Heterologous expression of bovine lactoferricin in Pichia methanolica.
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 alpha-factor signal peptide. The alpha-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.
Wang
Haikuan
H
Key Lab of Diary Science, Ministry of Education, Harbin, PO 150030, P. R. China. hkwang@tust.edu.cn
Zhao
Xinhuai
X
Lu
Fuping
F
D000429:Alcohol Oxidoreductases / Q000235:genetics; D000818:Animals; D002417:Cattle; D003001:Cloning, Molecular; D005822:Genetic Vectors / Q000235:genetics; D007781:Lactoferrin / Q000096:biosynthesis* / Q000235:genetics / Q000494:pharmacology; D008826:Microbial Sensitivity Tests; D010843:Pichia / Q000235:genetics*; D011401:Promoter Regions, Genetic; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000302:isolation & purification / Q000494:pharmacology
D011994:Recombinant Proteins; C082171:lactoferricin B; D000429:Alcohol Oxidoreductases; C019643:alcohol oxidase; D007781:Lactoferrin