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Expression of active spinach glycolate oxidase in Aspergillus nidulans
Author(s) -
Devchand Medha,
Skipper Nigel,
Anton David L.,
DiCosimo Robert,
Gavagan John E.
Publication year - 1996
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/(sici)1097-0290(19960505)50:3<341::aid-bit13>3.0.co;2-q
Subject(s) - aspergillus nidulans , spinach , chemistry , aspergillus , biochemistry , biology , botany , gene , mutant
The biocatalytic production of glyoxylic acid from glycolic acid requires two enzymes: glycolate oxidase, which catalyzes the oxidation of glycolic acid by oxygen to produce glyoxylic acid and hydrogen peroxide, and catalase, which decomposes the byproduct hydrogen peroxide. As an alternative to isolation from the leaf peroxisomes of spinach, glycolate oxidase has now been cloned and expressed in transformants of Aspergillus nidulans T580 at levels ranging from 1.7 to 36 IU/g dry wt. cells. The glycolate oxidase of transformant strain T17 comprises ca. 1.9% of total cell protein and is expressed at near 100% activity. © 1996 John Wiley & Sons, Inc.