, freeze dried and used as enzyme preparations according to the invention.
  • proteolytic activity was determined using hemoglobin or casein as substrates according to the method of Rick (1974).
  • the fractions collected during gel chromatography corresponded to molecular weights of roughly 20 000-40 000 dalton.
  • Such preparations were used in accordance with the claims of the invention, and will be referred to as "chromatographed preparations of krill enzymes".
  • the mixture was afterwards cooled to 4 °C and centrifuged at 12 000 g for 15 min.
  • the water soluble fraction after centrifugation accounted for approximately 60 % of the dry weight of the cod muscle hydrolysed.
  • the present fish protein concentrate exhibited very good sensory and functional properties.
  • the water soluble fraction was freeze dried.
  • the present beef protein concentrate exhibited very good sensory and functional properties.
  • soy protein isolate 3 g were suspended in 100 ml of deionised water and hydrolysed with 30 mg of "purified krill enzymes" for 120 min at 50 °C and pH 7.5 as outlined in Example: 2A.
  • the hydrolysed soy protein preparation was fxeeze diried.
  • the present soy protein concentrate exhibited very good functional properties, and was very satisfactory from: the point of view of bitterness.
  • Erozen Antarctic krill (Euphausia superba) were thawed and macerated as described in Example 1A. 50 g of macerated krill were placed in a plastic bottle with screw cap and incubated at 50 °C for 20 h at the natural pH of the krill. During this period a considerable proportion of the total protein of the krill was converted to free amino acids.
  • Example 1B 3 g dry weight of macerated capelin (Mallotus villosus) were suspended in 100 ml deionised water. 0.20 g of "freeze dried krill extract" (Example 1B) were added, and the hydrolysis allowed to proceed at pH 7.0 for 20 h at 50 °C. After hydrolysis the mixture was centrifuged at 13 000 g for 40 min in the cold. The aqueous phase after centrifugation was removed and treated as described in Example 4C.
  • Example 4A 25 ml of the aqueous phase arising from autolysis of krill (Example 4A) or from hydrolysis of the fish protein (Example 4B) were treated in an Amicon Diaflo Ultrafiltration Unit using a Diaflo Ultrafilter type YC having a 500 MW cutoff.
  • the low-molecular fraction containing a high proportion of free amino acids was concentrated and freeze dried.
  • the present sample contains a mixture of free amino acids.
  • the preparation is suitable as a source of amino acids in microbial media. This was demonstrated by including the preparation at a concentration of 0.5 % w/v in a microbiological medium instead of Trypton. In separate experiments a Lactobacillus sp. and a Bacillus sp. was inoculated into the medium. The rate of growth was of the same order in the medium containing krill autolysate as in that with Trypton.
  • Frozen capelin (Mallotus villosus) were thawed, macerated and 3 g dry weight suspended in 100 ml deionised water. 0.20 g of "freeze dried krill extract” were added, and the hydrolysis carried out at 50 °C for 20 h at pH 7.0. After hydrolysis the mixture was centrifuged at 13 000 g for 40 min. The aqueous phase was concentrated in a rotary evaporator and freeze dried.
  • the preparation served as a good source of amino acids for the growth of a Lactobacillus sp. and a Bacillus sp.
  • a piece of beef longissimus dorsi muscle weighing approximately 100 g was injected with approximately 10 ml of a 1 % solution of "purified krill enzymes" in water using a syringe.
  • the enzyme was distributed throughout the sample by injecting small amounts enzyme solution into various parts of the muscle.
  • the sample was kept at 10 °C for 1 week. After heating to 80 °C for 10 min to inactivate the enzyme, the piece of meat treated with enzyme was noticeably more tender than a control injected with just water, and stored under the same conditions.
  • the hydrolysate was added 15 mg of "chromatographed krill enzyme", and incubated at 30 °C for 3 hours.
  • the treatment with the krill enzyme significantly reduced the bitterness of the hydrolysate.
  • a sample of raw cows hide was treated with a 2 % solution of "purified krill extract" for 24 h at 30 ° C .
  • the treatment caused effective depilation of the hide.
  • a frozen herring (Clupea harengus) was thawed and placed in a solution containing 0.5 % (w/v) of "freeze dried krill extract". The herring was left in the solution for one week at 5 °C. After this treatment the scales of the fish could easily be brushed off.
  • Frozen capelin (Mallotus villosus) were thawed and placed in a solution containing 2 % (w/v) of "freeze dried krill extract". The fish were left in the solution for one week at 5 °C. The treatment effected a partial breakdown of the skirt, and allowed the remainder of the skin on the fish to be easily removed.
  • Eitazen shrimps (Pandalus borealis) were thawed and placed in a solution containing 2 % (w/v) of "freeze dried krill extract". The shrimps were left in the solution for four days at 5 °C. The shrimps were subsequently heated briefly in hot water. After the present treatment the shells could easily be removed from the shrimps.
  • the kidney from a rat was removed and cut into small pieces.
  • the pieces of the kidney were placed in buffer containing 0.25 % (w/v) of "chromatographed krill enzymes" and 0.01 M EDTA prewarmed to 37 °C.
  • the suspension was gently shaken during the incubation which lasted for 60 min. The procedure resulted in the liberation of individual kidney cells.
  • Frozen herring (Clupea harengus) was thawed and ground in a meat grinder. 25 g of the ground herring were mixed with an equal weight of water. 0.15 g of "freeze dried krill extract" were added, and the mixture incubated for three days at 5 °C. After incubation the mixture was heated to 90 °C for 10 min, and subsequently centrifuged at 13 000 g for 30 min. A distinct oil phase was formed during centrifugation.
  • Frozen herring (Clupea harengus) was thawed and ground in a meat grinder. 25 g of the ground herring were mixed with an equal weight of deionised water, and added 2 g of "freeze dried krill extract". The mixture was incubated at 40 °C for 24 h, during which period free fatty acids were produced. A preparation of free fatty acids was isolated as discribed in Example 15C.

