Expression, characterization and one step purification of heterologous glucose oxidase gene from Aspergillus niger ATCC 9029 in Pichia pastoris

Q4 Biochemistry, Genetics and Molecular Biology EuPA Open Proteomics Pub Date : 2018-09-01 DOI:10.1016/j.euprot.2018.09.001
Fakhry Belyad , Ali Asghar Karkhanei , Jamshid Raheb
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引用次数: 13

Abstract

Glucose Oxidase (GOD), is a common flavoprotein from Aspergillus niger ATCC 9029 with a broad application in biotechnology, food and medical industries. In this study, GOD gene was cloned into the expression vector, pPIC9 and screened by the alcohol oxidase promoter. The enzyme production increased at 28 °C. GOD activity induced by 1.0% methanol and the highest level of GOD production was the result of shaking rate at 225 rpm. The highest enzyme activity obtained at a pH value ranged from 5 to 7 at 50 °C. The enzyme was stable at a broad pH range and temperature.

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毕赤酵母中黑曲霉ATCC 9029异源葡萄糖氧化酶基因的表达、鉴定及一步纯化
葡萄糖氧化酶(GOD)是黑曲霉ATCC 9029中常见的黄酮类蛋白,在生物技术、食品和医疗等领域有着广泛的应用。本研究将GOD基因克隆到表达载体pPIC9中,通过乙醇氧化酶启动子进行筛选。在28 °C时酶产量增加。1.0%甲醇诱导的GOD活性和最高的GOD产量是在225 rpm的转速下产生的。在50 °C条件下,pH值为5 ~ 7时酶活性最高。该酶在较宽的pH范围和温度下稳定。
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EuPA Open Proteomics
EuPA Open Proteomics Biochemistry, Genetics and Molecular Biology-Biochemistry
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Proceedings of the EuBIC-MS 2020 Developers’ Meeting Editorial: The next generation in (EuPA Open) Proteomics Aims & scope Proceedings of the EuBIC Winter School 2019 Introducing the YPIC challenge
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