Literature DB >> 12882306

Isolation and biochemical characterization of a new NADH oxidase from Lactobacillus brevis.

Werner Hummel1, Bettina Riebel.   

Abstract

A new NADH oxidase, useful for the regeneration of NAD+, was isolated and characterized from Lactobacillus brevis. In crude extracts the activity was from 10-15 U mg(-1). After purification by four chromatographic steps, an activity of 116 U mg(-1) was obtained with 14% yield. Highest activity was from pH 5.5-7 and at 40 degrees C. The enzyme requires dithiothreitol to prevent oxidative deactivation. The Km value for NADH was 24 microM.

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Year:  2003        PMID： 12882306     DOI： 10.1023/a:1021730131633

Source DB:  PubMed          Journal:  Biotechnol Lett        ISSN： 0141-5492            Impact factor:   2.461


  9 in total

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Journal:  Biotechnol Lett       Date:  2021-04-12       Impact factor: 2.461

4.  New biotechnological perspectives of a NADH oxidase variant from Thermus thermophilus HB27 as NAD+-recycling enzyme.

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5.  Codon-Optimized NADH Oxidase Gene Expression and Gene Fusion with Glycerol Dehydrogenase for Bienzyme System with Cofactor Regeneration.

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Journal:  Comput Struct Biotechnol J       Date:  2014-02-26       Impact factor: 7.271

7.  In situ examination of Lactobacillus brevis after exposure to an oxidizing disinfectant.

Authors:  Yu Zhao; Susanne Knøchel; Henrik Siegumfeldt
Journal:  Front Microbiol       Date:  2014-11-26       Impact factor: 5.640

8.  Lactobacilli enhance reactive oxygen species-dependent apoptosis-inducing signaling.

Authors:  Hannah Krüger; Georg Bauer
Journal:  Redox Biol       Date:  2017-01-24       Impact factor: 11.799

9.  A water-forming NADH oxidase from Lactobacillus pentosus suitable for the regeneration of synthetic biomimetic cofactors.

Authors:  Claudia Nowak; Barbara Beer; André Pick; Teresa Roth; Petra Lommes; Volker Sieber
Journal:  Front Microbiol       Date:  2015-09-16       Impact factor: 5.640
  9 in total

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