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

Vasileios Raikos (Corresponding Author), Helen Hays, David Stead, He Ni

Research output: Contribution to journalArticle

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
JournalInternational Journal of Food Science and Technology
Early online date29 May 2019
DOIs
Publication statusE-pub ahead of print - 29 May 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

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",
author = "Vasileios Raikos and Helen Hays 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 = "5",
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doi = "10.1111/ijfs.14211",
language = "English",
journal = "International Journal of Food Science and Technology",
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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, Vasileios

AU - Hays, 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 - 2019/5/29

Y1 - 2019/5/29

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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