Production and optimization of a kiwi pectin methylesterase inhibitor in Pichia pastoris GS115
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- 作者：Qian Liu (1)
Wentao Xu (1)
Shiwen Han (1)
Dongyan Cao (1)
Xiaoyun He (1)
Kunlun Huang (1)
Xiaohong Mei (1) - 关键词：pectin methylesterase inhibitor ; Pichia pastoris ; codon optimization ; nickel ion chelating affinity chromatography
- 刊名：Food Science and Biotechnology
- 出版年：2014
- 出版时间：December 2014
- 年：2014
- 卷：23
- 期：6
- 页码：1971-1976
- 全文大小：460 KB
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Wentao Xu (1)
Shiwen Han (1)
Dongyan Cao (1)
Xiaoyun He (1)
Kunlun Huang (1)
Xiaohong Mei (1)
1. College of Food Science and Nutritional Engineering, China Agricultural University, Beijing, 100083, China - ISSN：2092-6456
文摘
Gene sequence coding of a kiwi pectin methylesterase inhibitor was optimized, synthesized, and expressed in Pichia pastoris GS115 based on P. pastoris preferred codon usage. The expression level of the recombinant protein (kwPMEI) increased by 89.74% after codon optimization. Expression conditions of recombinant strains were optimized. The highest production of kwPMEI was achieved using 0.8% sorbitol (added every 24 h), 0.05% oleic acid (added at the beginning of induction), and 0.5% methanol (added every 12 h). kwPMEI was purified using Ni2+ chelating affinity chromatography and 17 mg of the protein was harvested from 60 mL of a culture supernatant. Activity analysis showed that kwPMEI efficiently inhibited the activity of different plant PMEs. High expression levels and purification of kwPMEI will promote applications in fruit and vegetable juices.