详细信息
Interaction between oyster peptides and anthocyanins: Stability improvement, structure changes and α-amylase and α-glucosidase inhibition effect ( SCI-EXPANDED收录 EI收录)
文献类型:期刊文献
英文题名:Interaction between oyster peptides and anthocyanins: Stability improvement, structure changes and α-amylase and α-glucosidase inhibition effect
作者:Zhong, Kaicui[1,2];Jiang, Meiling[1,2];Cao, Wenhong[1,2];Gao, Jialong[1];Zheng, Huina[1,2];Lin, Haisheng[1];Qin, Xiaoming[1];Chen, Zhongqin[1,2]
机构:[1]Guangdong Ocean Univ, Coll Food Sci & Technol, Natl Res & Dev Branch, Guangdong Prov Engn Technol Res Ctr Seafood,Ctr Sh, Zhanjiang 524088, Peoples R China;[2]Guangdong Ocean Univ, Shenzhen Inst, Shenzhen 518120, Peoples R China
年份:2025
卷号:221
外文期刊名:LWT-FOOD SCIENCE AND TECHNOLOGY
收录:SCI-EXPANDED(收录号:WOS:001442188200001)、、EI(收录号:20251017996562)、Scopus(收录号:2-s2.0-85219495954)、WOS
基金:This work was financially supported by the National Natural Science Foundation of China (32201971) , the Guangdong Basic and Applied Basic Research Foundation (2024A1515011763) , the Science and Technology Plan Project of Zhanjiang City (2021E05017) , the Guangdong Basic and Applied Basic Research Foundation (2021A1515110621) , the Program for scientific research start-up funds of Guangdong Ocean University (060302042007) and China Agriculture Research System of MOF and MARA (CARS-49) .
语种:英文
外文关键词:Oyster peptides; Anthocyanins; Interaction; Stability; Hypoglycemic activity
外文摘要:The purpose of the present work was to create the oyster peptides (OPs)-black soybean seed coat anthocyanins (ACNs) complexes, investigate their stability improvement, interactions and alpha-amylase and alpha-glucosidase inhibition effect. The stability analysis results showed that OPs could effectively improve the stabilities (solution, light and pH stability) of ACNs. Interaction characterization demonstrated that the interaction between ACNs and OPs primarily involved hydrogen bonding, electrostatic forces, and hydrophobic interactions. OPs-ACNs complexes possessed significant inhibitory activity against alpha-glucosidase (88.6% when 3 mg/mL, Kic 1.05 mg/ mL) and alpha-amylase (64.68% when 3 mg/mL, Kic 0.04 mg/mL and Kiu 0.07 mg/mL). Moreover, the enzyme inhibition kinetic analysis indicated that ACNs-OPs exhibit competitive inhibition towards alpha-glucosidase and mixed inhibition towards alpha-amylase, with competitive inhibition being the predominant type. Altogether, the results suggested that OPs complex with ACNs could effectively improve ACNs' stability and hypoglycemic effect in vitro through non-covalent interactions.
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