Simultaneous catalysis and product separation by cross-linked enzyme crystals
| Autor: | Matti Leisola, Johan Finell, Ossi Pastinen, Jouni Jokela |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Xylose isomerase
Arabinose Ribose Pentoses Oligosaccharides Bioengineering Isomerase Xylose Disaccharides Applied Microbiology and Biotechnology Catalysis Fungal Proteins chemistry.chemical_compound Bacterial Proteins Xylobiose Organic chemistry Aldose-Ketose Isomerases Trichoderma Chromatography Ribulose Enzymes Immobilized Streptomyces Xylan Endo-1 3-beta-Xylosidase Xylosidases chemistry Solubility Streptomyces rubiginosus Xylanase Crystallization Biotechnology |
| Zdroj: | Biotechnology and bioengineering. 72(4) |
| ISSN: | 0006-3592 |
| Popis: | Crystalline cross-linked xylose isomerase (CLXI, EC 5.3.1.5) and xylanase (CLX, EC 3.2.1.8) were studied in a packed-bed reactor for simultaneous catalytic reaction and separation of substrates from reaction products. Streptomyces rubiginosus xylose isomerase catalyzed a slow isomerization of L-arabinose to L-ribulose and an epimerization to L-ribose. In equilibrium the reaction mixture contained 52.5% arabinose, 22.5% ribulose, and 25% ribose. In a packed-bed column filled with CLXI, a simultaneous reaction and separation resulted in fractions where arabinose concentration varied between 100-0%, ribulose between 0-55%, and ribose between 0-100%. Trichoderma reesei xylanase II hydrolyzed and transferred xylotetraose mainly to xylotriose and xylobiose. In a packed-bed column filled with CLX, xylotetraose rapidly reacted to xylobiose and xylose by a mechanism that is not yet fully understood. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text