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Enzymatic properties of immobilized Alcaligenes faecalis cells with cell‐associated β‐glucosidase activity
Author(s) -
Wheatley Margaret A.,
Phillips Colin R.
Publication year - 1984
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/bit.260260604
Subject(s) - chemistry , cellulase , immobilized enzyme , alcaligenes , enzyme , chromatography , hydrolysis , trichoderma reesei , alcaligenes faecalis , thermal stability , biochemistry , bacteria , organic chemistry , pseudomonas , biology , genetics
Enzymatic properties of Alcaligenes faecalis cells immobilized in polyacrylamide were characterized and compared with those reported for the extracted enzyme, and with those measured for free cells. Many of the properties reflected those of the extracted enzyme rather than those measured in the free whole cells prior to immobilization, suggesting cell disruption during immobilization. These properties included the pH activity profile, a slightly broader pH stability profile, and the activation energy. Electron micrographs showed evidence of cell debris among the polymer matrix. The immobilized cells were not viable, and did not consume glucose. Thermal stability was less after immobilization with a half‐life of 16 h at 45°C, and 3.5 h at 50°C. The immobilized preparation was more stable when stored lyophilized rather than in buffer, losing 23 and 52% activity, respectively, after six months. The enzyme was irreversibly inhibited by both acetate and citrate buffers. If the immobilized enzyme is to be used in conjunction with cellulases from Trichoderma reesei for cellulase saccharification, the optimal conditions would be pH 5.5 and 45°C in a buffer containing no carboxylic acid groups.