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Coenzyme regeneration catalyzed by NADH oxidase from Lactobacillus brevis in the reaction of l-amino acid oxidation

Paper ID Volume ID Publish Year Pages File Format Full-Text
4631 235 2008 9 PDF Available
Title
Coenzyme regeneration catalyzed by NADH oxidase from Lactobacillus brevis in the reaction of l-amino acid oxidation
Abstract

In this paper l-methionine oxidation catalyzed by l-phenylalanine dehydrogenase from Rhodococcus sp. M4 was studied. It was found that the reaction equilibrium is shifted to the side of reduction, and it was therefore necessary to regenerate NAD+ to increase l-methionine conversion. NADH oxidase from Lactobacillus brevis was used for that purpose. The enzyme was kinetically characterized. It was found that the enzyme is inhibited by NAD+. Hence, NADH oxidation catalyzed by NADH oxidase was described by the Michaelis–Menten equation which included anticompetitive NAD+ inhibition. l-Methionine oxidation was described by formal double-substrate Michaelis–Menten model which included competitive product inhibition by NADH. 2-Oxo-4-methylthiobutyric acid reduction was described by formal three-substrate Michaelis–Menten kinetics which included competitive inhibition by NAD+. Experiments were carried out in the batch and in the continuously operated enzyme membrane reactor. 100% l-methionine conversion was achieved in the batch reactor. The conversion was lower in the continuously operated enzyme membrane reactor where enzyme deactivation occurred.

Keywords
Amino acid; Coenzyme regeneration; NADH oxidase; l-Phenylalanine dehydrogenase; Enzymes; Enzyme biocatalysis
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Coenzyme regeneration catalyzed by NADH oxidase from Lactobacillus brevis in the reaction of l-amino acid oxidation
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Publisher
Database: Elsevier - ScienceDirect
Journal: Biochemical Engineering Journal - Volume 39, Issue 2, 15 April 2008, Pages 319–327
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
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Price was $35.95
You save - $31
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Full-text PDF Download
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