14 research outputs found
Immobilization of Lipases Produced by the Endophytic Fungus Cercospora kikuchii on Chitosan Microparticles
An Efficient Binary Solvent Mixture for Monoacylglycerol Synthesis by Enzymatic Glycerolysis
Enzymatic Production of Monoacylglycerols with Camellia Oil by the Glycerolysis Reaction
Monoglyceride and Diglyceride Production Through Lipase-Catalyzed Glycerolysis and Molecular Distillation
Packed-Bed Reactor Running on Babassu Oil and Glycerol to Produce Monoglycerides by Enzymatic Route using Immobilized Burkholderia cepacia Lipase
Effect of reaction rate on converted products from wheat germ oil by immobilized lipase ethanolysis
Monoglycerides and Diglycerides Synthesis in a Solvent-Free System by Lipase-Catalyzed Glycerolysis
Construction of the yeast whole-cell Rhizopus oryzae lipase biocatalyst with high activity*
Surface display is effectively utilized to construct a whole-cell biocatalyst. Codon optimization has been proven to be effective in maximizing production of heterologous proteins in yeast. Here, the cDNA sequence of Rhizopus oryzae lipase (ROL) was optimized and synthesized according to the codon bias of Saccharomyces cerevisiae, and based on the Saccharomyces cerevisiae cell surface display system with α-agglutinin as an anchor, recombinant yeast displaying fully codon-optimized ROL with high activity was successfully constructed. Compared with the wild-type ROL-displaying yeast, the activity of the codon-optimized ROL yeast whole-cell biocatalyst (25 U/g dried cells) was 12.8-fold higher in a hydrolysis reaction using p-nitrophenyl palmitate (pNPP) as the substrate. To our knowledge, this was the first attempt to combine the techniques of yeast surface display and codon optimization for whole-cell biocatalyst construction. Consequently, the yeast whole-cell ROL biocatalyst was constructed with high activity. The optimum pH and temperature for the yeast whole-cell ROL biocatalyst were pH 7.0 and 40 °C. Furthermore, this whole-cell biocatalyst was applied to the hydrolysis of tributyrin and the resulted conversion of butyric acid reached 96.91% after 144 h