NO845059L - PROCEDURE FOR PREPARING ALGINATES WITH CHANGED PHYSICAL PROPERTIES AND USING THESE ALGINATES. - Google Patents
PROCEDURE FOR PREPARING ALGINATES WITH CHANGED PHYSICAL PROPERTIES AND USING THESE ALGINATES.Info
- Publication number
- NO845059L NO845059L NO845059A NO845059A NO845059L NO 845059 L NO845059 L NO 845059L NO 845059 A NO845059 A NO 845059A NO 845059 A NO845059 A NO 845059A NO 845059 L NO845059 L NO 845059L
- Authority
- NO
- Norway
- Prior art keywords
- alginates
- alginate
- physical properties
- epimerase
- gels
- Prior art date
Links
- 229920000615 alginic acid Polymers 0.000 title claims description 32
- 238000000034 method Methods 0.000 title claims description 9
- 230000000704 physical effect Effects 0.000 title claims description 5
- 235000010443 alginic acid Nutrition 0.000 claims description 29
- 108090000790 Enzymes Proteins 0.000 claims description 19
- 102000004190 Enzymes Human genes 0.000 claims description 19
- 239000000499 gel Substances 0.000 claims description 17
- FHVDTGUDJYJELY-UHFFFAOYSA-N 6-{[2-carboxy-4,5-dihydroxy-6-(phosphanyloxy)oxan-3-yl]oxy}-4,5-dihydroxy-3-phosphanyloxane-2-carboxylic acid Chemical compound O1C(C(O)=O)C(P)C(O)C(O)C1OC1C(C(O)=O)OC(OP)C(O)C1O FHVDTGUDJYJELY-UHFFFAOYSA-N 0.000 claims description 16
- 229940072056 alginate Drugs 0.000 claims description 15
- 238000002360 preparation method Methods 0.000 claims description 10
- 241000589149 Azotobacter vinelandii Species 0.000 claims description 7
- 210000004027 cell Anatomy 0.000 claims description 6
- 108090001066 Racemases and epimerases Proteins 0.000 claims description 4
- 241000199919 Phaeophyceae Species 0.000 claims description 3
- 150000001768 cations Chemical class 0.000 claims description 3
- 108010084926 mannuronan c-5-epimerase Proteins 0.000 claims description 3
- 241000894006 Bacteria Species 0.000 claims description 2
- 239000011942 biocatalyst Substances 0.000 claims description 2
- 239000003094 microcapsule Substances 0.000 claims description 2
- 210000003463 organelle Anatomy 0.000 claims description 2
- AEMOLEFTQBMNLQ-UHFFFAOYSA-N beta-D-galactopyranuronic acid Natural products OC1OC(C(O)=O)C(O)C(O)C1O AEMOLEFTQBMNLQ-UHFFFAOYSA-N 0.000 description 6
- AEMOLEFTQBMNLQ-BZINKQHNSA-N D-Guluronic Acid Chemical compound OC1O[C@H](C(O)=O)[C@H](O)[C@@H](O)[C@H]1O AEMOLEFTQBMNLQ-BZINKQHNSA-N 0.000 description 5
- 239000011575 calcium Substances 0.000 description 5
- 238000006345 epimerization reaction Methods 0.000 description 5
- IXPNQXFRVYWDDI-UHFFFAOYSA-N 1-methyl-2,4-dioxo-1,3-diazinane-5-carboximidamide Chemical compound CN1CC(C(N)=N)C(=O)NC1=O IXPNQXFRVYWDDI-UHFFFAOYSA-N 0.000 description 4
- 239000002253 acid Substances 0.000 description 4
- 235000010413 sodium alginate Nutrition 0.000 description 4
- 239000000661 sodium alginate Substances 0.000 description 4
- 229940005550 sodium alginate Drugs 0.000 description 4
- HOPRXXXSABQWAV-UHFFFAOYSA-N anhydrous collidine Natural products CC1=CC=NC(C)=C1C HOPRXXXSABQWAV-UHFFFAOYSA-N 0.000 description 3
- 125000002091 cationic group Chemical group 0.000 description 3
- UTBIMNXEDGNJFE-UHFFFAOYSA-N collidine Natural products CC1=CC=C(C)C(C)=N1 UTBIMNXEDGNJFE-UHFFFAOYSA-N 0.000 description 3
- 150000002500 ions Chemical class 0.000 description 3
- 229920000642 polymer Polymers 0.000 description 3
- 239000011148 porous material Substances 0.000 description 3
- 238000004611 spectroscopical analysis Methods 0.000 description 3
- GFYHSKONPJXCDE-UHFFFAOYSA-N sym-collidine Natural products CC1=CN=C(C)C(C)=C1 GFYHSKONPJXCDE-UHFFFAOYSA-N 0.000 description 3
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 2
- 108010093096 Immobilized Enzymes Proteins 0.000 description 2
