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Expression of the Aspergillus niger glucose oxidase gene in Saccharomyces cerevisiae and its potential applications in wine production

Malherbe, D. F., Toit, M., Cordero Otero, R. R., Rensburg, P., Pretorius, I. S.·2003·Applied Microbiology and Biotechnology
DOI 10.1007/s00253-002-1208-0
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Abstract

There is a growing consumer demand for wines containing lower levels of alcohol and chemical preservatives. The objectives of this study were to express the Aspergillus niger gene encoding a glucose oxidase (GOX; beta- d-glucose:oxygen oxidoreductase, EC 1.1.3.4) in Saccharomyces cerevisiae and to evaluate the transformants for lower alcohol production and inhibition of wine spoilage organisms, such as acetic acid bacteria and lactic acid bacteria, during fermentation. The A. niger structural glucose oxidase (gox) gene was cloned into an integration vector (YIp5) containing the yeast mating pheromone alpha-factor secretion signal (MFalpha1(S)) and the phosphoglycerate-kinase-1 gene promoter (PGK1(P)) and terminator (PGK1(T)). The PGK1(P)- MFalpha1(S)- gox- PGK1(T) cassette (designated GOX1) was introduced into a laboratory strain (Sigma1278) of S. cerevisiae. Yeast transformants were analysed for the production of biologically active glucose oxidase on selective agar plates and in liquid assays. The results indicated that the recombinant glucose oxidase was active and was produced beginning early in the exponential growth phase, leading to a stable level in the stationary phase. The yeast transformants also displayed antimicrobial activity in a plate assay against lactic acid bacteria and acetic acid bacteria. This might be explained by the fact that a final product of the GOX enzymatic reaction is hydrogen peroxide, a known antimicrobial agent. Microvinification with the lab…

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Metadata

Authors
Malherbe, D. F., Toit, M., Cordero Otero, R. R., Rensburg, P., & Pretorius, I. S.
Venue
Applied Microbiology and Biotechnology
Publisher
Springer Science and Business Media LLC
Published
2003-02-11
Volume
61
Issue
5-6
Pages
502-511
ISSN
  • 0175-7598
  • 1432-0614
DOI
10.1007/s00253-002-1208-0
Cited by
97
References
1
Language
en
Licence
www.springer.com/tdm (tdm)

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