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Preparation and properties of immobilized methanol oxidase
Author(s) -
Baratti J.,
Couderc R.,
Cooney C. L.,
Wang D. I. C.
Publication year - 1978
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.260200303
Subject(s) - chemistry , homogenizer , methanol , chromatography , formaldehyde , immobilized enzyme , kinetics , adsorption , ammonium sulfate , alcohol oxidase , yeast , cellulose , enzyme , biochemistry , organic chemistry , pichia pastoris , physics , quantum mechanics , gene , recombinant dna
Methanol oxidase produced by the yeast Hansenula polymorpha DL‐1 was used for the enzymatic oxidation of methanol to formaldehyde. The kinetics of enzyme and protein release during cell desruption were studied at the laboratory scale with a Braun homogenizer and the pilot plant scale with a Manton–Gaulin homogenizer. Conditions were defined for maximum release and retention of high activity in cell‐free extracts. Methanol oxidase was immobilized by adsorption on DEAE‐cellulose from enzymes in cell‐free extracts or from ammonium sulfate purified purified fractions. The kinetics of formaldehyde formation with both soluble and immobilized enzyme was studied in batch and continuous reactors.