- IAJILQKETJEXLJ-SQOUGZDYSA-N L-guluronic acid Chemical compound O=C[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(O)=O IAJILQKETJEXLJ-SQOUGZDYSA-N 0.000 description 2
- 241001598113 Laminaria digitata Species 0.000 description 2
- 150000007513 acids Chemical class 0.000 description 2
- 229910052791 calcium Inorganic materials 0.000 description 2
- AEMOLEFTQBMNLQ-YBSDWZGDSA-N d-mannuronic acid Chemical compound O[C@@H]1O[C@@H](C(O)=O)[C@H](O)[C@@H](O)[C@H]1O AEMOLEFTQBMNLQ-YBSDWZGDSA-N 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 238000005538 encapsulation Methods 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 244000000000 soil microbiome Species 0.000 description 2
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 241000195493 Cryptophyta Species 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- JVTAAEKCZFNVCJ-UHFFFAOYSA-M Lactate Chemical compound CC(O)C([O-])=O JVTAAEKCZFNVCJ-UHFFFAOYSA-M 0.000 description 1
- 241000296380 Laminaria hyperborea Species 0.000 description 1
- 241001491705 Macrocystis pyrifera Species 0.000 description 1
- -1 Na<+> Chemical class 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 238000011138 biotechnological process Methods 0.000 description 1
- 235000010410 calcium alginate Nutrition 0.000 description 1
- 239000000648 calcium alginate Substances 0.000 description 1
- 229960002681 calcium alginate Drugs 0.000 description 1
- OKHHGHGGPDJQHR-YMOPUZKJSA-L calcium;(2s,3s,4s,5s,6r)-6-[(2r,3s,4r,5s,6r)-2-carboxy-6-[(2r,3s,4r,5s,6r)-2-carboxylato-4,5,6-trihydroxyoxan-3-yl]oxy-4,5-dihydroxyoxan-3-yl]oxy-3,4,5-trihydroxyoxane-2-carboxylate Chemical compound [Ca+2].O[C@@H]1[C@H](O)[C@H](O)O[C@@H](C([O-])=O)[C@H]1O[C@H]1[C@@H](O)[C@@H](O)[C@H](O[C@H]2[C@H]([C@@H](O)[C@H](O)[C@H](O2)C([O-])=O)O)[C@H](C(O)=O)O1 OKHHGHGGPDJQHR-YMOPUZKJSA-L 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000010924 continuous production Methods 0.000 description 1
- 230000009144 enzymatic modification Effects 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 238000001879 gelation Methods 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 125000005613 guluronic acid group Chemical group 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 229920000867 polyelectrolyte Polymers 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000008719 thickening Effects 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P19/00—Preparation of compounds containing saccharide radicals
- C12P19/24—Preparation of compounds containing saccharide radicals produced by the action of an isomerase, e.g. fructose
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/02—Enzymes or microbial cells immobilised on or in an organic carrier
- C12N11/10—Enzymes or microbial cells immobilised on or in an organic carrier the carrier being a carbohydrate
Landscapes
- Organic Chemistry (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Health & Medical Sciences (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Enzymes And Modification Thereof (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
Description
Den foreliggende oppfinnelse er knyttet til fremstilling av alginater med forbedrede fysikalske egenskaper, særlig med hensyn til å danne gel med uorganiske eller polyvalente, organiske ioner. Disse modifiserte alginatene skal anvendes for immobilisering/innkapsling av enzymer og/eller celler til bruk i bioteknologiske prosesser. The present invention relates to the production of alginates with improved physical properties, particularly with regard to forming gels with inorganic or polyvalent organic ions. These modified alginates are to be used for immobilisation/encapsulation of enzymes and/or cells for use in biotechnological processes.
