Yiting Wang,Jingyi Lu,Jialei Chu,Guangrong Huang,Wenwei Chen,Zhenbao Jia,Fei Tao
{"title":"Isolation and Characteristics\nof the Novel Proteinaceous\nInhibitor against Pancreatic α-Amylase from White Kidney\nBean (\n Phaseolus vulgaris\n )","authors":"Yiting Wang,Jingyi Lu,Jialei Chu,Guangrong Huang,Wenwei Chen,Zhenbao Jia,Fei Tao","doi":"10.1021/acs.jafc.6c12164","DOIUrl":null,"url":null,"abstract":"Abstract A novel proteinaceous α-amylase inhibitor was isolated from white kidney bean (Phaseolus vulgaris) by ammonium sulfate fractionation followed by DEAE-Sepharose Fast Flow and HiTrap DEAE-Sepharose Fast Flow chromatography. The purified inhibitor was identified as annexin (UniProt accession: V7BSM8) by HPLC-MS/MS, with a molecular mass of 35.97 kDa determined by MALDI-TOF MS. Annexin inhibited pancreatic α-amylase in a concentration-dependent manner, with an IC50 of 8.81 μM. The kinetic results were consistent with a noncompetitive inhibition pattern. Intrinsic fluorescence spectroscopy indicated that annexin binding to α-amylase induced static fluorescence quenching and conformational changes in the enzyme. Molecular dynamics simulations supported formation of a stable α-amylase–annexin complex, with electrostatic and van der Waals interactions as major energetic contributors. These findings identify annexin as a previously unrecognized α-amylase inhibitor from P. vulgaris with potential for modulating starch digestion and postprandial glycemic responses.","PeriodicalId":41,"journal":{"name":"Journal of Agricultural and Food Chemistry","volume":"12 1","pages":""},"PeriodicalIF":6.7000,"publicationDate":"2026-10-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Agricultural and Food Chemistry","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1021/acs.jafc.6c12164","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"AGRICULTURE, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 0
Abstract
Abstract A novel proteinaceous α-amylase inhibitor was isolated from white kidney bean (Phaseolus vulgaris) by ammonium sulfate fractionation followed by DEAE-Sepharose Fast Flow and HiTrap DEAE-Sepharose Fast Flow chromatography. The purified inhibitor was identified as annexin (UniProt accession: V7BSM8) by HPLC-MS/MS, with a molecular mass of 35.97 kDa determined by MALDI-TOF MS. Annexin inhibited pancreatic α-amylase in a concentration-dependent manner, with an IC50 of 8.81 μM. The kinetic results were consistent with a noncompetitive inhibition pattern. Intrinsic fluorescence spectroscopy indicated that annexin binding to α-amylase induced static fluorescence quenching and conformational changes in the enzyme. Molecular dynamics simulations supported formation of a stable α-amylase–annexin complex, with electrostatic and van der Waals interactions as major energetic contributors. These findings identify annexin as a previously unrecognized α-amylase inhibitor from P. vulgaris with potential for modulating starch digestion and postprandial glycemic responses.
期刊介绍:
The Journal of Agricultural and Food Chemistry publishes high-quality, cutting edge original research representing complete studies and research advances dealing with the chemistry and biochemistry of agriculture and food. The Journal also encourages papers with chemistry and/or biochemistry as a major component combined with biological/sensory/nutritional/toxicological evaluation related to agriculture and/or food.