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Heterologous expression of bovine lactoferricin in Pichia methanolica

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Abstract

According to the bias of codon utilization of Pichia methanolica, a fragment encoding bovine lactoferricin has been cloned and expressed in the P. methanolica under the control of the alcohol oxidase promoter, which was followed by the Saccharomyces cerevisiae α-factor signal peptide. The α-factor signal peptide efficiently directed the secretion of bovine lactoferricin from the recombinant yeast cell. The recombinant bovine lactoferricin appears to be successfully expressed, as it displays antibacterial activity (antibacterial assay). Moreover, the identity of the recombinant product was estimated by Tricine-SDS-PAGE.

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Abbreviations

AUG1:

alcohol oxidase

LfcinB:

bovine lacto-ferricin

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Authors and Affiliations

  1. Key Lab of Diary Science, Ministry of Education, Harbin, PO 150030, P. R. China

    HaiKuan Wang & XinHuai Zhao

  2. Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science and Technology, Tianjin, PO 300457, P. R. China

    HaiKuan Wang & FuPing Lu

Authors
  1. HaiKuan Wang
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  2. XinHuai Zhao
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  3. FuPing Lu
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Correspondence to HaiKuan Wang.

Additional information

Published in Russian in Biokhimiya, 2007, Vol. 72, No. 6, pp. 785–789.

Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM06-332, April 29, 2007.

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Wang, H., Zhao, X. & Lu, F. Heterologous expression of bovine lactoferricin in Pichia methanolica . Biochemistry Moscow 72, 640–643 (2007). https://doi.org/10.1134/S0006297907060065

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  • DOI: https://doi.org/10.1134/S0006297907060065

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