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In Silico and In Vitro Assessment of Portuguese Oyster () Proteins as Precursor of Bioactive Peptides. | LitMetric

In this study, the potential bioactivities of Portuguese oyster () proteins were predicted through in silico analyses and confirmed by in vitro tests. proteins were characterized by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and identified by proteomics techniques. Hydrolysis simulation by BIOPEP-UWM database revealed that pepsin (pH > 2) can theoretically release greatest amount of bioactive peptides from proteins, predominantly angiotensin I-converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory peptides, followed by stem bromelain and papain. Hydrolysates produced by pepsin, bromelain and papain have shown ACE and DPP-IV inhibitory activities in vitro, with pepsin hydrolysate (PEH) having the strongest activity of 78.18% and 44.34% at 2 mg/mL, respectively. Bioactivity assays of PEH fractions showed that low molecular weight (MW) fractions possessed stronger inhibitory activity than crude hydrolysate. Overall, in vitro analysis results corresponded with in silico predictions. Current findings suggest that in silico analysis is a rapid method to predict bioactive peptides in food proteins and determine suitable enzymes for hydrolysis. Moreover, proteins can be a potential source of peptides with pharmaceutical and nutraceutical application.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6829514PMC
http://dx.doi.org/10.3390/ijms20205191DOI Listing

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