In Silico and In Vitro Assessment of Portuguese Oyster (Crassostrea angulata) Proteins as Precursor of Bioactive Peptides

Abstract

In this study, the potential bioactivities of Portuguese oyster (Crassostrea angulata) proteins were predicted through in silico analyses and confirmed by in vitro tests. C. angulata 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 C. angulata 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, C. angulata proteins can be a potential source of peptides with pharmaceutical and nutraceutical application.

In silico proteolysis and analysis of bioactive peptides from sequences of fatty acid desaturase 3 (FAD3) of flaxseed protein

“…Different enzymes have different potential to release bioactive peptides from proteins, which attribute to their specific cleavage sites ( Gomez et al, 2019 ). In our study, stem bromelain treated FAD3 proteins relatively release higher frequency index of DPP-IV inhibitors as compared to other two protease, while the value of relative release frequency (W) was higher in regulating bioactivity released from ficin protease.…”

“…For in silico prediction of biological activities of any protein sequence and investigation of release of bioactive peptides using specific proteases, BIOPEP database can be used for initial mining of bioactive peptides, that provided large collection of sequences including bioactive peptides, proteins, sensory peptides and allergenic proteins ( Minkiewicz et al, 2008 ). This database has been previously used for identification and analysis of bioactive peptides from number of sources such as products from plants, animals and seafood like porcine myofibrillar proteins ( Keska and Stadnik, 2016 ), bovine meat proteins ( Minkiewicz et al, 2011 ), yak milk casein ( Lin et al, 2018 ), giant grouper roe proteins ( Panjaitan et al, 2018 ), portuguese oyster proteins ( Gomez et al, 2019 ), cereal storage proteins ( Cavazos and Gonzalez de Mejia, 2013 ) and oilseed proteins ( Han et al, 2019 ). Additionally, various online and offline bioinformatics tools such as PeptideRanker, ToxinPred, AllergenFP, AGGRESCAN, Innovagen/PepCalc, SwissADME, etc., have been used previously to study various parameters of peptides.…”

Dipeptide YA is Responsible for the Positive Effect of Oyster Hydrolysates on Alcohol Metabolism in Single Ethanol Binge Rodent Models

“…Another product of oysters is hydrolysate, where bioactive peptides are released from the parent protein by enzymatic hydrolysis [ 42 ]. Thus, OH has higher functional and physiological activity than oyster or its extract [ 16 ]. The antioxidant and anti-inflammatory effects of OH are likely to be exhibited by the YA dipeptide, which is a main component released from oyster by an enzymatic hydrolysis process.…”

“…Recently, oysters have been processed by enzymatic hydrolysis to improve their nutritional properties. Oyster hydrolysate (OH) contains a large amount of free amino acids and low-molecular peptides, and has high physiological activity compared to oyster extract [ 16 ]. OH has antioxidant and anti-inflammatory activity [ 17 , 18 ].…”

Peptides for Health Benefits 2019

“…Cai et al [19] explore the cytoprotective mechanism of antioxidant pentapeptides from a protein hydrolysate of miiuy croaker (Miichthys miiuy) swim bladder against oxidative damage to human umbilical vein endothelial cells. Gomez et al [20] report on the potential bioactivities of Portuguese oyster (Crassostrea angulata) proteins through in silico analyses and in vitro tests. C. angulata proteins were proven to be sources of angiotensin I-converting enzyme and dipeptidyl peptidase IV inhibitory peptides with pharmaceutical and nutraceutical applications.…”