Expression of Bovine β-Casein in Saccharomyces Cerevisiae and Characterization of the Protein Produced in Vivo

Publication Date



Recombinant DNA technology offers numerous opportunities for engineering food proteins and for studying their structure-function relationship. As part of the study of structure-function of bovine caseins, it is necessary to produce mutant proteins in experimental amounts and correlate their new structure to their physiochemical characteristics. To this end, bovine β-casein was expressed in the yeast Saccharomyces cerevisia by a fusion to the HXK1 (hexokinase P1) gene. Casein was produced during late exponential/early stationary phase of growth on glucose as would be predicted for a gene under the control of the HXK1 promoter. Bovine β-casein was posttranslationally modified by yeast. Internal phosphorylated forms were observed as well as a high molecular weight form that appeared to be O-glycosylated and largely localized to the periplasmic space.


Dairy Science



URL: https://digitalcommons.calpoly.edu/dsci_fac/40