A new production method for glucose oxidase

Debaetselier, A.; Dohet, P.; Beukelaer, Michèle De; Ha-Thi, V.; Hanotier, J.; Frederick, K.; Rosenberg, Steven; Vasavada, Amit

doi:10.1016/0168-1656(92)90117-r

Cited by 11 publications

(3 citation statements)

References 10 publications

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“…In 1992, Baetselier et al confirmed that expressing up to 1.5 g/L using a suitable vector-host system was possible [38]. In this study, they used expression vectors pαGO1 and pSGO2, which contain an expression cassette of the regulated hybrid promoter ADH2-GAPDH, the α-factor or GOx signal sequence for secretion, the mature GOx cDNA, and the GAPDH terminator.…”

Section: Goxmentioning

confidence: 89%

“…In this study, they used expression vectors pαGO1 and pSGO2, which contain an expression cassette of the regulated hybrid promoter ADH2-GAPDH, the α-factor or GOx signal sequence for secretion, the mature GOx cDNA, and the GAPDH terminator. The yeast strain GRF181 transformants of these plasmids were cultured on a YP medium with 8% sucrose [38]. The bidirectional inducible promoters can control recombinant expression in S. cerevisiae, galactose dehydrogenase 1 (GAL1), and UDP-glucose-epimerase (GAL10).…”

Section: Goxmentioning

confidence: 99%

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State of the Art Technologies for High Yield Heterologous Expression and Production of Oxidoreductase Enzymes: Glucose Oxidase, Cellobiose Dehydrogenase, Horseradish Peroxidase, and Laccases in Yeasts P. pastoris and S. cerevisiae

Crnoglavac Popović,

Stanišić,

Prodanović

2024

Fermentation

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Oxidoreductase (OXR) enzymes are in high demand for biocatalytic applications in the food industry and cosmetics (glucose oxidase (GOx) and cellobiose dehydrogenase (CDH)), bioremediations (horseradish peroxidase (HRP) and laccase (LAC)), and medicine for biosensors and miniature biofuel cells (GOx, CDH, LAC, and HRP). They can be used in a soluble form and/or within the yeast cell walls expressed as chimeras on the surface of yeast cells (YSD), such as P. pastoris and S. cerevisiae. However, most of the current studies suffer from either low yield for soluble enzyme expression or low enzyme activity when expressed as chimeric proteins using YSD. This is always the case in studies dealing with the heterologous expression of oxidoreductase enzymes, since there is a requirement not only for multiple OXR gene integrations into the yeast genome (super transformations), and codon optimization, but also very careful design of fermentation media composition and fermentation conditions during expression due to the need for transition metals (copper and iron) and metabolic precursors of FAD and heme. Therefore, scientists are still trying to find the optimal formula using the above-mentioned approaches; most recently, researcher started using protein engineering and directed evolution to increase in the yield of recombinant enzyme production. In this review article, we will cover all the current state-of-the-art technologies and most recent advances in the field that yielded a high expression level for some of these enzymes in specially designed expression/fermentation systems. We will also tackle and discuss new possibilities for further increases in fermentation yield using cutting-edge technologies such as directed evolution, protein and strain engineering, high-throughput screening methods based on in vitro compartmentalization, flow cytometry, and microfluidics.

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Section: Goxmentioning

confidence: 89%

Section: Goxmentioning

confidence: 99%

State of the Art Technologies for High Yield Heterologous Expression and Production of Oxidoreductase Enzymes: Glucose Oxidase, Cellobiose Dehydrogenase, Horseradish Peroxidase, and Laccases in Yeasts P. pastoris and S. cerevisiae

Crnoglavac Popović,

Stanišić,

Prodanović

2024

Fermentation

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“…Native leaders often possess certain advantages, which is proved by many cases including human serum albumin (HSA) (Sleep et al, 1990), human interferon (IFN) (Piggott et al, 1987), and Aspergillus niger glucose oxidase (GOD) (De Baetselier et al, 1992). However, recombinant proteins produced by S. cerevisiae are often hyperglycosylated and retained in the periplasmic space (Spear & Ng, 2003;Schmidt, 2004).…”

Section: Engineering the Signal Sequencementioning

confidence: 99%

Metabolic engineering of recombinant protein secretion by Saccharomyces cerevisiae

et al. 2012

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The yeast Saccharomyces cerevisiae is a widely used cell factory for the production of fuels and chemicals, and it is also provides a platform for the production of many heterologous proteins of medical or industrial interest. Therefore, many studies have focused on metabolic engineering S. cerevisiae to improve the recombinant protein production, and with the development of systems biology, it is interesting to see how this approach can be applied both to gain further insight into protein production and secretion and to further engineer the cell for improved production of valuable proteins. In this review, the protein post-translational modification such as folding, trafficking, and secretion, steps that are traditionally studied in isolation will here be described in the context of the whole system of protein secretion. Furthermore, examples of engineering secretion pathways, high-throughput screening and systems biology applications of studying protein production and secretion are also given to show how the protein production can be improved by different approaches. The objective of the review is to describe individual biological processes in the context of the larger, complex protein synthesis network.

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Engineering glucose oxidase for bioelectrochemical applications

Mano

2019

Bioelectrochemistry

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There is still a growing interest in developing glucose sensors using glucose oxidase.Since 2012, over 1000 papers are published every year, while efficient commercial sensors exist on the market. Among those glucose sensors, few have been thought and well-engineered and do not solve the problems associated with glucose oxidase; among which the O2 sensitivity of the enzyme or the competition between O2 and redox mediators for GOx's electrons. Enzyme engineering has been employed to solve those issues but screening GOx in homogeneous solution with O2 as an electron acceptor is not suitable. Very few reports describe the specific reengineering of GOx for electrochemical applications and are the subject of this review. It starts with a brief presentation of glucose oxidase and presents the recent progress in glucose oxidase reengineering by highlighting the kind of engineering/mutations performed to increase its electron transfer rate to electrode surfaces and, to decrease its O2 sensitivity. In addition, the review highlights the need to develop new screening methods involving electrochemical probing, essential to develop the next generation of glucose sensors; specific to glucose, O2 independent, biocompatible and stable over 2 weeks.

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A new production method for glucose oxidase

Cited by 11 publications

References 10 publications

State of the Art Technologies for High Yield Heterologous Expression and Production of Oxidoreductase Enzymes: Glucose Oxidase, Cellobiose Dehydrogenase, Horseradish Peroxidase, and Laccases in Yeasts P. pastoris and S. cerevisiae

State of the Art Technologies for High Yield Heterologous Expression and Production of Oxidoreductase Enzymes: Glucose Oxidase, Cellobiose Dehydrogenase, Horseradish Peroxidase, and Laccases in Yeasts P. pastoris and S. cerevisiae

Metabolic engineering of recombinant protein secretion by Saccharomyces cerevisiae

Engineering glucose oxidase for bioelectrochemical applications

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