Purification and Properties of Nicotinamide Adenine Dinucleotide-Dependent d - and l -Lactate Dehydrogenases in a Group N Streptococcus-Reference-Cited by-同舟云学术

Purification and Properties of Nicotinamide Adenine Dinucleotide-Dependent d - and l -Lactate Dehydrogenases in a Group N Streptococcus

Published:1972-08 Issue:2 Volume:111 Page:392-396
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Mou L.¹,Mulvena D. P.¹,Jonas H. A.¹,Jago G. R.¹

Affiliation:

1. Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, Victoria 3052, Australia, and C.S.I.R.O., Division of Food Research, Dairy Research Laboratory, Highett, Victoria 3190, Australia

Abstract

Streptococcus lactis strain 760, a group N streptococcus, was found to possess nicotinamide adenine dinucleotide-dependent dehydrogenase activities for both the l (+) and the d (−) isomers of lactic acid. The two enzymes were isolated and purified and were found to differ with respect to p H optima, activation by fructose-1,6-diphosphate, p H and heat stability, and the temperature at which each enzyme was formed in the organism during growth. The presence of a racemase for lactic acid was not detected by the methods used.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/jb.111.2.392-396.1972

Reference9 articles.

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