Expression, purification, and characterization of recombinant Chinese shrimp crustin-like protein (CruFc) in Pichia pastoris.
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.
Zhang
Jiquan
J
Institute of Oceanology, Chinese Academy of Sciences, Qingdao, 266071, PR China.
Li
Fuhua
F
Wang
Zaizhao
Z
Xiang
Jianhai
J
D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification*; D018533:Biomass; D005285:Fermentation / Q000187:drug effects; D015870:Gene Expression / Q000187:drug effects; D000432:Methanol / Q000494:pharmacology; D010100:Oxygen / Q000378:metabolism; D033561:Penaeidae / Q000737:chemistry* / Q000187:drug effects; D010843:Pichia / Q000187:drug effects / Q000235:genetics*; D010957:Plasmids; D011994:Recombinant Proteins / Q000235:genetics* / Q000302:isolation & purification*; D013997:Time Factors
D023181:Antimicrobial Cationic Peptides; D011994:Recombinant Proteins; D010100:Oxygen; D000432:Methanol