CS224911B1 - The enzyme degradation method of the pectin substances - Google Patents
The enzyme degradation method of the pectin substances Download PDFInfo
- Publication number
- CS224911B1 CS224911B1 CS434682A CS434682A CS224911B1 CS 224911 B1 CS224911 B1 CS 224911B1 CS 434682 A CS434682 A CS 434682A CS 434682 A CS434682 A CS 434682A CS 224911 B1 CS224911 B1 CS 224911B1
- Authority
- CS
- Czechoslovakia
- Prior art keywords
- enzyme
- pectin substances
- pectin
- degradation method
- enzyme degradation
- Prior art date
Links
- 108090000790 Enzymes Proteins 0.000 title claims description 22
- 102000004190 Enzymes Human genes 0.000 title claims description 22
- 229920001277 pectin Polymers 0.000 title claims description 13
- 235000010987 pectin Nutrition 0.000 title claims description 12
- 239000001814 pectin Substances 0.000 title claims description 12
- 239000000126 substance Substances 0.000 title claims description 12
- 238000000034 method Methods 0.000 title claims description 8
- 230000015556 catabolic process Effects 0.000 title description 7
- 238000006731 degradation reaction Methods 0.000 title description 7
- 230000002351 pectolytic effect Effects 0.000 claims description 7
- 230000007515 enzymatic degradation Effects 0.000 claims description 5
- -1 polyethylene terephthalate Polymers 0.000 claims description 5
- 229920000139 polyethylene terephthalate Polymers 0.000 claims description 5
- 239000005020 polyethylene terephthalate Substances 0.000 claims description 5
- 238000002360 preparation method Methods 0.000 claims description 5
- 150000001991 dicarboxylic acids Chemical class 0.000 claims description 2
- 150000002009 diols Chemical class 0.000 claims description 2
- 229920005862 polyol Polymers 0.000 claims description 2
- 150000003077 polyols Chemical class 0.000 claims description 2
- 108010059820 Polygalacturonase Proteins 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 230000000694 effects Effects 0.000 description 2
- 238000006911 enzymatic reaction Methods 0.000 description 2
- 230000001747 exhibiting effect Effects 0.000 description 2
- 108010093305 exopolygalacturonase Proteins 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 235000015203 fruit juice Nutrition 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 235000014101 wine Nutrition 0.000 description 2
- AEMOLEFTQBMNLQ-YMDCURPLSA-N D-galactopyranuronic acid Chemical group OC1O[C@H](C(O)=O)[C@H](O)[C@H](O)[C@H]1O AEMOLEFTQBMNLQ-YMDCURPLSA-N 0.000 description 1
- 108010029182 Pectin lyase Proteins 0.000 description 1
- 208000034809 Product contamination Diseases 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 238000009924 canning Methods 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 238000005352 clarification Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 235000019990 fruit wine Nutrition 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
Landscapes
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Description
Vynález sa týká. sposobu enzýmovej degradácie pektínových látok.The invention relates. method of enzyme degradation of pectin substances.
Enzýmové degradácie pektínoyých látok spočívajú v štiepení Qú -1,4 glykozidických vazieb medzi jednotkami D-galaktopyranurónovej kyseliny. Enzýmami, ktoré katalýzujú túto reakciu sú pektolytické enzýmy endopolygalakturonáza, exopolygalakturonáza a pektínlyáza, produkované mikroorganizmami alebo přítomné v rastlinách. Enzýmová degradácia pektínových látok sa v praxi uplatňuje napr. pri výrobě ovocných štiav a vín, kde jej účinnost* spočívá v zní žení viskozity· zlepšení klarifikácie a filtrácie a zvýšení stability finálnych produktov. Doteraz známe spósoby enzýmovej degradácie pektínových látok přítomných v týchto materiáloch sa zakladajú na ich inkubácii a uvedenými pektolytickými enzýmami, najmá endopolygalakturonázou, přidanými vo formě roztokov· alebo po ich rozpuštění v inkubačnom prostředí. Obecnou nevýhodou týchto postupov je, že po skončeni enzýmovej reakcie enzým zostává spolu ao sprievodnými látkami· pochádzajúcimi z povodného enzýmového preparátu, vo finálnom roztoku a spósobuje tak často nežiadúcu kontamináciu produktov. Ďaldím nedostat kom je, že enzým je použitelný len pre obmedzené množstvo substrátu a nie je možná jeho reutilizácia, ako aj skutočnosť, že zastavenie enzýmovej reakcie vžiadanom stupni je možné dosiahnuC lem inaktiváciou enzýmu jeho zahriatím.The enzymatic degradation of the pectic substances is based on the cleavage of Qu -1.4 glycosidic bonds between D-galactopyranuronic acid units. The enzymes that catalyze this reaction are the pectolytic enzymes endopolygalacturonase, exopolygalacturonase and pectin lyase, produced by microorganisms or present in plants. The enzymatic degradation of pectin substances is applied in practice e.g. in the production of fruit juices and wines, where its effectiveness * consists in reducing viscosity · improving clarification and filtration and increasing the stability of the final products. Hitherto known methods of enzymatic degradation of the pectin substances present in these materials are based on their incubation and by said pectolytic enzymes, in particular endopolygalacturonase, added in the form of solutions or after their dissolution in the incubation medium. A general disadvantage of these processes is that, after the enzyme reaction has ended, the enzyme remains together with the accompanying substances derived from the original enzyme preparation, in the final solution, and often causes undesirable product contamination. Another drawback is that the enzyme is only applicable to a limited amount of substrate and its reutilization is not possible, as is the fact that stopping the enzyme reaction at the desired stage can be achieved by inactivating the enzyme by heating it.
