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.
摘要：
研究了从面筋蛋白水解物中分离的面筋肽（GP）对糊化小麦淀粉的体外淀粉分解的影响。将胃蛋白酶水解产物中的GP分级分离成分子量(MWs)为500-3000、3500-7000、10-17和35-48kDa的级分。含有分子量>10kDa的肽的组分对酶活性和淀粉的淀粉分解具有很强的抑制作用，而MW<10kDa的GPs没有抑制作用。通过表面等离子体共振估计的结合常数表明，分子量>10kDa的级分中的肽与α-淀粉酶结合得更强，与MW<10kDa的肽相反。在消化参数和平衡结合亲和力之间观察到显着相关性。我们得出的结论是，面筋胃蛋白酶消化物中MW>10kDa的肽对淀粉的体外酶促水解具有很强的抑制作用，因为它们对α-淀粉酶具有很强的结合亲和力。
