Activity of NAD-Dependent Dehydrogenase Enzyme of Lactic Streptococci on Acetaldehyde and n-Hexanal 1

R H Schmidt; L K Farron; T R Bateh; P E Araujo

doi:10.4315/0362-028X-42.10.778

Activity of NAD-Dependent Dehydrogenase Enzyme of Lactic Streptococci on Acetaldehyde and n-Hexanal ¹

J Food Prot. 1979 Oct;42(10):778-779. doi: 10.4315/0362-028X-42.10.778.

Authors

R H Schmidt¹, L K Farron¹, T R Bateh¹, P E Araujo¹

Affiliation

¹ Food Science and Human Nutrition Department, IFAS, University of Florida, Gainesville, Florida 32611.

PMID: 30812129
DOI: 10.4315/0362-028X-42.10.778

Abstract

Alcohol dehydrogenase (alcohol:NAD oxidoreductase, E.C. 1.1.1.1) activity was observed on acetaldehyde and n-hexanal in homogenized cell extract of Steptococcus lactis C2. Substrate inhibition was apparent at levels of n-hexanal above 4.0 mM. Increased centrifugal force from 12.000 × g for 20 min to 350,000 × g for 1 h resulted in increased specific activity in the cell-extract supernatant fluids. Aldehyde dehydrogenase (aldehyde: NAD oxidoreductose; E.C. 1.2.1.3) was not detected in any of the cell extracts. A possible involvement of the enzyme system with flavor modification in lactic-fermented oilseed milk is suggested.