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 journalArticle

1 Citation (Scopus)

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

Fingerprint

Streptomyces griseus
Lactalbumin
Pronase
lactalbumin
enzymatic treatment
Enzyme activity
Fruits
whey protein
hydrolysates
Fruit
fruit extracts
lactokinins
Proteins
Peptides
fruits
phenolic compounds
Enzymes
enzymes
Fluorescence
peptides

Keywords

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

ASJC Scopus subject areas

  • Food Science
  • Industrial and Manufacturing Engineering

Cite this

@article{7608aab4042b43b898396359dd694c85,
title = "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",
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.",
keywords = "whey protein, salal berry, protease, peptides, ACE-inhibition, BIOACTIVE PEPTIDES, MOLECULAR-STRUCTURE, IDENTIFICATION, BETA-LACTOGLOBULIN, DIGESTION, OVINE, CHEESE WHEY, ALBUMIN, YOGURT, MILK",
author = "Vassilios Raikos and Helen Hayes and David Stead and He Ni",
note = "This work is part of the Strategic Research Programme 2016-2021 and is funded by the Scottish Government's Rural and Environment Science and Analytical Services Division (RESAS).",
year = "2019",
month = "11",
doi = "10.1111/ijfs.14211",
language = "English",
volume = "54",
pages = "2975--2982",
journal = "International Journal of Food Science and Technology",
issn = "0950-5423",
publisher = "Wiley-Blackwell",
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TY - JOUR

T1 - 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

AU - Raikos, Vassilios

AU - Hayes, Helen

AU - Stead, David

AU - Ni, He

N1 - This work is part of the Strategic Research Programme 2016-2021 and is funded by the Scottish Government's Rural and Environment Science and Analytical Services Division (RESAS).

PY - 2019/11

Y1 - 2019/11

N2 - 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.

AB - 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.

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KW - peptides

KW - ACE-inhibition

KW - BIOACTIVE PEPTIDES

KW - MOLECULAR-STRUCTURE

KW - IDENTIFICATION

KW - BETA-LACTOGLOBULIN

KW - DIGESTION

KW - OVINE

KW - CHEESE WHEY

KW - ALBUMIN

KW - YOGURT

KW - MILK

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U2 - 10.1111/ijfs.14211

DO - 10.1111/ijfs.14211

M3 - Article

VL - 54

SP - 2975

EP - 2982

JO - International Journal of Food Science and Technology

JF - International Journal of Food Science and Technology

SN - 0950-5423

IS - 11

ER -