Alginatgeler som immobiliseringsmateriale har flere svakheter, hvorav to vesentlige skal nevnes: Alginate gels as an immobilization material have several weaknesses, of which two significant ones should be mentioned:
1) Kalsium-alginatgeler destabiliseres av forbindelser1) Calcium-alginate gels are destabilized by compounds
med affinitetet for kalsium, f.eks. EDTA, citrat, laktat og fosfat, samt av høye konsentrasjoner av kationer som Na<+>, K<+>with affinity for calcium, e.g. EDTA, citrate, lactate and phosphate, as well as high concentrations of cations such as Na<+>, K<+>
og Mgand Mg
2) Alginater som anvendes idag har en høy grad av kjemisk heterogenitet og gir geler med så store porer at proteiner - enzymer og andre makromolekyler - kan lekke ut, samtidig som størrelsefordelingen av porene er vanskelig å kontrollere. 2) Alginates used today have a high degree of chemical heterogeneity and produce gels with such large pores that proteins - enzymes and other macromolecules - can leak out, while the size distribution of the pores is difficult to control.
Alginat er det viktigste strukturpolysakkarid i marine brunalger og benyttes til en rekke industrielle formål, hvor man utnytter polymerens egenskaper som polyelektrolytt, f.eks. til geldannelse og fortykning, samt dens evne til vann- og ionebinding. Alginate is the most important structural polysaccharide in marine brown algae and is used for a number of industrial purposes, where the polymer's properties as a polyelectrolyte are exploited, e.g. for gelation and thickening, as well as its ability to bind water and ions.
Oppfinnelsens formål er derfor å fremstille alginater med fysikalske egenskaper som tilfredsstiller kravene til øket gelstyrke og stabilitet og bedre kontrollerbar porestørrelse. The purpose of the invention is therefore to produce alginates with physical properties that satisfy the requirements for increased gel strength and stability and better controllable pore size.
Kjemisk sett er alginat et polyuronid bygget opp av to uronsyrer D-mannuronsyre (M) og C-5-epimeren L-guluronsyre (G). Disse er ordnet på en slik måte at polymeren videre er bygget opp av tre typer sekvenser: (G)-rike sekvenser betegnet G-blokker, (M)-rike sekvenser betegnet M-blokker og alter-nerende struktur symbolisert som (MGMGMG). Chemically speaking, alginate is a polyuronide made up of two uronic acids D-mannuronic acid (M) and the C-5 epimer L-guluronic acid (G). These are arranged in such a way that the polymer is further built up of three types of sequences: (G)-rich sequences denoted G-blocks, (M)-rich sequences denoted M-blocks and alternating structure symbolized as (MGMGMG).
Alginatets evne til å danne gel ved ionebinding og denne gelens egenskaper avhenger både av det relative innhold av de to uronsyrene og av fordelingen av guluronsyre-enhetene langs kjeden. Et høyt innhold av (G)-blokker gir f.eks. et alginat med stor evne til geldannelse, noe som teknisk sett er en verdifull egenskap ved polymeren. The alginate's ability to form a gel by ion binding and the properties of this gel depend both on the relative content of the two uronic acids and on the distribution of the guluronic acid units along the chain. A high content of (G)-blocks gives e.g. an alginate with great ability to gel, which technically is a valuable property of the polymer.
Foreliggende oppfinnelse er basert på følgende:The present invention is based on the following:
Alginatet syntetiseres i algen som polymannuronsyre og modifiseres deretter av et enzym, mannuronan~C-5-epimerase som endrer D-mannuronsyre-rester til L-guluronsyre-rester inne i kjeden. Når dette enzymet virker på alginat, vil både det relative innhold og uronsyresekvensen bli forandret, og dermed de fysikalske egenskapene. The alginate is synthesized in the algae as polymannuronic acid and is then modified by an enzyme, mannuronan~C-5-epimerase, which changes D-mannuronic acid residues to L-guluronic acid residues inside the chain. When this enzyme acts on alginate, both the relative content and the uronic acid sequence will be changed, and thus the physical properties.
