Heterologous protein secretion by Candida utilis.

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Bibliographic Details
Title:	Heterologous protein secretion by Candida utilis.
Authors:	Kunigo, Maya¹, Buerth, Christoph¹, Tielker, Denis¹, Ernst, Joachim¹ joachim.ernst@uni-duesseldorf.de
Source:	Applied Microbiology & Biotechnology. Aug2013, Vol. 97 Issue 16, p7357-7368. 12p.
Subjects:	Candida utilis, Proteins, Secretion, Candida albicans, Saccharomyces cerevisiae, Gene expression, Yeast research
Abstract:	The yeast Candida utilis (also referred to as Torula) is used as a whole-cell food additive and as a recombinant host for production of intracellular molecules. Here, we report recombinant C. utilis strains secreting significant amounts of Candida antarctica lipase B (CalB). Native and heterologous secretion signals led to secretion of CalB into the growth medium; CalB was enzymatically active and it carried a short N-glycosyl chain lacking extensive mannosylation. Furthermore, CalB fusions to the C. utilis Gas1 cell wall protein led to effective surface display of enzymatically active CalB and of β-galactosidase. Secretory production in C. utilis was achieved using a novel set of expression vectors containing sat1 conferring nourseothricin resistance, which could be transformed into C. utilis, Pichia jadinii, Candida albicans, and Saccharomyces cerevisiae; C. utilis promoters including the constitutive TDH3 and the highly xylose-inducible GXS1 promoters allowed efficient gene expression. These results establish C. utilis as a promising host for the secretory production of proteins. [ABSTRACT FROM AUTHOR]
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Database:	Engineering Source

Description
Abstract:	The yeast Candida utilis (also referred to as Torula) is used as a whole-cell food additive and as a recombinant host for production of intracellular molecules. Here, we report recombinant C. utilis strains secreting significant amounts of Candida antarctica lipase B (CalB). Native and heterologous secretion signals led to secretion of CalB into the growth medium; CalB was enzymatically active and it carried a short N-glycosyl chain lacking extensive mannosylation. Furthermore, CalB fusions to the C. utilis Gas1 cell wall protein led to effective surface display of enzymatically active CalB and of β-galactosidase. Secretory production in C. utilis was achieved using a novel set of expression vectors containing sat1 conferring nourseothricin resistance, which could be transformed into C. utilis, Pichia jadinii, Candida albicans, and Saccharomyces cerevisiae; C. utilis promoters including the constitutive TDH3 and the highly xylose-inducible GXS1 promoters allowed efficient gene expression. These results establish C. utilis as a promising host for the secretory production of proteins. [ABSTRACT FROM AUTHOR]
ISSN:	01757598
DOI:	10.1007/s00253-013-4890-1