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.