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学科主题: Biochemical Research Methods; Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology
题名: Cell surface display of functionally active lipases from Yarrowia lipolytica in Pichia pastoris
作者: Jiang, Zheng-Bing; Song, Hui-Ting; Gupta, Nishith; Ma, Li-Xin; Wu, Zhen-Bin
通讯作者: Jiang, ZB, Hubei Univ, Coll Life Sci, Wuhan 430062, Peoples R China
关键词: cell surface display ; protein expression ; lipase ; Pichia pastoris
刊名: PROTEIN EXPRESSION AND PURIFICATION
发表日期: 2007-11-01
DOI: 10.1016/j.pep.2007.07.003
卷: 56, 期:1, 页:35-39
收录类别: SCI
文章类型: Article
部门归属: Hubei Univ, Coll Life Sci, Wuhan 430062, Peoples R China; Hubei Univ, Coll Chem & Chem Engn, Wuhan 430062, Peoples R China; Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Peoples R China; Humboldt Univ, Dept Mol Parasitol, D-10115 Berlin, Germany
WOS标题词: Science & Technology ; Life Sciences & Biomedicine
类目[WOS]: Biochemical Research Methods ; Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
研究领域[WOS]: Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
摘要: The lipase genes of Yarrowia lipolytica, LIPY7 and LIPY8, fused with FLO-flocculation domain sequence from Saccharomyces cerevisiae at their N-termini, were expressed in Pichia pastoris KM71. Following the induction with methanol, the recombinant proteins were displayed on the cell surface of P. pastoris, as confirmed by the confocal laser scanning microscopy. The LipY7p and LipY8p were anchored on P. pastoris via the flocculation functional domain of Flo 1 p. The surface-displayed lipases were characterized for their application as the whole-cell biocatalyst. These lipases can also be cleaved off from their anchor by enterokinase treatment to yield functionally active proteins in the supernatant offering an alternative purification method for LipY7p and LipY8p. (c) 2007 Elsevier Inc. All rights reserved.
英文摘要: The lipase genes of Yarrowia lipolytica, LIPY7 and LIPY8, fused with FLO-flocculation domain sequence from Saccharomyces cerevisiae at their N-termini, were expressed in Pichia pastoris KM71. Following the induction with methanol, the recombinant proteins were displayed on the cell surface of P. pastoris, as confirmed by the confocal laser scanning microscopy. The LipY7p and LipY8p were anchored on P. pastoris via the flocculation functional domain of Flo 1 p. The surface-displayed lipases were characterized for their application as the whole-cell biocatalyst. These lipases can also be cleaved off from their anchor by enterokinase treatment to yield functionally active proteins in the supernatant offering an alternative purification method for LipY7p and LipY8p. (c) 2007 Elsevier Inc. All rights reserved.
关键词[WOS]: SACCHAROMYCES-CEREVISIAE ; YEAST STRAINS ; GENE FLO1 ; CONSTRUCTION ; SYSTEM ; ACID
语种: 英语
WOS记录号: WOS:000250639100005
ISSN号: 1046-5928
Citation statistics:
内容类型: 期刊论文
URI标识: http://ir.ihb.ac.cn/handle/152342/8384
Appears in Collections:中科院水生所知识产出(2009年前)_期刊论文

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作者单位: 1.Hubei Univ, Coll Life Sci, Wuhan 430062, Peoples R China
2.Hubei Univ, Coll Chem & Chem Engn, Wuhan 430062, Peoples R China
3.Chinese Acad Sci, Inst Hydrobiol, State Key Lab Freshwater Ecol & Biotechnol, Wuhan 430072, Peoples R China
4.Humboldt Univ, Dept Mol Parasitol, D-10115 Berlin, Germany

Recommended Citation:
Jiang, Zheng-Bing; Song, Hui-Ting; Gupta, Nishith; Ma, Li-Xin; Wu, Zhen-Bin.Cell surface display of functionally active lipases from Yarrowia lipolytica in Pichia pastoris,PROTEIN EXPRESSION AND PURIFICATION,2007,56(1):35-39
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