Abstract

This study investigated the effect of endogenous proteins on the α-amylase-catalyzed hydrolysis of gelatinized corn starch, to analyze the influence of starch granule-associated protein (SGAP) and storage protein on the hydrolytic reaction and the structure of the hydrolysate molecules. The effect of chemicals that disrupted starch/protein binding interactions on the rheology of gelatinized starch revealed the mechanism of starch hydrolysis inhibition. Native corn starch had a lower degree of hydrolysis and a higher proportion of incompletely hydrolyzed long chains than corn starch with the SGAP removed. Storage protein also inhibited starch hydrolysis, but less strongly than SGAP. Rheological analysis showed that SGAP interacted strongly with starch chains by hydrogen bonding, hydrophobic and electrostatic interactions, whereas storage protein only interacted strongly by hydrogen bonding. The stronger binding interactions between SGAP and starch appeared to be the main reason for its stronger inhibition of starch hydrolysis than that of storage protein.

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