Highly Selective Oxidation of Benzyl Alcohol Using Engineered Gluconobacter Oxydans in Biphasic System

The Gluconobacter oxydans M5 with disruption of the pyrroloquinoline quinine-dependent membrane-bound aldehyde dehydrogenase (ALDH) was used for the oxidation of benzyl alcohol. The selectivity toward benzaldehyde showed an obvious increase for the engineered strain, which reached the 67.3%, while t...

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Bibliographic Details
Published in:Current microbiology 2011-04, Vol.62 (4), p.1123-1127
Main Authors: Wu, Jian, Li, Ming Hua, Lin, Jin Ping, Wei, Dong Zhi
Format: Article
Language:English
Subjects:
Alcohol
aldehyde dehydrogenase
Aldehyde Dehydrogenase - genetics
Aldehyde Dehydrogenase - metabolism
Aldehydes
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
benzyl alcohol
Benzyl Alcohol - metabolism
Biomedical and Life Sciences
Biotechnology
Biotransformation
Genetic Engineering
Gluconobacter oxydans
Gluconobacter oxydans - enzymology
Gluconobacter oxydans - genetics
Gluconobacter oxydans - metabolism
Life Sciences
Microbiology
Oxidation
Oxidation-Reduction
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Summary:The Gluconobacter oxydans M5 with disruption of the pyrroloquinoline quinine-dependent membrane-bound aldehyde dehydrogenase (ALDH) was used for the oxidation of benzyl alcohol. The selectivity toward benzaldehyde showed an obvious increase for the engineered strain, which reached the 67.3%, while the wild strain had only 2.8%. Meantime, the aqueous/isooctane (1:1) biphasic system was used for the further improvement of selectivity. By these methods, nearly 100% selectivity and conversion rate could be obtained within 1 h at the optimum initial benzyl alcohol concentration of 5.0 g/l.
ISSN:0343-8651
1432-0991
DOI:10.1007/s00284-010-9831-y