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Effect of organic solvents on the activity of glucoamylase
Author(s) -
Nagamoto H.,
Yasuda T.,
Inoue H.
Publication year - 1986
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260280807
Subject(s) - maltose , maltotriose , chemistry , methanol , ethylene glycol , aqueous solution , starch , ethanol , reaction rate constant , organic chemistry , glycerol , kinetics , chromatography , enzyme , physics , quantum mechanics
Hydrolyses of maltose, maltotriose, and soluble starch catalyzed by glucoamylase ( Asp. Niger ) were carried out in the aqueous solutions of methanol, ethanol, ethylene glycol, and 1,4‐dioxane at 40°C and at the optimum pH in the respective solutions. By the kinetic analysis based on the subsite model, it was shown that the intrinsic rate constant, K int , was electrostatically affected by the dielectric constant of the hydroorganic solutions. The affinity of the third subsite, A 3 , which affects the apparent rate constant, K 0 , was correlated with the × G tr 's of maltose and amino acid side chains.