Cell surface display of Candida antarctica lipase A by saccharomyces cerevisiae and its practical properties

Abstract:

Lipase A gene of Candida Antarctica (cala) was displayed for the first time on the surface of Saccharomyces cerevisiae using a-agglutinin as an anchor protein, recombinant strains were screened on minimal dextrose plates. Results of immunofluorescence microscopy assay revealed that the CALA-a-agglutinin fusion proteins were successfully anchored on the S. cerevisiae cell surface. Furthermore, yeast displayed CALA produced halo on the MD plate containing tributyrin, suggesting that CALA was active on the cell wall. Yeast displayed CALA displayed maximal activity after 72 h cultivation in YNB-CAA medium, with an activity of 80.4 U/g dry cells. The optimal temperature and pH for yeast displayed CALA were 70 °C and pH 8.0, respectively. It remained 60% of activity after incubation at 50 °C for 2 h and the lipase still remained 70% activity after incubated in buffer containing 30% dimethyl sulfoxide for 2 h. Those properties make yeast displayed CALA great potential for industrial application.