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- W2009191195 abstract "A purification method for α-D-galactosidase from Coffea canephora is described. Two enzymes, α-D-galactosidases I and II, having molecular weights of 28,000 and 36,500, respectively, were found and extensively purified. The reaction mechanism of α-D-galactosidase II was studied. The enzyme hydrolysed aryl and alkyl α-D-galactopyranosides and was severely inhibited by excess of these substrates. No inhibition occurred with raffinose. The influence of para substituents on the reaction rate of phenyl α-D-galactopyranosides, the effect of added alcohols, and the non-competitive inhibition by methyl α-D-galactopyranoside were investigated. A two-step mechanism with the formation of an enzyme-galactosyl complex is proposed. With aryl galactopyranosides, the reaction of the enzyme-galactosyl complex with water is rate-limiting. Influences of the substituents on the inhibition constant were investigated by linear free-energy relationships, and significant correlations between this constant and electronic parameters could be calculated. The influence of pH on the reaction is complex." @default.
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- W2009191195 date "1975-05-01" @default.
- W2009191195 modified "2023-09-27" @default.
- W2009191195 title "Purification and properties of coffee-bean α-D-galactosidase" @default.
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- W2009191195 doi "https://doi.org/10.1016/s0008-6215(00)87017-2" @default.
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