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 |
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Authors: | Vassilios Raikos Helen Hays David Stead He Ni |
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Affiliation: | 1. Rowett Institute, University of Aberdeen, Foresterhill, Aberdeen, AB25 2ZD UK;2. Guangdong Provincial Key Lab of Biotechnology for Plant Development, School of Life Sciences, South China Normal University, Guangzhou, 510631 China |
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Abstract: | Whey proteins mixed with salal fruits extract (0–20% w/w) were hydrolysed with Pronase E from Streptomyces griseus for a period of 8 h. The angiotensin-converting enzyme (ACE) inhibitory activity of the hydrolysates was highest (IC50: 0.087 mg mL?1) 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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Keywords: | ACE-inhibition peptides protease salal berry whey protein |
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