Related Experiment Video
Updated: Jul 13, 2026

Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 25, 2010
Heterologous expression of bovine lactoferricin in Pichia methanolica
Haikuan Wang1, Xinhuai Zhao, Fuping Lu
1Key Lab of Diary Science, Ministry of Education, Harbin, PO 150030, P. R. China. hkwang@tust.edu.cn
Abstract:
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.
Related Concept Videos
Production of Pharmaceuticals
Microbial Fermentation

