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Cell surface display of functionally active lipases from Yarrowia lipolytica in Pichia pastoris
Jiang, Zheng-Bing; Song, Hui-Ting; Gupta, Nishith; Ma, Li-Xin; Wu, Zhen-Bin; Jiang, ZB, Hubei Univ, Coll Life Sci, Wuhan 430062, Peoples R China
2007-11-01
Source PublicationPROTEIN EXPRESSION AND PURIFICATION
ISSN1046-5928
Volume56Issue:1Pages:35-39
AbstractThe 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.; 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.
SubtypeArticle
KeywordCell Surface Display Protein Expression Lipase Pichia Pastoris
DepartmentHubei 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
Subject AreaBiochemical Research Methods ; Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
DOI10.1016/j.pep.2007.07.003
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
Indexed BySCI
Language英语
WOS Research AreaBiochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
WOS SubjectBiochemical Research Methods ; Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
WOS IDWOS:000250639100005
WOS KeywordSACCHAROMYCES-CEREVISIAE ; YEAST STRAINS ; GENE FLO1 ; CONSTRUCTION ; SYSTEM ; ACID
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Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/152342/8384
Collection期刊论文
Corresponding AuthorJiang, ZB, Hubei Univ, Coll Life Sci, Wuhan 430062, Peoples R China
Affiliation1.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
GB/T 7714
Jiang, Zheng-Bing,Song, Hui-Ting,Gupta, Nishith,et al. Cell surface display of functionally active lipases from Yarrowia lipolytica in Pichia pastoris[J]. PROTEIN EXPRESSION AND PURIFICATION,2007,56(1):35-39.
APA Jiang, Zheng-Bing,Song, Hui-Ting,Gupta, Nishith,Ma, Li-Xin,Wu, Zhen-Bin,&Jiang, ZB, Hubei Univ, Coll Life Sci, Wuhan 430062, Peoples R China.(2007).Cell surface display of functionally active lipases from Yarrowia lipolytica in Pichia pastoris.PROTEIN EXPRESSION AND PURIFICATION,56(1),35-39.
MLA Jiang, Zheng-Bing,et al."Cell surface display of functionally active lipases from Yarrowia lipolytica in Pichia pastoris".PROTEIN EXPRESSION AND PURIFICATION 56.1(2007):35-39.
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