ArticleMolecules (Basel, Switzerland)2021
The Procyanidin C1-Dependent Inhibition of the Hydrolysis of Potato Starch and Corn Starch Induced by Pancreatin.
Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 5 citations in OpenAlex.
- Applying Isothermal Titration Calorimetry and Saturation Transfer Difference-NMR to Study the Mode of Interaction of Flavan-3-ols with α-Amylase to Understand Their Impact on Starch Hydrolysis.Journal of agricultural and food chemistry · 2025Article
- Article
- Further slowing down of hydrolysis of amylose heated with black soybean extract by treating with nitrite under gastric conditions.Scientific reports · 2022Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Procyanidins are contained in various foods, and their effects on starch hydrolysis have been reported. In Japan, black soybeans, which contain a trimeric procyanidin, procyanidin C1 (proC1), are cooked with rice and used to prepare dumplings. In this study, the effects of proC1 on the pancreatin-induced formation of reducing sugars and starch hydrolysis were studied using potato starch and corn starch. ProC1 inhibited both reactions; the inhibition was greater in potato starch than corn starch when added to heated potato starch and corn starch. When heated with proC1, its inhibitory effects decreased, especially in potato starch, suggesting the important role of proC1 itself for the inhibition of potato starch hydrolysis. ProC1 also inhibited the hydrolysis when added to heated, longer amylose (average molecular weight: 31,200), and the inhibition decreased when heated with the amylose. On the other hand, proC1 could not inhibit the hydrolysis when added to heated, shorter amylose (average molecular weight: 4500), but could when heated with the amylose, suggesting the important role of the degradation products of proC1 for the inhibition. We discuss the mechanism of the proC1-dependent inhibition of amylose hydrolysis, taking the molecular weight into account.
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