Oppfinnelsen vedrører således en fremgangsmåte for fremstilling av alginater med forbedrede fysikalske genskaper ved bruk av enzymatisk modifikasjon på polymert nivå. Fremgangsmåten erkarakterisert vedat alginater utvunnet fra brunalger eller bakterier inokuleres med et enzympreparat. The invention thus relates to a method for producing alginates with improved physical characteristics using enzymatic modification at the polymeric level. The method is characterized by the fact that alginates extracted from brown algae or bacteria are inoculated with an enzyme preparation.
Som enzympreparat anvendes fortrinnsvis et C-5-epimerase-preparat, særlig en alginat-lyase-fri mannuronan-C-5-epimerase fremstilt fra jordbakterien Azotobacter vinelandii. A C-5 epimerase preparation is preferably used as an enzyme preparation, in particular an alginate lyase-free mannuronan C-5 epimerase produced from the soil bacterium Azotobacter vinelandii.
Oppfinnelsen omfatter også anvendelse av de modifiserte alginater til immobilisering av enzymer, celleorganeller og celler ved innfangning i geler av alginat eller av alginat med egnede kationer, samt immobilisering av biokatalysatorer ved innkapsling i alginat-polykation-mikrokapsler. The invention also includes the use of the modified alginates for immobilization of enzymes, cell organelles and cells by entrapment in gels of alginate or of alginate with suitable cations, as well as immobilization of biocatalysts by encapsulation in alginate-polycation microcapsules.
Mannuronan-C-5-epimerasen kan isoleres fra kulturer av jordbakterien Azotobacter vinelandii som produserer både-alginat og epimerasen ekstracellulært. Det at enzymet er ekstracellulært er en stor fordel ved isolering, og det indi-kerer også at enzymet kan fungere fritt i løsning uavhengig av intracellulære faktorer, noe som er gunstig med tanke på teknisk utnyttelse. The mannuronan-C-5 epimerase can be isolated from cultures of the soil bacterium Azotobacter vinelandii which produces both alginate and the epimerase extracellularly. The fact that the enzyme is extracellular is a major advantage for isolation, and it also indicates that the enzyme can function freely in solution independent of intracellular factors, which is favorable in terms of technical utilization.
Anvendelse av immobiliserte enzymer som katalysatorer har fått en stadig større industriell betydning og vil i de kommende år være et av de viktigste ekspansjonsområder for bioteknologien. Immobiliserte enzymer er ofte mer stabile, The use of immobilized enzymes as catalysts has become increasingly important industrially and will in the coming years be one of the most important areas of expansion for biotechnology. Immobilized enzymes are often more stable,
men først og fremst er de lettere å håndtere enn frie, løselige enzymer og kan anvendes i kontinuerlige prosesser. but primarily they are easier to handle than free, soluble enzymes and can be used in continuous processes.
Ved siden av immobilisering av enkle enzymer er det også utviklet teknikker for immobilisering av hele celler. Cellene kan tjene som bærer for et enkelt enzym, slik at isolering av enzymet er unødvendig før immobilisering, eller også kan man benytte flere enzymer i cellen til å katalysere prosesser i flere trinn (f.eks. syntese av hormoner, proteiner etc). Alongside the immobilization of simple enzymes, techniques have also been developed for the immobilization of whole cells. The cells can serve as a carrier for a single enzyme, so that isolation of the enzyme is unnecessary before immobilization, or several enzymes can be used in the cell to catalyze processes in several steps (e.g. synthesis of hormones, proteins, etc.).
Vi har undersøkt epimerisering av en rekke høypolymere alge- og bakteriealginater med varierende blokkstruktur og sammensetning, og konklusjonene er at samtlige alginater lar seg epimerisere i betydelig grad. Epimeriseringsgraden varierer We have investigated the epimerization of a number of highly polymeric algal and bacterial alginates with varying block structure and composition, and the conclusions are that all alginates can be epimerized to a significant extent. The degree of epimerization varies
fra 60 til 90% avhengig av alginatenes opprinnelige blokkstruktur og for enkelte alginater gir dette mer enn en for-dobling av gelstyrken målt i 2% homogene Ca-alginatgeler. from 60 to 90% depending on the original block structure of the alginates and for some alginates this gives more than a doubling of the gel strength measured in 2% homogeneous Ca-alginate gels.
