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Article

A thermostable triple mutant of pyranose 2-oxidase from Trametes multicolor with improved properties for biotechnological applications.

Biotechnology journal - 1 Apr 2009

Spadiut Oliver, Radakovits Katrin, Pisanelli Ines, Salaheddin Clara, Yamabhai Montarop, Tan Tien-Chye, Divne Christina, Haltrich Dietmar

Abstract excerpt

In order to increase the thermal stability and the catalytic properties of pyranose oxidase (P2Ox) from Trametes multicolor toward its poor substrate D-galactose and the alternative electron acceptor 1,4-benzoquinone (1,4-BQ), we designed the triple-mutant T169G/E542K/V546C. Whereas the wild-type enzyme clearly favors D-glucose as its substrate over D-galactose [substrate selectivity...

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Identifiers

PMID: 19291706
DOI: 10.1002/biot.200800260

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