Enzymatic properties of α-d-galactosidase from Trichoderma reesei☆

@inproceedings{Savelev1996EnzymaticPO,
  title={Enzymatic properties of α-d-galactosidase from Trichoderma reesei☆},
  author={Andrew N. Savel'ev and Farid M. Ibatyllin and Elena V. Eneyskaya and Anatoly M. Kachurin and Kirill N. Neustroev},
  year={1996}
}
Abstract The kinetics of hydrolysis of a number of natural and synthetic substrates [melibiose, raffinose, stachyose, methyl α- d -galactopyranoside, and p-nitrophenyl α- d -galactopyranoside (PNPG)], catalyzed by α- d -galactosidase from the fungus Trichoderma reesei, has been studied. A number of N-acyl-α-d-galactopyranosylamines, which are competitive inhibitors of α- d -galactosidase, have been synthesized, and the KI values for these compounds have been obtained. The inhibiting properties… CONTINUE READING