Screening of key dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from casein hydrolysates based on peptidomics, chemometrics, recombination, and omission experiments
{"title":"Screening of key dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from casein hydrolysates based on peptidomics, chemometrics, recombination, and omission experiments","authors":"Sijie Wang, Minzhi Zhou, Jingjing Qian, Danyin Yang, Lin Zheng, Mouming Zhao","doi":"10.1016/j.foodchem.2025.146639","DOIUrl":null,"url":null,"abstract":"Casein is considered a good source for preparing dipeptidyl-peptidase IV (DPP-IV) inhibitory peptides. However, the contributions of identified DPP-IV inhibitory peptides in actual casein hydrolysates to the overall activities remain unclear. This study screened the key DPP-IV inhibitory peptides in the casein hydrolysate generated with proteaxh (CXH) by peptidomics, chemometrics, recombination, and omission experiments. Our results showed that Xaa-Pro-Xaa-Pro-type (XPXP-type) peptides with 4–8 residues and other Xaa-Pro-type (XP-type) peptides with 2–5 residues, especially containing an N-terminal residue (Ile, Leu, Val, Ala, Met, Phe, Gly, and Tyr) contributed greatly to CXH. CXH (900 mg/kg) showed an obvious hypoglycemic effect <em>in vivo</em>. Nine novel DPP-IV inhibitory peptides (MPIQ, APFPEVF, MPIQA, APFP, YPE, MPFP, LPLP, FPEVF, and APFPEV) were identified. Twenty screened XP-type peptides accounted for 39.69 % and 45.16 % of the DPP-IV inhibitory activities of CXH and its digest, and LPVP showed the highest contribution value (over 9 %).","PeriodicalId":318,"journal":{"name":"Food Chemistry","volume":"108 1","pages":""},"PeriodicalIF":9.8000,"publicationDate":"2025-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Chemistry","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1016/j.foodchem.2025.146639","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
引用次数: 0
Abstract
Casein is considered a good source for preparing dipeptidyl-peptidase IV (DPP-IV) inhibitory peptides. However, the contributions of identified DPP-IV inhibitory peptides in actual casein hydrolysates to the overall activities remain unclear. This study screened the key DPP-IV inhibitory peptides in the casein hydrolysate generated with proteaxh (CXH) by peptidomics, chemometrics, recombination, and omission experiments. Our results showed that Xaa-Pro-Xaa-Pro-type (XPXP-type) peptides with 4–8 residues and other Xaa-Pro-type (XP-type) peptides with 2–5 residues, especially containing an N-terminal residue (Ile, Leu, Val, Ala, Met, Phe, Gly, and Tyr) contributed greatly to CXH. CXH (900 mg/kg) showed an obvious hypoglycemic effect in vivo. Nine novel DPP-IV inhibitory peptides (MPIQ, APFPEVF, MPIQA, APFP, YPE, MPFP, LPLP, FPEVF, and APFPEV) were identified. Twenty screened XP-type peptides accounted for 39.69 % and 45.16 % of the DPP-IV inhibitory activities of CXH and its digest, and LPVP showed the highest contribution value (over 9 %).
期刊介绍:
Food Chemistry publishes original research papers dealing with the advancement of the chemistry and biochemistry of foods or the analytical methods/ approach used. All papers should focus on the novelty of the research carried out.