消化(炼金术)
胃蛋白酶
抗氧化剂
水解物
化学
肽
生物化学
酶
色谱法
食品科学
水解
作者
Gürkan Bilir,Mohammadreza Khalesi,María Cermeño,Richard J. Fitzgerald,Deniz Ekinci
标识
DOI:10.1021/acs.jafc.2c00578
摘要
This study investigated the characterization of proteins from the Irish limpet (Patella vulgata) and assessed the in vitro biological activities of hydrolysates obtained following gastrointestinal digestion (INFOGEST) of a limpet protein concentrate (LPC). The physicochemical properties and the digestibility of the LPC were investigated, along with the angiotensin-converting enzyme (ACE) inhibition and antioxidant activities of the LPC-digested samples. All the digested samples examined outperformed the LPC in terms of activity. Peptides were identified using LC-MS/MS after digestion. A total of 38 and 19 peptides were identified in LPC-G and LPC-GI, respectively, using a database search and a de novo approach. Most of the identified peptides had hydrophobic amino acids, which may contribute to their antioxidant and ACE inhibitory activities. The findings of this study showed that LPC has high nutritional quality with good digestibility and could serve as a potential source of antioxidative and ACE inhibitory peptides following gastrointestinal digestion.
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