| Abstract: | 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. |
