Somashekar_2007_J.Biosci.Bioeng_103_122

A detailed kinetic study of the esterification of D-glucose with L-alanine catalyzed by lipases 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(m L-alanine)= 4.9+/-0.51x10(-3) M, K(m D-glucose)=0.21+/-0.018x10(-3) M, and K(i D-glucose)=1.76+/-0.19x10(-3) M; for CRL-k(cat)= 0.75+/-0.08x10(-3) M h(-1) mg(-1), K(m L-alanine)=56.2+/-5.7x10(-3) M, K(m D-glucose)=16.2+/-1.8x10(-3) M, and K(i D-glucose) =21.0+/-1.9x10(-3) M.