Expression and purification of two lipases from Yarrowia lipolytica AS 2.1216

We isolated two lipase genes LIPY7, LIPY8 from Yarrowia lipolytica CGMCC (China general microbiological culture collection center) AS 2.1216. The LIPY7 and LIPY8 genes encode a 366 and a 371-amino acid protein, respectively. The lipase genes with 6 × His tag sequence were cloned into expression vect...

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Published inProtein expression and purification Vol. 47; no. 2; pp. 393 - 397
Main Authors Song, Hui-Ting, Jiang, Zheng-Bing, Ma, Li-Xin
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.06.2006
Subjects
Bacterial Proteins - biosynthesis
Bacterial Proteins - isolation & purification
Cloning
Cloning, Molecular
Expression
Gene Expression
Lipase
Lipase - biosynthesis
Lipase - isolation & purification
Pichia
Pichia pastoris
Purification
Recombinant Proteins - biosynthesis
Recombinant Proteins - isolation & purification
Yarrowia - enzymology
Yarrowia - genetics
Yarrowia lipolytica
Purification
Lipase
Expression
Cloning
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Summary:We isolated two lipase genes LIPY7, LIPY8 from Yarrowia lipolytica CGMCC (China general microbiological culture collection center) AS 2.1216. The LIPY7 and LIPY8 genes encode a 366 and a 371-amino acid protein, respectively. The lipase genes with 6 × His tag sequence were cloned into expression vector pPIC9K and successfully integrated into a heterologous fungal host Pichia pastoris KM71, respectively. The recombinants were induced by methanol to secrete active lipases into cultural medium. The recombinant lipases were also purified and characterized.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:1046-5928
1096-0279
DOI:10.1016/j.pep.2006.02.007