Capacity of N- and C-domains of Saccharomyces cerevisiae flo1p cell wall protein homologue to expose lip2 lipase on cell surface of Yarrowia lipolytica yeast

• Published in: Applied biochemistry and microbiology 2011-12, Vol.47 (8), p.744-753
• Main Authors: Yuzbasheva, E. Yu, Yuzbashev, T. V, Konstantinova, T. K, Laptev, I. A, Perkovskaya, N. I, Sineokii, S. P
• Format: Article
• Language: English
• Subjects: Biochemistry; Biomedical and Life Sciences; Biotechnology; Cell culture; Cell surface; Cell walls; Cellular biology; culture media; Data processing; Enzymes; Genomic analysis; Immobilization; Life Sciences; Medical Microbiology; Microbiology; Proteins; Saccharomyces cerevisiae; Triacylglycerol lipase; Yarrowia lipolytica; Yeast; Yeasts
• ISSN: 0003-6838; 1608-3024
• DOI: 10.1134/S0003683811080114

The closest homologue of the Saccharomyces cerevisiae Flo1p cell wall protein was detected in Yarrowia lipolytica yeast (YALI0C09031p) by the method of genomic analysis, and capacity of its N- and C-domains to expose the Lip2 lipase on the cell surface was studied. The efficient fixation of the enzyme on the Y. lipolytica cell wall surface was demonstrated. The activity of the cell-bound lipase was 9170 and 3200 units per 1 g of dry solid matter when using N- and C-domains of the cell wall protein, respectively. At the same time, in the case of immobilization using the N-domain, approximately 30% of the total lipase activity was detected in the culture medium, whereas when using C-domain of the cell wall protein YALI0C09031p, practically all lipase was in the immobilized state. Obtained values of the level of the cell-bound lipase activity considerably exceed previously published data opening a prospect for new technological solutions which meet industrial needs.