Engineering of pyranose dehydrogenase for increased oxygen reactivity.
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ABSTRACT:
SUBMITTER: Krondorfer I
PROVIDER: S-EPMC3948749 | biostudies-literature | 2014
REPOSITORIES: biostudies-literature
Publications
Engineering of pyranose dehydrogenase for increased oxygen reactivity.
Krondorfer Iris I Lipp Katharina K Brugger Dagmar D Staudigl Petra P Sygmund Christoph C Haltrich Dietmar D Peterbauer Clemens K CK
PloS one 20140310 3
Pyranose dehydrogenase (PDH), a member of the GMC family of flavoproteins, shows a very broad sugar substrate specificity but is limited to a narrow range of electron acceptors and reacts extremely slowly with dioxygen as acceptor. The use of substituted quinones or (organo)metals as electron acceptors is undesirable for many production processes, especially of food ingredients. To improve the oxygen reactivity, site-saturation mutagenesis libraries of twelve amino acids around the active site o ...[more]
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