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Stability of immobilized maltotetraose‐forming amylase from Pseudomonas stutzeri
Author(s) -
Kimura Takashi,
Ogata Masafumi,
Yoshida Masahiro,
Nakakuki Teruo
Publication year - 1989
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.260330708
Subject(s) - pseudomonas stutzeri , chemistry , substrate (aquarium) , immobilized enzyme , enzyme , chromatography , kinetics , amylase , industrial and production engineering , biochemistry , biology , bacteria , ecology , genetics , physics , quantum mechanics , electrical engineering , engineering
The stability of immobilized maltotetraose (G 4 )‐forming amylase (1,4‐α‐ D ‐glucan maltoteraohydrolase, EC 3.2.1.60) from Pseudomonas stutzeri was investigated in both batch and continous processes. The inactivation process of the immobilized enzyme seemed to obey first‐order kinetics, and the immobilized enzyme became more stable when coexisting with 20–30 wt % substrate and calcium ions. From intensive studies on the operational stability in the continuous process, the apparent half‐life of G 4 productivity in a constant‐flow system was mainly affected by the reaction temperature, substrate concentration, and initial immobilized enzyme activity. A new factor, immobilized enzyme stability factor f s , was proposed to evaluate the half‐life of the immobilized enzyme system.