The * hydrolase enzyme that catalyses the hydrolysis of the α(l-4) glucosidic bonds in starch. Amylase occurs in two forms, designated α and β. β-amylase only attacks the nonreducing ends of a starch molecule, successively hydrolysing alternate α(l-4) linkages and releasing maltose molecules. β-amylase is found in germinating seeds and is important for the production of malt in the brewing industry. Amylose is completely degraded to maltose by β-amylase but amylopectin is only partially broken down because the β-amylase cannot attack α(l-4) linkages beyond the first branch on each chain. A separate enzyme, α(l-6)-glucosidase, exists to hydrolyse the α(l-6) branching linkages of amylopectin. α-amylase differs from β-amylase in that it can attack α(l-4) bonds within the starch molecule. It thus degrades amylopectin more completely than β-amylase. |
