Abstract:
:Acetobacter pasteurianus oxidizes glycidol with high activity, comparable to the oxidation of ethanol. The organism has a preference for the S-enantiomer, and the kinetic resolution process obeys a simple relationship, indicating an enantiomeric ratio (E) of 19. The compound is converted into glycidic acid, although a transient accumulation of glycidaldehyde occurs initially. Determination of other parameters revealed a temperature optimum of 50 degrees C, long-term stability (cells in the resting state), and a pH optimum compatible with the chemical stability of glycidol. However, it was also noted that respiration rates decrease at concentrations of glycidol above 1 M. This is most likely caused by substrate inhibition of the glycidol-oxidizing enzyme, the quinohemoprotein ethanol dehydrogenase. Comparison with existing methods for enantiomerically pure glycidol production indicated a number of attractive points for the method described here, although definitive evaluation must await further studies on the long-term stability under process conditions, reusability of the cells, and the mechanism of glycidol inhibition.
journal_name
Enzyme Microb Technoljournal_title
Enzyme and microbial technologyauthors
Geerlof A,Jongejan JA,van Dooren TJ,Racemakers-Franken PC,van den Tweel WJ,Duine JAdoi
10.1016/0141-0229(94)90143-0subject
Has Abstractpub_date
1994-12-01 00:00:00pages
1059-63issue
12eissn
0141-0229issn
1879-0909pii
0141-0229(94)90143-0journal_volume
16pub_type
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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