Uvedené nedostatky sa odstraňujú postupom podfa vynálezu, ktorého podstatou je, že enzýmová degradácia sa uskutočňuje pomocou pektolytického enzýmového preparátu, ireverzibilne zakotveného na nerozpustnú polymérnu látku typu polykondenzátu na báze diolov a dikarboxylových kyselin, s výhodou na polyetylóntereftalát.These drawbacks are overcome by the process according to the invention, wherein the enzymatic degradation is carried out by means of a pectolytic enzyme preparation irreversibly anchored to an insoluble polymer of the polyol type based on diols and dicarboxylic acids, preferably polyethylene terephthalate.
Základný účinok spósobu degradácie pektínových látok podfa vynálezu spočívá v možnosti oddelenia enzýmu od produktov reakcie a to v ktoromkofvek stádiu reakcie, ako aj v možnosti mnohonásobného kontinuálneho alebo diskoxt&inuálneho použitia ireverzibilne zakotveného enzýmu, vyplývajúcej z jeho neobyčajme vysokej operačnej stability. ĎalšouThe basic effect of the method of degrading the pectin substances of the invention lies in the possibility of separating the enzyme from the reaction products at any stage of the reaction as well as in the possibility of multiple continuous or discoxual use of the irreversibly anchored enzyme resulting from its unusually high operational stability. Another
-h 224 911 výhodou spósobu podlá vynálezu je, že pektolytické enzýiay zakotvené na polyetyléntereftalát sa svojimi vlastnosťamž /závialosť aktivity na pH a teplote/ nelíšia od rozpustného enzymu, takže enzýmová degradácia sa móže uskutočňovať za rovnakých podmienok ako pri použití rozpustnéj pektinázy.It is an advantage of the method according to the invention that the pectolytic enzymes anchored to polyethylene terephthalate do not differ from the soluble enzyme in their properties (depending on the pH and temperature activity), so that the enzyme degradation can be carried out under the same conditions as using soluble pectinase.
Příklad 1 g pektolytického enzýmového preparátu zmobilizovaného na polyetyléntereftalát /specifický povrch nosiča 50 až 120 m /g; objem porov 2 až 3 cm /g/ sa suspenduje vil roztoku obsahujúceho pektín. Po úpravě pH na 3,8 až 4,8 sa zmes inkubuje ža miešania pri teplote nepresahujúcej 45 °C dovtedy, kým sa nedosiahne žiadaný stupeň: degradácie pektínových látok prejavujúci sa příslušnou hodnotou viskozity a obsahu redukujúcich skupím v roztoku. Po skončeni reakcie sa zmobilizovaný enzým oddeli filtráciou alebo ceotrifugácíou & móže sa použit? k degradácii ďalšej dávky substrátu. Dosiahnutie maximálněj degradácie pektínu sa prejaví nemeniacim. sa pomerom viskozity a obsahu redukujúcich skupin produktu.Example 1 g of a pectolytic enzyme preparation mobilized to polyethylene terephthalate / specific surface area of 50-120 m / g; a pore volume of 2-3 cm (g) is suspended in 1 pectin-containing solution. After adjusting the pH to 3.8 to 4.8, the mixture is incubated with stirring at a temperature not exceeding 45 ° C until the desired degree of degradation of pectin substances is achieved, exhibiting the appropriate viscosity and reducing groups content in the solution. When the reaction is complete, the enzyme is mobilized by filtration or by centrifugation. to degrade the next substrate dose. Achieving maximum degradation of pectin is manifested as unchanged. by the ratio of viscosity and content of reducing product groups.
Příklad 2Example 2
Pektolytický enzýmový preparát imobilizovaný na polyetyléntereftalát /poměr enzýmu k nosičů = 1 : 100/ sa naplní do kolony. Cez vzniklý štipec enzýmového gelu sa filtruje roztok obsahujúci pektínové látky, upravený na pH 3,8 až 4,8, Rýchlosť prietoku kolonou a výška stípca zmobilizovaného enzýrnu sa volia tak, ahy sa počas prietoku pektínovej látky cez vrstvu zmobilizovaného enzýmu dosiahol žiadaný stupem jej degradácie» prejavujúci sa příslušnou hodnotou viskozity a obsahu redukujúcich skupím.The pectolytic enzyme preparation immobilized to polyethylene terephthalate (enzyme to carrier ratio = 1: 100) is loaded onto the column. The pectin-containing solution, adjusted to a pH of 3.8 to 4.8, is filtered through the resulting gel gel column. The column flow rate and column height of the mobilized enzyme are selected such that the desired degree of degradation is achieved during the flow of pectin substance through the layer of mobilized enzyme. Exhibiting an appropriate value of viscosity and content of reducing groups.