EksemplerExamples
Eksempel 1Example 1
Natrium-alginat fra Laminaria digitata, i en mengde av 0,07 vekt%, ble oppløst i kationisk buffer, 0,05M kollidin pH 7,0 og Ca 6,8mM. Dette ble inkubert med lyase-fritt C-5-epimerase-preparat fra A. vinelandii ved 30°C i 8 timer. Epimeriseringsgraden, målt ved hjelp av høyoppløselig n.m.r.-spektroskopi, viser en økning i guluronsyreinnhold fra 41% til 69% (se tabell) . Sodium alginate from Laminaria digitata, in an amount of 0.07% by weight, was dissolved in cationic buffer, 0.05M collidine pH 7.0 and Ca 6.8mM. This was incubated with lyase-free C-5-epimerase preparation from A. vinelandii at 30°C for 8 hours. The degree of epimerization, measured using high-resolution n.m.r. spectroscopy, shows an increase in guluronic acid content from 41% to 69% (see table).
Eksempel 2Example 2
Natrium-alginat fra Macrocystis pyrifera, i en mengde av 0,07 vekt%, ble oppløst i kationisk buffer, 0,05M kollidin pH 7,0 og Ca 6,8mM. Dette ble inkubert med lyase-fritt C-5-epimerase-preparat fra A. vinelandii ved 30°C i 8 timer. Epimeriseringsgraden, målt ved hjelp av høyoppløselig n.m.r.-spektroskopi, viser en økning i guluronsyreinnhold fra 37% til 62%. (Se tabell). Sodium alginate from Macrocystis pyrifera, in an amount of 0.07% by weight, was dissolved in cationic buffer, 0.05M collidine pH 7.0 and Ca 6.8mM. This was incubated with lyase-free C-5-epimerase preparation from A. vinelandii at 30°C for 8 hours. The degree of epimerization, measured by high-resolution n.m.r. spectroscopy, shows an increase in guluronic acid content from 37% to 62%. (See table).
Eksempel 3Example 3
Natrium-alginat fra Laminaria hyperborea, i en mengde av 0,07 vekt%, ble oppløst i kationisk buffer, 0,05M kollidin pH Sodium alginate from Laminaria hyperborea, in an amount of 0.07% by weight, was dissolved in cationic buffer, 0.05M collidine pH
2+ 2+
7,0 og Ca 6,8mM. Dette ble inkubert med lyase-fritt C-5-epi-merase-preparat fra A. vinelandii ved 30°C i 8 timer. Epimeriseringsgraden, målt ved hjelp av høyoppløselig n.m.r.-spektroskopi, viser en økning i guluronsyreinnhold fra 68% til 79%. (Se tabell). 7.0 and about 6.8mM. This was incubated with lyase-free C-5 epimerase preparation from A. vinelandii at 30°C for 8 hours. The degree of epimerization, measured by high-resolution n.m.r. spectroscopy, shows an increase in guluronic acid content from 68% to 79%. (See table).
Eksempel 4Example 4
Natrium-alginat fra Laminaria digitata som inneholder 40% guluronsyre, behandles med C-5-epimerase fra A. vinelandii pH 7,0 og Ca<2+>0,68mM i 6 timer ved 30°C. Det modifiserte alginatet inneholder 63% guluronsyre. Gelstyrke-målinger av homogene 2% kalsiumgeler viser en gelstyrke på 3,8 N/cm 2 og 9,6 N/cm 2 i henholdsvis nativt og enzym-modifisert alginat. Sodium alginate from Laminaria digitata containing 40% guluronic acid is treated with C-5-epimerase from A. vinelandii pH 7.0 and Ca<2+>0.68mM for 6 hours at 30°C. The modified alginate contains 63% guluronic acid. Gel strength measurements of homogeneous 2% calcium gels show a gel strength of 3.8 N/cm 2 and 9.6 N/cm 2 in native and enzyme-modified alginate, respectively.
(Se figur 1).(See Figure 1).