Landscapes

  • Chemical & Material Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Organic Chemistry (AREA)
  • Engineering & Computer Science (AREA)
  • Zoology (AREA)
  • Wood Science & Technology (AREA)
  • Genetics & Genomics (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • General Health & Medical Sciences (AREA)
  • Microbiology (AREA)
  • Biotechnology (AREA)
  • Biochemistry (AREA)
  • General Engineering & Computer Science (AREA)
  • Molecular Biology (AREA)
  • Biomedical Technology (AREA)
  • Medicinal Chemistry (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Meat, Egg Or Seafood Products (AREA)

Abstract

L'invention concerne l'utilisation d'enzymes choisies à partir d'animaux appartenent à l'ordre des euphauciacés. On utilise les enzymes pour modifier les constituants de protéines, peptides et/ou lipides de matières biologiques dans des procédés industriels.
PCT/SE1989/000235 1988-05-05 1989-04-27 Procede de modification de proteines, peptides et/ou lipides au moyen d'enzymes provenant d'euphauciaces Ceased WO1989010960A1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
SE8801701-7 1988-05-05
SE8801701A SE8801701D0 (sv) 1988-05-05 1988-05-05 Production technology based on enzymic method

Publications (1)

Publication Number Publication Date
WO1989010960A1 true WO1989010960A1 (fr) 1989-11-16

Family

ID=20372242

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/SE1989/000235 Ceased WO1989010960A1 (fr) 1988-05-05 1989-04-27 Procede de modification de proteines, peptides et/ou lipides au moyen d'enzymes provenant d'euphauciaces

Country Status (2)

Country Link
SE (1) SE8801701D0 (fr)
WO (1) WO1989010960A1 (fr)

