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Simultaneous catalysis and product separation by cross‐linked enzyme crystals
Author(s) -
Leisola Matti,
Jokela Jouni,
Finell Johan,
Pastinen Ossi
Publication year - 2001
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/1097-0290(20010220)72:4<501::aid-bit1013>3.0.co;2-j
Subject(s) - xylobiose , chemistry , xylose isomerase , arabinose , xylose , isomerase , ribulose , xylanase , hydrolysis , packed bed , chromatography , stereochemistry , biochemistry , enzyme , fermentation , rubisco
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. © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 72: 501–505, 2001.