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Expression, purification, and characterization of recombinant Chinese shrimp crustin-like protein (CruFc) in Pichia pastoris

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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 μM rCruFc inhibited growth of Staphylococcus aureus.

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Acknowledgements

This work was supported by Major State Basic Research development Program of China (2006CB101804) and Key Program of National Natural Science Foundation of China (30230280).

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Correspondence to Jianhai Xiang.

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Zhang, J., Li, F., Wang, Z. et al. Expression, purification, and characterization of recombinant Chinese shrimp crustin-like protein (CruFc) in Pichia pastoris . Biotechnol Lett 29, 813–817 (2007). https://doi.org/10.1007/s10529-007-9317-6

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  • DOI: https://doi.org/10.1007/s10529-007-9317-6

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