High-level expression of prolyl endopeptidase in Pichia pastoris using PLA2 as a fusion partner
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- 作者：Ting Jianga ; jiangting75@outlook.com" class="auth_mail" title="E-mail the corresponding author ; Chao Kanga ; b ; Xiao-Wei Yua ; yuxw@jiangnan.edu.cn" class="auth_mail" title="E-mail the corresponding author ; Yan Xua ; yxu@jiangnan.edu.cn" class="auth_mail" title="E-mail the corresponding author
- 关键词：PEP ; prolyl endopeptidase ; MOH ; recombinant PEP ; PLA2 ; phospholipase A2 ; CBD ; cellulose-binding domain ; SUMO ; small ubiquitin-related modifier ; MBP ; maltose binding protein ; GST ; glutathione-S-transferase ; BMGY ; buffered minimal glycerol-complex medium ; BMMY ; buffered minimal methanol-complex medium ; LB ; luria-bertani ; LLB ; low salt luria-bertani ; CLMH ; CBD fused with MOH ; SLMH ; SUMO fused with MOH ; MLMH ; MBP fused with MOH ; PLMH ; PLA2 fused with MOH ; PMF ; peptide mass fingerprinting ; DTT ; dithi
- 刊名：Journal of Molecular Catalysis B: Enzymatic
- 出版年：2016
- 出版时间：March 2016
- 年：2016
- 卷：125
- 期：Complete
- 页码：81-87
- 全文大小：1756 K
文摘
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Fusion expression is an effective strategy to improve protein secretion level.
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PLA2 was successfully used as a fusion chaperon for the first time.
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P. pastoris GS115 can be a suitable host for heterogenous expression.
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