{Reference Type}: Journal Article
{Title}: Inhibition of In Vitro Amylolysis of Wheat Starch by Gluten Peptides.
{Author}: Xiong Y;Gu C;Yu J;Copeland L;Wang S;
{Journal}: J Agric Food Chem
{Volume}: 71
{Issue}: 19
{Year}: 2023 May 17
{Factor}: 5.895
{DOI}: 10.1021/acs.jafc.3c01434
{Abstract}: The effect of gluten peptides (GPs) isolated from a gluten proteolysate on in vitro amylolysis of gelatinized wheat starch was investigated. GPs in a pepsin hydrolysate were fractionated into fractions with molecular weights (MWs) of 500-3000, 3500-7000, 10-17, and 35-48 kDa. The fractions containing peptides with MW > 10 kDa had a strong inhibitory effect on enzyme activity and amylolysis of starch, whereas GPs with MW <10 kDa had no inhibitory effect. Binding constants estimated by surface plasmon resonance showed that peptides in the fractions with MW > 10 kDa bound more strongly to α-amylase, in contrast to peptides of MW <10 kDa. Significant correlations were observed between digestion parameters and equilibrium binding affinity. We conclude that peptides with MW >10 kDa in a pepsin digest of gluten have a strong inhibitory effect on in vitro enzymatic hydrolysis of starch due to their strong binding affinity to α-amylase.