인문학
사회과학
자연과학
공학
의약학
농수해양학
예술체육학
복합학
DBpia AI
AI 에이전트
AI 아이디어
AI 리더
AI 뷰어
Citeasy
크롬 서지관리 다운로드
지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
초록·키워드
Abstract This study focused on the production of angiotensin‐converting enzyme inhibitory peptides (ACEIPs) from peanut meal ( Arachis hypogaea Linn) fermented by Lactobacillus pentosus . The fermentation process was optimized using the response surface methodology with ACE inhibitory activity as the experimental indicator. ACEIPs were further purified after fermentation using ultrafiltration and Sephadex G‐25 gel chromatography. The effect of different molecular weights (ranging from 0.5 to 1.5 kDa) of ACEIP on ACE inhibitory activity was investigated, and a maximum inhibitory rate of 48.83% was achieved. The content of ACEIP was 78.95%. Amino acid analysis revealed that the hydrophobic amino acids accounted for 43.09% of the total content. Among the identified amino acids, glutamic acid had the highest content of 14.94%, followed by leucine and aspartic acid. Matrix‐assisted laser desorption/ionization time‐of‐flight–mass spectrometry (MS) and liquid chromatography–tandem MS were used to identify the molecular weights of the selected ACEIPs, yielding six ACEIPs with good stability and high hydrophilicity. Flexible docking of the six ACEIPs with ACE was simulated using AutoDock Vina (v1.5.7). The result showed that the ACEIPs formed 11, 8, 7, 9, 7, and 6 hydrogen bonds with ACE residues, and the lowest binding energies between them were −9.8, −8.1, −9.0, −9.3, −8.2, and−9.1 kcal/mol, respectively. Among them, GFGINAENNHRIF exhibited superior ACE inhibitory activity and binding stability.
인공지능 문자 인식 모델을 통해 추출된 텍스트로, 일부 오타나 오류가 포함될 수 있으나 지속적으로 개선 중입니다.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.
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