Claims (5)
Priority Applications (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| NO845059A NO845059L (en) | 1984-12-17 | 1984-12-17 | PROCEDURE FOR PREPARING ALGINATES WITH CHANGED PHYSICAL PROPERTIES AND USING THESE ALGINATES. |
| EP19860900291 EP0204805A1 (en) | 1984-12-17 | 1985-12-16 | Process for producing alginates having improved physical properties, and the use of said alginates |
| PCT/NO1985/000080 WO1986003781A1 (en) | 1984-12-17 | 1985-12-16 | Process for producing alginates having improved physical properties, and the use of said alginates |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| NO845059A NO845059L (en) | 1984-12-17 | 1984-12-17 | PROCEDURE FOR PREPARING ALGINATES WITH CHANGED PHYSICAL PROPERTIES AND USING THESE ALGINATES. |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NO845059L true NO845059L (en) | 1986-06-18 |
Family
ID=19887997
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO845059A NO845059L (en) | 1984-12-17 | 1984-12-17 | PROCEDURE FOR PREPARING ALGINATES WITH CHANGED PHYSICAL PROPERTIES AND USING THESE ALGINATES. |
Country Status (3)
| Country | Link |
|---|---|
| EP (1) | EP0204805A1 (en) |
| NO (1) | NO845059L (en) |
| WO (1) | WO1986003781A1 (en) |
Families Citing this family (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| NO160374C (en) * | 1986-10-17 | 1989-04-12 | Protan As | PROCEDURE FOR MODIFICATION OF ALGINATES (POLYURONIDES) TO GET CHANGED PHYSICAL PROPERTIES. |
| GB9221163D0 (en) * | 1992-10-08 | 1992-11-25 | Nobipol And Protan Biopolymer | Dna compounds |
| FR2849056B1 (en) * | 2002-12-19 | 2007-07-13 | Centre Nat Rech Scient | MANNURONANE C5-EPIMERASES OF BROWN ALGAE, METHODS OF OBTAINING AND USES |
| NO320691B1 (en) * | 2004-06-14 | 2006-01-16 | Ntnu Technology Transfer As | New contrast release system. |
| JP2008519595A (en) * | 2004-11-12 | 2008-06-12 | エフエムシー バイオポリマー エイエス | Modified alginate and production method and use thereof |
| EP2048943B1 (en) | 2006-07-04 | 2014-09-03 | Spermvital AS | Preservation and controlled delivery/ release of spermatozoa |
| US9540630B2 (en) | 2008-09-17 | 2017-01-10 | Beta O2 Technologies Ltd. | Optimization of alginate encapsulation of islets for transplantation |
| US9446168B2 (en) | 2010-06-07 | 2016-09-20 | Beta-O2 Technologies Ltd. | Multiple-layer immune barrier for donor cells |
| EP4083074A1 (en) | 2011-06-02 | 2022-11-02 | Massachusetts Institute Of Technology | Modified alginates for cell encapsulation and cell therapy |
| GB201120368D0 (en) | 2011-11-24 | 2012-01-04 | Sperm Vital As | Methods for the preparation of hydrogels |
| DK3547834T3 (en) | 2016-12-05 | 2021-11-08 | Spermvital As | COMPOSITION WITH LONG-TERM RELEASE |
| JP7510355B2 (en) | 2018-06-04 | 2024-07-03 | スパームヴァイタル アクティーゼルスカブ | Functionalization kit for preparing hydrogels |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SU742434A1 (en) * | 1978-10-11 | 1980-06-25 | Ленинградский ордена Трудового Красного Знамени институт текстильной и легкой промышленности им.С.М.Кирова | Method of preparing immobilized peroxydase |
| JPS5974984A (en) * | 1982-10-21 | 1984-04-27 | Sumitomo Chem Co Ltd | Preparation of immobilized enzyme or microorganism |
-
1984
- 1984-12-17 NO NO845059A patent/NO845059L/en unknown
-
1985
- 1985-12-16 WO PCT/NO1985/000080 patent/WO1986003781A1/en unknown
- 1985-12-16 EP EP19860900291 patent/EP0204805A1/en not_active Withdrawn
Also Published As
| Publication number | Publication date |
|---|---|
| WO1986003781A1 (en) | 1986-07-03 |
| EP0204805A1 (en) | 1986-12-17 |
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