The α-amylase of the beetle Callosobruchus chinensis properties

C. chinensis larval amylase is activated by Ca(2+) and inhibited by Cl(-) and EDTA (K(i) 6.7x10(-3)m). GSH and 2-mercaptoethanol activate, presumably at different sites, as 2-mercaptoethanol interferes with Ca(2+) activation, whereas GSH enhances it. The inhibition by iodoacetic acid and N-ethylmaleimide (K(i) 1.55x10(-2)m) suggest that free thiol groups are essential for activity. The pH optimum of 5.2-5.4 is moved to 5.6-5.8 by Ca(2+) and 2-mercaptoethanol. The activation energy is 7270 cal/mol, and is not affected by Ca(2+) and 2-mercaptoethanol. K(m) for soluble starch is 2.3mg/ml.