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Heterologous protein secretion by Candida utilis.

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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]
Copyright of Applied Microbiology & Biotechnology is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Heterologous protein secretion by Candida utilis.
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  Data: <searchLink fieldCode="JN" term="%22Applied+Microbiology+%26+Biotechnology%22">Applied Microbiology & Biotechnology</searchLink>. Aug2013, Vol. 97 Issue 16, p7357-7368. 12p.
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  Data: <searchLink fieldCode="DE" term="%22Candida+utilis%22">Candida utilis</searchLink><br /><searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Secretion%22">Secretion</searchLink><br /><searchLink fieldCode="DE" term="%22Candida+albicans%22">Candida albicans</searchLink><br /><searchLink fieldCode="DE" term="%22Saccharomyces+cerevisiae%22">Saccharomyces cerevisiae</searchLink><br /><searchLink fieldCode="DE" term="%22Gene+expression%22">Gene expression</searchLink><br /><searchLink fieldCode="DE" term="%22Yeast+research%22">Yeast research</searchLink>
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  Data: 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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  Data: <i>Copyright of Applied Microbiology & Biotechnology is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1007/s00253-013-4890-1
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      – Code: eng
        Text: English
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      – SubjectFull: Proteins
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      – SubjectFull: Secretion
        Type: general
      – SubjectFull: Candida albicans
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              Text: Aug2013
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