Angiotensin‐converting enzyme inhibitory activity of hydrolysates generated from whey protein fortified with salal fruits (Galtheria shallon) by enzymatic treatment with Pronase from Streptomyces griseus

Vassilios Raikos* (Corresponding Author), Helen Hayes, David Stead, He Ni

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)
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Abstract

Whey proteins mixed with salal fruits extract (0% - 20% w/w) were hydrolyzed with Pronase E from Streptomyces griseus for a period of 8 h. The ACE inhibitory activity of the hydrolysates was highest (IC50: 0.087 mg/mL) for samples fortified with the highest extract concentration (20%). Peptides (>7 amino acids) with documented ACE inhibitory activity (DAQSAPLRVY, ALPMHIR, DKVGINY, LHLPLPL, YPFPGPI, YPFPGPIPN, VYPFPGPIPN) were identified bv LC-MS/MS data analysis using a database search approach. Fluorescence spectra of the whey proteins mixed with salal fruits extract indicates fluorescence quenching for α-lactalbumin. SDS-PAGE analysis suggests that α-lactalbumin is less susceptible to proteolysis when the extract is included in the formula. Data indicate that α-lactalbumin may be interacting with phenolic compounds naturally present in salal fruits. These interactions and the formation of complexes between a-Lac and phenolic compounds may affect the hydrolysis pattern of whey protein and the release of peptides with ACE-inhibitory activity.
Original languageEnglish
Pages (from-to)2975-2982
Number of pages8
JournalInternational Journal of Food Science and Technology
Volume54
Issue number11
Early online date29 May 2019
DOIs
Publication statusPublished - Nov 2019

Keywords

  • whey protein
  • salal berry
  • protease
  • peptides
  • ACE-inhibition
  • BIOACTIVE PEPTIDES
  • MOLECULAR-STRUCTURE
  • IDENTIFICATION
  • BETA-LACTOGLOBULIN
  • DIGESTION
  • OVINE
  • CHEESE WHEY
  • ALBUMIN
  • YOGURT
  • MILK

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