Cited By (20)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1995014489A1 (fr) * 1993-11-22 1995-06-01 Phairson Medical Inc. Composition comprenant des composes utilises comme agent therapeutique
US5422261A (en) * 1993-04-16 1995-06-06 Baxter International Inc. Composition containing collagenase and chymopapain for hydrolyzing connective tissue to isolate cells
EP0729708A1 (fr) * 1995-03-03 1996-09-04 F. Hoffmann-La Roche Ag Utilisation d'enzymes du krill dans les aliments pour animaux
US5670358A (en) * 1995-10-19 1997-09-23 Baxter International Inc. Method for inhibiting chymopapain and papain enzyme activity with polysaccharides of animal origin
WO1998034498A1 (fr) * 1997-02-07 1998-08-13 Biozyme Systems Inc. Procede et appareil de traitement d'hydrolysats de krill
WO1999039589A1 (fr) * 1998-02-09 1999-08-12 Biozyme Systems Inc. Procede et appareil de traitement d'hydrolysats de krill
US6056981A (en) * 1994-02-28 2000-05-02 Biozyme Systems Inc. Euphausiid harvesting and processing method and apparatus
EP0930010A3 (fr) * 1994-02-28 2000-05-17 Biozyme Systems Inc. Procédé et appareil de récolte et de traitement des euphausiaces
US6112699A (en) * 1994-02-28 2000-09-05 Biozyme Systems, Inc. Euphausiid harvesting and processing method and apparatus
WO2003066545A3 (fr) * 2002-02-06 2003-11-27 Green Earth Ind Llc Installation de production d'acides amines
US6960451B2 (en) 2002-02-06 2005-11-01 Green Earth Industries Proteolytic fermenter
US7070953B1 (en) 1999-10-20 2006-07-04 Nordur Ehf Protein hydrolysates produced with the use of cod proteases
WO2007133093A3 (fr) * 2006-05-16 2008-04-10 Biozymatic Sus Procédé de décomposition de déchets organiques
CN104302190A (zh) * 2012-05-17 2015-01-21 长濑化成株式会社 食品素材改性用酶制剂
US9028877B2 (en) 2007-03-28 2015-05-12 Aker Biomarine Antarctic As Bioeffective krill oil compositions
US9220735B2 (en) 2007-03-28 2015-12-29 Aker Biomarine Antarctic As Methods of using krill oil to treat risk factors for cardiovascular, metabolic, and inflammatory disorders
US9867856B2 (en) 2014-01-10 2018-01-16 Aker Biomarine Antarctic As Phospholipid compositions and their preparation
US10456412B2 (en) 2015-02-11 2019-10-29 Aker Biomarine Antarctic As Lipid extraction processes
US10704011B2 (en) 2013-06-14 2020-07-07 Aker Biomarine Antarctic As Lipid extraction processes
US10864223B2 (en) 2015-02-11 2020-12-15 Aker Biomarine Antarctic As Lipid compositions

Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1984001715A1 (fr) * 1982-10-25 1984-05-10 Hellgren Lars G I Composition enzymatique pour nettoyage therapeutique et/ou non therapeutique, utilisation et preparation de la composition
WO1985004809A1 (fr) * 1984-04-24 1985-11-07 Hellgren Lars G I Composition enzymatique servant de promoteur de la digestion a differents niveaux des voies digestives et procede pour faciliter la digestion

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1984001715A1 (fr) * 1982-10-25 1984-05-10 Hellgren Lars G I Composition enzymatique pour nettoyage therapeutique et/ou non therapeutique, utilisation et preparation de la composition
WO1985004809A1 (fr) * 1984-04-24 1985-11-07 Hellgren Lars G I Composition enzymatique servant de promoteur de la digestion a differents niveaux des voies digestives et procede pour faciliter la digestion

Non-Patent Citations (3)

* Cited by examiner, † Cited by third party
Title
CHEMICAL ABSTRACTS, Vol. 105, (1986), abstract No. 72633t, Experientia 1986, 42(4), 403-4 (Eng). *
COMP. BIOCHEM. PHYSIOL., Vol. 83B, No. 4, 1986, pages 801-805, (KNUT KR. OSNES et al.), "Hydrolysis of proteins by peptide hydrolases of antarctic krill, euphausia superba", see page 805. *
PROCESS BIOCHEMISTRY, Vol. 14, October 1979, pages 17-19, (T ELLINGSEN and V MOHR), "A new process for the utilization of antarctic krill". *

