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

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 enzy...

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Bibliographic Details
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
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Summary: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.
ISSN:0003-6838
1608-3024
DOI:10.1134/S0003683811080114