1887

Abstract

Summary: is the first member of the Enterobacteriaceae found to possess a thiamine pyrophosphate-dependent pyruvate decarboxylase yielding acetaldehyde and CO. In conjunction with an NAD-dependent ethanol dehydrogenase this represents the route of ethanol formation and explains the high ethanol yields previously reported. The organism also possesses an α-acetolactate decarboxylase and is thus able to produce acetoin by both the recognized microbial pathways. Fermentation balances for pyruvate with bacterial suspensions and extracts at pH 6.0 are recorded. NADH oxidase and lactate dehydrogenase are present but NADH-NADP transhydrogenase, coenzyme A-dependent acetaldehyde dehydrogenase, formate dehydrogenase or formate hydrogenlyase could not be detected. The findings are discussed in relation to the classification of and the comparative biochemistry of the Enterobacteriaceae.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-68-3-295
1971-11-01
2019-10-23
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-68-3-295
Loading
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error