Please use this identifier to cite or link to this item: https://doi.org/10.1006/prep.2001.1395
Title: Low-temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris
Authors: Li, Z.
Xiong, F.
Lin, Q.
D'Anjou, M.
Daugulis, A.J.
Yang, D.S.C.
Hew, C.L. 
Issue Date: 2001
Citation: Li, Z., Xiong, F., Lin, Q., D'Anjou, M., Daugulis, A.J., Yang, D.S.C., Hew, C.L. (2001). Low-temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris. Protein Expression and Purification 21 (3) : 438-445. ScholarBank@NUS Repository. https://doi.org/10.1006/prep.2001.1395
Abstract: Antifreeze proteins and antifreeze glycoproteins are structurally diverse molecules that share a common property in binding to ice crystals and inhibiting ice crystal growth. Type II fish antifreeze protein of Atlantic herring (Clupea harengus harengus) is unique in its requirement of Ca2+ for antifreeze activity. In this study, we utilized the secretion vector pGAPZα A to express recombinant herring antifreeze protein (WT) and a fusion protein with a C-terminal six-histidine tag (WT-6H) in yeast Pichia pastoris wild-type strain X-33 or protease-deficient strain SMD1168H. Both recombinant proteins were secreted into the culture medium and properly folded and functioned as the native herring antifreeze protein. Furthermore, our studies demonstrated that expression at a lower temperature increased the yield of the recombinant protein dramatically, which might be due to the enhanced protein folding pathway, as well as increased cell viability at lower temperature. These data suggested that P. pastoris is a useful system for the production of soluble and biologically active herring antifreeze protein required for structural and functional studies. © 2001 Academic Press.
Source Title: Protein Expression and Purification
URI: http://scholarbank.nus.edu.sg/handle/10635/101040
ISSN: 10465928
DOI: 10.1006/prep.2001.1395
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