Cited By (38)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5422261A (en) * 1993-04-16 1995-06-06 Baxter International Inc. Composition containing collagenase and chymopapain for hydrolyzing connective tissue to isolate cells
US5424208A (en) * 1993-04-16 1995-06-13 Baxter International Inc. Method for isolating cells from tissue with a composition containing collagenase and chymopapin
WO1995014489A1 (fr) * 1993-11-22 1995-06-01 Phairson Medical Inc. Composition comprenant des composes utilises comme agent therapeutique
US6056981A (en) * 1994-02-28 2000-05-02 Biozyme Systems Inc. Euphausiid harvesting and processing method and apparatus
US6112699A (en) * 1994-02-28 2000-09-05 Biozyme Systems, Inc. Euphausiid harvesting and processing method and apparatus
EP0930010A3 (fr) * 1994-02-28 2000-05-17 Biozyme Systems Inc. Procédé et appareil de récolte et de traitement des euphausiaces
EP0729708A1 (fr) * 1995-03-03 1996-09-04 F. Hoffmann-La Roche Ag Utilisation d'enzymes du krill dans les aliments pour animaux
US5670358A (en) * 1995-10-19 1997-09-23 Baxter International Inc. Method for inhibiting chymopapain and papain enzyme activity with polysaccharides of animal origin
US6555155B2 (en) 1996-10-21 2003-04-29 Biozyme Systems, Inc. Method and apparatus for harvesting, digestion and dehydrating of krill hydrolysates and co-drying and processing of such hydrolysates
WO1998034498A1 (fr) * 1997-02-07 1998-08-13 Biozyme Systems Inc. Procede et appareil de traitement d'hydrolysats de krill
WO1999039589A1 (fr) * 1998-02-09 1999-08-12 Biozyme Systems Inc. Procede et appareil de traitement d'hydrolysats de krill
US7070953B1 (en) 1999-10-20 2006-07-04 Nordur Ehf Protein hydrolysates produced with the use of cod proteases
WO2003066545A3 (fr) * 2002-02-06 2003-11-27 Green Earth Ind Llc Installation de production d'acides amines
US6960451B2 (en) 2002-02-06 2005-11-01 Green Earth Industries Proteolytic fermenter
WO2007133093A3 (fr) * 2006-05-16 2008-04-10 Biozymatic Sus Procédé de décomposition de déchets organiques
US9072752B1 (en) 2007-03-28 2015-07-07 Aker Biomarine Antarctic As Bioeffective krill oil compositions
US9730966B2 (en) 2007-03-28 2017-08-15 Aker Biomarine Antartic As Method of reducing appetite in a human subject comprising administering krill oil composition
US9034388B2 (en) 2007-03-28 2015-05-19 Aker Biomarine Antartic As Bioeffective krill oil compositions
US11865143B2 (en) 2007-03-28 2024-01-09 Aker Biomarine Antarctic As Bioeffective krill oil compositions
US9078905B2 (en) 2007-03-28 2015-07-14 Aker Biomarine Antarctic As Bioeffective krill oil compositions
US9119864B2 (en) 2007-03-28 2015-09-01 Aker Biomarine Antarctic As Bioeffective krill oil compositions
US9220735B2 (en) 2007-03-28 2015-12-29 Aker Biomarine Antarctic As Methods of using krill oil to treat risk factors for cardiovascular, metabolic, and inflammatory disorders
US9320765B2 (en) 2007-03-28 2016-04-26 Aker Biomarine Antarctic As Bioeffective krill oil compositions
US9375453B2 (en) 2007-03-28 2016-06-28 Aker Biomarine Antarctic As Methods for producing bioeffective krill oil compositions
US9644170B2 (en) 2007-03-28 2017-05-09 Aker Biomarine Antarctic As Bioeffective krill oil compositions
US9644169B2 (en) 2007-03-28 2017-05-09 Aker Biomarine Antarctic As Bioeffective krill oil compositions
US9028877B2 (en) 2007-03-28 2015-05-12 Aker Biomarine Antarctic As Bioeffective krill oil compositions
US9816046B2 (en) 2007-03-28 2017-11-14 Aker Biomarine Antarctic As Bioeffective krill oil compositions
US10543237B2 (en) 2007-03-28 2020-01-28 Aker Biomarine Antarctic As Bioeffective krill oil compositions
US9889163B2 (en) 2007-03-28 2018-02-13 Aker Biomarine Antarctic As Bioeffective krill oil compositions
US10010567B2 (en) 2007-03-28 2018-07-03 Aker Biomarine Antarctic As Bioeffective krill oil compositions
CN104302190A (zh) * 2012-05-17 2015-01-21 长濑化成株式会社 食品素材改性用酶制剂
US10704011B2 (en) 2013-06-14 2020-07-07 Aker Biomarine Antarctic As Lipid extraction processes
US11578289B2 (en) 2013-06-14 2023-02-14 Aker Biomarine Antarctic As Lipid extraction processes
US9867856B2 (en) 2014-01-10 2018-01-16 Aker Biomarine Antarctic As Phospholipid compositions and their preparation
US10456412B2 (en) 2015-02-11 2019-10-29 Aker Biomarine Antarctic As Lipid extraction processes
US10864223B2 (en) 2015-02-11 2020-12-15 Aker Biomarine Antarctic As Lipid compositions
US11819509B2 (en) 2015-02-11 2023-11-21 Aker Biomarine Antarctic As Lipid compositions

