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Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 25, 2010
Expression, purification, and characterization of recombinant Chinese shrimp crustin-like protein (CruFc) in Pichia
Jiquan Zhang1, Fuhua Li, Zaizhao Wang
1Institute of Oceanology, Chinese Academy of Sciences, Qingdao, 266071, PR China.
Abstract:
A crustin-like protein (CruFc) from Fenneropenaeus chinensis was expressed in Pichia pastoris and then purified to electrophoretic homogeneity on a Sephacryl S-100 column with a band corresponding to the expected one (13 kDa) shown by 15% SDS-PAGE. Western blot indicated that the rCruFc specifically reacted with polyclonal rabbit anti-Fenneropenaeus chinensis CruFc. Production in a 5 l bioreactor gave 237 mg rCruFc/l. Antimicrobial assay revealed that 4 microM rCruFc inhibited growth of Staphylococcus aureus.

