Extraction and Characterization of Protein Concentrates from Limpets (Patella vulgata) and Peptide Release Following Gastrointestinal Digestion


Bilir G., Khalesi M., Cermeno M., FitzGerald R. J., EKİNCİ D.

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, cilt.70, sa.36, ss.11212-11223, 2022 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 70 Sayı: 36
  • Basım Tarihi: 2022
  • Doi Numarası: 10.1021/acs.jafc.2c00578
  • Dergi Adı: JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Analytical Abstracts, Applied Science & Technology Source, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, Chemical Abstracts Core, Chimica, Compendex, EMBASE, Environment Index, Food Science & Technology Abstracts, MEDLINE, Pollution Abstracts, Veterinary Science Database, DIALNET
  • Sayfa Sayıları: ss.11212-11223
  • Anahtar Kelimeler: Patella vulgata, PDCAAS, peptide, solubility, ACE inhibitor, antioxidant, in vitro bioactivity, digestibility, limpet, ANGIOTENSIN-CONVERTING ENZYME, WHITING MICROMESISTIUS-POUTASSOU, FATTY-ACID PROFILE, IN-VITRO, PROXIMATE COMPOSITION, BIOACTIVE PEPTIDES, FUNCTIONAL-PROPERTIES, NUTRITIONAL-VALUE, BY-PRODUCT, ANTIOXIDANT
  • Ondokuz Mayıs Üniversitesi Adresli: Evet

Özet

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.