Inhibition of Rhizomucor miehei and Candida rugosa Lipases by D-Glucose in Esterification between L-Alanine and D-Glucose(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)
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概要
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A detailed kinetic study of the esterification of D-glucose with L-alanine catalyzed by Upases from Rhizomucor miehei(RML) and Candida rugosa(CRL) showed that both lipases follow the Ping-Pong Bi-Bi mechanism, in which L-alanine and D-glucose bind in subsequent steps releasing water and L-alanyl-D-glucose, with competitive substrate inhibition by D-glucose at higher concentrations leading to the formation of dead-end lipase・D-glucose complexes. An attempt to obtain the best fit of this kinetic model through curve fitting yielded good approximates of the apparent values of four important kinetic parameters: for RML-k_<cat>=0.29±0.028x10^3 M h^<-1> mg^<-1>, K_<mL-alanine>=4.9±0.51x10^<-3>M, K_<mD-glucose>=0.21±0.018x10^<-3> 0.75±0.08x10^<-3>Mh^<-1>mg^<-1>, K_<mL-alanine>=56.2±5.7x10^<-3>M, K_<mD-glucose>=16.2±1.8x10^<-3>M, and K_<iD-glucose>=21.0±1.9x10^<-3>M.
- 社団法人日本生物工学会の論文
- 2007-02-25
著者
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Divakar Soundar
Department Of Fermentation Technology And Bioengineering Central Food Technological Research Institu
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Somashekar Bhandya
Department of Fermentation Technology and Bioengineering, Central Food Technological Research Instit
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Lohith Kenchaiah
Department of Fermentation Technology and Bioengineering, Central Food Technological Research Instit
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Manohar Balaraman
Department of Food Engineering, Central Food Technological Research Institute
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Lohith Kenchaiah
Department Of Fermentation Technology And Bioengineering Central Food Technological Research Institu
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Manohar Balaraman
Department Of Food Engineering Central Food Technological Research Institute
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Somashekar Bhandya
Department Of Fermentation Technology And Bioengineering Central Food Technological Research Institu