Add time:08/20/2019         Source:sciencedirect.com

1.1.|The competitive inhibition and barley malt α-glucosidase (α-d-glucoside glucohydrolase, EC 2.3.1.20) with Tris and erythritol has been studied in the pH interval 3–7 with maltose as substrate.2.2.|At pH 4.6, Tris and erythritol compete with each other and with maltose for the enzyme.3.3.|The variation of the inhibitor constant for Tris and erythritol and of the Michaelis constant for maltose with pH, shows that Tris and maltose react with different groups in the enzyme, which makes it unlikely that Tris is a substrate analogue.4.4.|Erythritol requires 2 groups in the enzyme and competes with maltose for one of the groups.

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