期刊
INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY
卷 54, 期 11, 页码 2975-2982出版社
WILEY
DOI: 10.1111/ijfs.14211
关键词
ACE-inhibition; peptides; protease; salal berry; whey protein
资金
- Scottish Government's Rural and Environment Science and Analytical Services Division (RESAS)
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 alpha-lactalbumin. SDS-PAGE analysis suggests that alpha-lactalbumin is less susceptible to proteolysis when the extract is included in the formula. Data indicate that alpha-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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