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Immobilized yeast cells with methanol oxidase activity: Preparation and enzymatic properties
Author(s) -
Couderc R.,
Baratti J.
Publication year - 1980
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.260220605
Subject(s) - chemistry , hydrogen peroxide , methanol , yeast , enzyme , polyacrylamide gel electrophoresis , immobilized enzyme , alcohol oxidase , biochemistry , polyacrylamide , oxidase test , gel electrophoresis , chromatography , organic chemistry , polymer chemistry , pichia pastoris , recombinant dna , gene
Cells form the yeast Hansenula polymorpha (ATCC 26012) were successfully immobilized by entrapment in a polyacrylamide gel. The resulting gel showed high methanol oxidase activity especially after treatment with a detergent (CTAB). The enzymatic properties of the gel‐entrapped cell were not very different from that of the soluble enzyme except that no inhibition was observed at high methanol concentration. In continuous reactors, the gel‐entrapped cells showed a much higher stability than other enzyme preparations. The inactivation mechanism was investigated and proved to be the oxidation of essential SH group(s) of the methanol oxidase molecule by hydrogen peroxide. Treatment with β‐mercaptoethanol prevented inactivation or regenerated activity.