Also Published As

Publication number Publication date
SE8801701D0 (sv) 1988-05-05

Similar Documents

Publication Publication Date Title
WO1989010960A1 (fr) Procede de modification de proteines, peptides et/ou lipides au moyen d'enzymes provenant d'euphauciaces
EP1227736B1 (fr) Hydrolysats proteiques obtenus a partir de proteases marines
Gildberg Recovery of proteinases and protein hydrolysates from fish viscera
JP3153237B2 (ja) タンパク質加水分解物
Mora et al. Possible uses of processed slaughter byproducts
JP3712130B2 (ja) 凝固を引き起こさずにその中の微生物を殺すための水性タンパク質溶液の処理方法
WO2001028353A1 (fr) Hydrolysats proteiques obtenus a partir de proteases marines
KRISTINSSON et al. Hydrolysis of salmon muscle proteins by an enzyme mixture extracted from Atlantic salmon (Salmo salar) pyloric caeca
JP3325892B2 (ja) 肉加水分解産物の製造方法及び肉加水分解産物の使用
JP2000001499A (ja) 生物活性を有するペプチド、その用途、およびその製造方法
Estiasih et al. Valorisation of viscera from fish processing for food industry utilizations
Williams et al. Application of the plastein reaction to mycoprotein: I. Plastein synthesis
KR950013948B1 (ko) 쓴맛 폴리펩티드를 함유하는 효소적으로 가수분해된 단백질의 쓴맛을 없애는 방법
Yuliatmo et al. Increasing of angiotensin converting enzyme inhibitory derived from Indonesian native chicken leg protein using Bacillus cereus protease enzyme.
WO2001018229A1 (fr) Procede de production d'hydrolysats proteiques a partir de peptone animale et procede de conservation de muqueuse
Ledward et al. Recovery and utilisation of by‐product proteins of the meat industry
RU2132142C1 (ru) Способ получения белкового гидролизата из мясного и мясокостного сырья убойных животных
Leonid et al. Production of herbal protein isolates with the enzymatic hydrolysis technology
Abdulazeez et al. Production and antioxidant properties of protein hydrolysate from Rastrelliger kanagurta (Indian mackerel).
KR101837118B1 (ko) 박테리아 배양 산물을 이용한 콜라겐의 추출 방법
JP2804220B2 (ja) 食用骨粉の製造法
JP2001178398A (ja) 発酵調味料及びその製造方法
Bazhenovа et al. Preparation of the enzyme solution from the whole bovine abomasum for modification of properties of the collagen containing rumen
CA1325133C (fr) Mode de preparation de substances sapides consistant principalement en peptides de faible poids moleculaire
García-Carrerño et al. Langostilla (Pleuroncondes planipes) as a source of protein hydrolysate and carotenoprotein

Legal Events

Date Code Title Description
AK Designated states

Kind code of ref document: A1

Designated state(s): JP US

AL Designated countries for regional patents

Kind code of ref document: A1

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