文献类型：期刊文献

英文题名：Structure-function insights into the digestive fate of angiotensin-converting enzyme-inhibitory peptides from microwave-treated corn gluten meal

作者：Hamzeh, Ali Wongngam, Wasana Roytrakul, Sittiruk Aueviriyavit, Sasitorn Wongwanakul, Ratjika Tian, Fu Yongsawatdigul, Jirawat Aluko, Rotimi E.

第一作者：Hamzeh, Ali

通信作者：Yongsawatdigul, J[1]

机构：[1]Suranaree Univ Technol, Inst Res & Dev, Nakhon Ratchasi 30000, Thailand;[2]Suranaree Univ Technol, Inst Agr Technol, Sch Food Technol, Nakhon Ratchasi 30000, Thailand;[3]Rajamangala Univ Technol, Fac Agr & Technol, Dept Agroind, Isan SURIN Campus, Surin 32000, Thailand;[4]Natl Ctr Genet Engn & biotechnol, Pathum Thani 12120, Thailand;[5]Natl Sci & Technol Dev Agcy, Natl Nanotechnol Ctr, 111 Thailand Sci Pk, Pathum Thani 12120, Thailand;[6]Guizhou Inst Technol, Coll Food & Pharmaceut Engn, Guiyang 550000, Peoples R China;[7]Univ Manitoba, Dept Food & Human Nutr Sci, Winnipeg, MB R3T 2N2, Canada

第一机构：Suranaree Univ Technol, Inst Res & Dev, Nakhon Ratchasi 30000, Thailand

通信机构：corresponding author), Suranaree Univ Technol, Inst Agr Technol, Sch Food Technol, Nakhon Ratchasi 30000, Thailand.

年份：2026

卷号：13

外文期刊名：FOOD CHEMISTRY: MOLECULAR SCIENCES

收录：Scopus(收录号：2-s2.0-105045200169);WOS:【ESCI(收录号:WOS:001825604300001)】；

基金：This research was supported by National Research Council of Thailand (N42A650548). Additional funding was received from the Office of the Permanent Secretary of the Ministry of Higher Education, Science, Research, and Innovation. A full-time researcher fellowship was provided to AH by Suranaree University of Technology.

语种：英文

外文关键词：Bioactive peptides; Molecular dynamics; Caco-2 permeability; Gastrointestinal digestion

摘要：Corn gluten meal (CGM) is an underutilized byproduct with rigid structure, which limits efficient peptide release during enzymatic hydrolysis. While microwave pretreatment can disrupt the rigid CGM matrix and enhance peptide release, this study investigated how downstream gastrointestinal modification and transport behavior ultimately influence the functional fate of the enzymatically liberated peptide sequences. Enzymatic hydrolysis of microwave-pretreated CGM led to a 3.3-fold increase in peptide yield while maintaining angiotensin-converting enzyme (ACE)-inhibitory activity at a level comparable to that of the untreated CGM hydrolysate. From this digest, the purified peptide DVPSADAPAAAV (DV-12) exhibited potent in vitro ACE inhibition (IC50 = 57 mu M). Simulated gastrointestinal digestion partially hydrolyzed DV-12 to DVPSADAPAAA (DA-11), a minor structural modification that was overestimated by in silico digestion models yet resulted in a substantial reduction in ACE-inhibitory potency. Kinetic analysis and molecular dynamics simulations revealed that this truncation fundamentally altered peptide-ACE interactions: DV-12 (K; = 8 mu M) maintained more stable coordination near the ACE Zn2+ catalytic center, whereas DA-11 displayed substantially weaker binding (K; = 1.06 mM). In Caco-2 monolayers, both peptides crossed the epithelial barrier at low rates, with apparent permeability coefficients of 9.96 & times; 10-8 and 8.23 & times; 10-8 cm & sdot;s-1 for DV-12 and DA-11, respectively, while unabsorbed peptide fractions, particularly DV-12, concurrently reduced intracellular reactive oxygen species. These findings demonstrated that increasing peptide yield alone does not guarantee preserved downstream functionality, as subtle structural modifications occurring during digestion and transport toward absorption could markedly alter peptide bioactivity and should therefore be considered in the development of functional food ingredients.