Pri maximálnej degradácii sa v obidvoch prípadoch podlá příkladu X a 2 zfska produkt nekoutaminováný enzýmom alebo jeho sprievodnými látkami, vyznačujúci sa nízkou viskozitou· ktorý obsahuje D-galaktopyramurónovú kyselinu a jej 3 až 4 najnižšie oligomery.At maximum degradation, in both cases according to Examples X and 2, the product is non-contaminated by the enzyme or its accompanying substances, characterized by a low viscosity containing D-galactopyramuronic acid and its 3 to 4 lowest oligomers.
Vynález je možné využiť v konzervárenském priemysle, pri výrob» ovocných štiav a vo vinárskom priemysle při stabili zácii vín.The invention can be used in the canning industry, in the production of fruit juices and in the wine industry for the stabilization of wines.
Claims (1)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CS434682A CS224911B1 (en) | 1982-06-11 | 1982-06-11 | The enzyme degradation method of the pectin substances |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CS434682A CS224911B1 (en) | 1982-06-11 | 1982-06-11 | The enzyme degradation method of the pectin substances |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CS224911B1 true CS224911B1 (en) | 1984-02-13 |
Family
ID=5385990
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CS434682A CS224911B1 (en) | 1982-06-11 | 1982-06-11 | The enzyme degradation method of the pectin substances |
Country Status (1)
| Country | Link |
|---|---|
| CS (1) | CS224911B1 (en) |
-
1982
- 1982-06-11 CS CS434682A patent/CS224911B1/en unknown
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Cerreti et al. | Immobilisation of pectinases into PVA gel for fruit juice application | |
| Demir et al. | The use of commercial pectinase in fruit juice industry. Part 3: Immobilized pectinase for mash treatment | |
| Amin et al. | Improvement of activity, thermo-stability and fruit juice clarification characteristics of fungal exo-polygalacturonase | |
| Denès et al. | Purification, properties and heat inactivation of pectin methylesterase from apple (cv Golden Delicious) | |
| Baker et al. | Pectinase stabilization of orange juice cloud | |
| Fachin et al. | Comparative study of the inactivation kinetics of pectinmethylesterase in tomato juice and purified form | |
| Sarιoğlu et al. | The use of commercial pectinase in the fruit juice industry, part 2: Determination of the kinetic behaviour of immobilized commercial pectinase | |
| Rehman et al. | Immobilization of pectinase from Bacillus licheniformis KIBGE-IB21 on chitosan beads for continuous degradation of pectin polymers | |
| JPS5836959B2 (en) | Method for producing palatinose using immobilized α-glucosyltransferase | |
| Castaldo et al. | Presence of residual pectin methylesterase activity in thermally stabilized industrial fruit preparations | |
| Burton et al. | Process of Infection with φX174: Effect of Exonucleases on the Replicative Form | |
| Alkorta et al. | Immobilization of pectin lyase from Penicillium italicum by covalent binding to nylon | |
| Tsen et al. | Fiber entrapment of naringinase from Penicillium sp. and application to fruit juice debittering | |
| Fayyaz et al. | Kinetics of papaya pectinesterase | |
| CS224911B1 (en) | The enzyme degradation method of the pectin substances | |
| Demirel et al. | The production of citric acid by using immobilized Aspergillus niger A-9 and investigation of its various effects | |
| Guiavarc’h et al. | Influence of sugars and polyols on the thermal stability of purified tomato and cucumber pectinmethylesterases: a basis for TTI development | |
| Lund et al. | Pectic enzymes of pigmented strains of Clostridium | |
| Demirel et al. | Performance of immobilized Pectinex Ultra SP-L on magnetic duolite-polystyrene composite particles Part I: a batch reactor study | |
| Bogra et al. | Immobilization of tomato (Lycopersicon esculentum) pectinmethylesterase in calcium alginate beads and its application in fruit juice clarification | |
| Thibault et al. | Aspergillus niger endopolygalacturonase: 2. Characterization and some properties | |
| Martinez-Madrid et al. | Degradation of limonin by entrapped Rhodococcus fascians cells | |
| Arslan et al. | The effect of gel composition on the adsorption of invertase on poly (acrylamide/maleic acid) hydrogels | |
| Nighojkar et al. | Production of low methoxyl pectin using immobilized pectinesterase bioreactors | |
| Maeda et al. | Preparation of immobilized soybean β‐amylase on porous cellulose beads and continuous maltose production |