ISSN:
0006-3592
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
The stability of immobilized maltotetraose (G4)-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 G4 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 fs, was proposed to evaluate the half-life of the immobilized enzyme system.
Additional Material:
11 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bit.260330708
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