ArticleMolecular biotechnology2014
Cloning, heterologous expression, purification and characterization of M12 mutant of Aspergillus niger glucose oxidase in yeast Pichia pastoris KM71H.
Article in Molecular biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 31 citations in OpenAlex.
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- Interface engineering of cellobiose dehydrogenase improves interdomain electron transfer.Protein science : a publication of the Protein Society · 2023Article
- Semi-rational design of cellobiose dehydrogenase for increased stability in the presence of peroxide.Molecular diversity · 2020Article
- A New Cold-Active Glucose Oxidase From Penicillium: High-Level Expression and Application in Fish Preservation.Frontiers in microbiology · 2020Article
- Expression ofPeerJ · 2020Article
- Biochemical and Thermodynamical Characterization of Glucose Oxidase, Invertase, and Alkaline Phosphatase Secreted by Antarctic Yeasts.Frontiers in molecular biosciences · 2017Article
- Improvement Strategies, Cost Effective Production, and Potential Applications of Fungal Glucose Oxidase (GOD): Current Updates.Frontiers in microbiology · 2017Review
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7 authors at 2 institutions in 2 countries.
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Abstract
Aspergillus niger glucose oxidase (GOx) genes for wild-type (GenBank accession no. X16061, swiss-Prot; P13006) and M12 mutant (N2Y, K13E, T30 V, I94 V, K152R) were cloned into pPICZαA vector for expression in Pichia pastoris KM71H strain. The highest expression level of 17.5 U/mL of fermentation media was obtained in 0.5 % (v/v) methanol after 9 days of fermentation. The recombinant GOx was purified by cross-flow ultrafiltration using membranes of 30 kDa molecular cutoff and DEAE ion-exchange chromatography at pH 6.0. Purified wt GOx had k cat of 189.4 s⁻¹ and K(m) of 28.26 mM while M12 GOx had k cat of 352.0 s⁻¹ and K m of 13.33 mM for glucose at pH 5.5. Specificity constants k(cat)/K(m) of wt (6.70 mM⁻¹ s⁻¹) and M12 GOx (26.7 mM⁻¹ s⁻¹) expressed in P. pastoris KM71H were around three times higher than for the same enzymes previously expressed in Saccharomyces cerevisiae InvSc1 strain. The pH optimum and sugar specificity of M12 mutant of GOx remained similar to the wild-type form of the enzyme, while thermostability was slightly decreased. M12 GOx expressed in P. pastoris showed three times higher activity compared to the wt GOx toward redox mediators like N,N-dimethyl-nitroso-aniline used for glucose strips manufacturing. M12 mutant of GOx produced in P. pastoris KM71H could be useful for manufacturing of glucose biosensors and biofuel cells.
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