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Expression of active spinach glycolate oxidase in Aspergillus nidulans

✍ Scribed by Medha Devchand; Nigel Skipper; David L. Anton; Robert DiCosimo; John E. Gavagan

Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
542 KB
Volume
50
Category
Article
ISSN
0006-3592

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✦ Synopsis

The biocatalytic production of glyoxylic acid from glycolic acid requires two enzymes: glycolate oxidase, which catalyzes the oxidation of glycolic acid by oxygen t o 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 drywt. cells. The glycolate oxidase of transformant strain TI7 comprises ca. 1.9% of total cell protein and is expressed at near 100% activity.

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