원문정보
초록
영어
Expression of proteins on the cell surface of Saccharomyces cerevisiae offers more advantages than other microbial systems, since it allows the folding and glycosylation of expressed heterologous eukaryotic proteins and can be subjected to many genetic manipulations. The endoxylanase gene from Bacillus sp. was expressed on the cell surface of S. cerevisiae by fusing with Aga2p linked to the membrane anchored protein, Aga1p. The endoxylanase gene was subcloned into the surface display vector, pCTcon (GAL1 promoter). The constructed
plasmid, pCTXYN (6.8 kb) was introduced to S. cerevisiae EBY100 cell and then yeast transformants were selected on the synthetic defined media lacking uracil. When the yeast transformants were grown on YPD medium, the total activity of the enzyme reached about 1.92 unit/ml. To produce efficiently xylooligosaccharide from xylan, various reaction conditions were examined. When the oat spelts xylan was hydrolyzed by treatment of cell surface-displayed
endoxylanase, it was found that xylose, xylobiose, and xylotriose were produced, and xylotriose was the main product.