Abstract
The effect of side-chain density on the kinetic parameters of a side-chain-cleaving hemicellulase was determined. Kinetic parameters were based on the rate of Trichoderrra reesei α-galactosidase-catalyzed liberation of galactose from galactomannan (guar and locust bean) substrates. The focus enzyme was the predominant α-galactosidase obtained from the fungus' galactomannan-supplemented cell-free culture medium. Substrate concentrations were based on the number of galactosyl moieties per volume reaction mixture. The K m values for the galactomannan substrates differed approximately 4.3-fold (28.36 and 121.16 μM), the more branched substrate having the higher K m . In contrast, the corresponding V max values were found to be essentially the same. The results indicate the enzyme preferentially acts at sites of low side-chain density.
Published Version
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