Expression and Secretion of Bovine β-Lactoglobulin In Saccharomyces cerevisiae

Abstract

A bovine β-Mactoglobulin (β-LG) was expressed in Saccharomyces cerevisiae carrying bovine pre-β-LG cDNA and secreted into its growth medium. The expression plasmid was constructed by inserting the whole coding region of the cDNA encoding pre-β-LG between the promoter and terminator of the yeast glyceraldehyde 3-phosphate dehydrogenase gene of pYG100, a yeast expression vector. In the supernatant of the yeast growth medium, β-LG with a native conformation was detected by sandwich ELISA, and its amount was estimated to be 1.1 mg/1. A Western-immunoblotting analysis revealed that β-LG secrected in the growth medium had the same mobility as that of authentic bovine β-LG. The N-terminal sequence was also identical with that of authentic mature bovine β-LG. © 1990, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.