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Enzymatic production of hydrogen peroxide and acetaldehyde in a pressure reactor
Author(s) -
Nelles L. P.,
Arnold J. A.,
Willman D. S.
Publication year - 1990
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.260360813
Subject(s) - hydrogen peroxide , acetaldehyde , chemistry , enzyme , production (economics) , biochemistry , organic chemistry , ethanol , economics , macroeconomics
Alcohol oxidase, an enzyme which exhibits relatively weak substrate specificity among short chain alcohols, forms the corresponding aldehyde and hydrogen peroxide as coproduct. The ability of alcohol oxidase from Pichia pastoris yeast to convert ethanol to acetaldehyde and hydrogen peroxide was examined in an oxygen pressure reactor under conditions, such that oxygen availability was sufficient to permit rapid catalysis. Hydrogen peroxide levels of ∼1.8/ M (6% w/w) were attained in 2–3 h with 2.8 μ M enzyme, corresponding to a productivity of ∼30 g peroxide/g enzyme. Optimal conditions (within equipment limitations) were 900 psi oxygen, 2.6 M ethanol, at 4 °C. Similar levels of products were reached in the reactor using enzyme immobilized covalently on controlled pore glass and noncovalently on an anion exchange support. Recycle of covalently immobilized enzyme was not possible as a result of enzyme inactivation after a single run. Limited recycle of noncovalently immobilized enzyme was accomplished with substantial decreases in levels of product attainable on each cycle.