scholarly journals In Silico Analysis of Bioactive Peptides Released from Giant Grouper (Epinephelus lanceolatus) Roe Proteins Identified by Proteomics Approach

Molecules ◽  
2018 ◽  
Vol 23 (11) ◽  
pp. 2910 ◽  
Author(s):  
Fenny Panjaitan ◽  
Honey Gomez ◽  
Yu-Wei Chang
Keyword(s):  
In Silico ◽  
Bioactive Peptides ◽  
In Silico Analysis ◽  
Epinephelus Coioides ◽  
Accession Number ◽  
Inhibitory Peptides ◽  
Dpp Iv ◽  
Ncbi Accession ◽  
Silico Analysis ◽  
Ncbi Accession Number

Major proteins contained in dried giant grouper roe (GR) such as vitellogenin (from Epinephelus coioides; NCBI accession number: AAW29031.1), apolipoprotein A-1 precursor (from Epinephelus coioides; NCBI accession number: ACI01807.1) and apolipoprotein E (from Epinephelus bruneus; NCBI accession number: AEB31283.1) were characterized through compiled proteomics techniques (SDS-PAGE, in-gel digestion, mass spectrometry and on-line Mascot database analysis). These proteins were subjected to in silico analysis using BLAST and BIOPEP-UWM database. Sequence similarity search by BLAST revealed that the aligned vitellogenin sequences from Epinephelus coioides and Epinephelus lanceolatus share 70% identity, which indicates that the sequence sample has significant similarity with proteins in sequence databases. Moreover, prediction of potential bioactivities through BIOPEP-UWM database resulted in high numbers of peptides predominantly with dipeptidyl peptidase-IV (DPP-IV) and angiotensin-I-converting enzyme (ACE-I) inhibitory activities. Pepsin (pH > 2) was predicted to be the most promising enzyme for the production of bioactive peptides from GR protein, which theoretically released 82 DPP-IV inhibitory peptides and 47 ACE-I inhibitory peptides. Overall, this work highlighted the potentiality of giant grouper roe as raw material for the generation of pharmaceutical products. Furthermore, the application of proteomics and in silico techniques provided rapid identification of proteins and useful prediction of its potential bioactivities.

scholarly journals Predicted Release and Analysis of Novel ACE-I, Renin, and DPP-IV Inhibitory Peptides from Common Oat (Avena sativa) Protein Hydrolysates Using in Silico Analysis

Foods ◽  
2017 ◽  
Vol 6 (12) ◽  
pp. 108 ◽  
Author(s):  
Stephen Bleakley ◽  
Maria Hayes ◽  
Nora O’ Shea ◽  
Eimear Gallagher ◽  
Tomas Lafarga
Keyword(s):  
Avena Sativa ◽  
In Silico ◽  
In Silico Analysis ◽  
Protein Hydrolysates ◽  
Inhibitory Peptides ◽  
Dpp Iv ◽  
Silico Analysis

scholarly journals Prediction of Bioactive Peptides from Chlorella sorokiniana Proteins Using Proteomic Techniques in Combination with Bioinformatics Analyses

2019 ◽  
Vol 20 (7) ◽  
pp. 1786 ◽  
Author(s):  
Lhumen A. Tejano ◽  
Jose P. Peralta ◽  
Encarnacion Emilia S. Yap ◽  
Fenny Crista A. Panjaitan ◽  
Yu-Wei Chang
Keyword(s):  
In Silico ◽  
Bioactive Peptides ◽  
Biological Activities ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
In Silico Analysis ◽  
Chlorella Sorokiniana ◽  
Molecular Characteristics ◽  
Sds Page ◽  
Silico Analysis

Chlorella is one of the most nutritionally important microalgae with high protein content and can be a good source of potential bioactive peptides. In the current study, isolated proteins from Chlorella sorokiniana were subjected to in silico analysis to predict potential peptides with biological activities. Molecular characteristics of proteins were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and proteomics techniques. A total of eight proteins were identified by proteomics techniques from 10 protein bands of the SDS-PAGE. The predictive result by BIOPEP’s profile of bioactive peptides tools suggested that proteins of C. sorokiniana have the highest number of dipeptidyl peptidase-IV (DPP IV) inhibitors, with high occurrence of other bioactive peptides such as angiotensin-I converting enzyme (ACE) inhibitor, glucose uptake stimulant, antioxidant, regulating, anti-amnestic and antithrombotic peptides. In silico analysis of enzymatic hydrolysis revealed that pepsin (pH > 2), bromelain and papain were proteases that can release relatively larger quantity of bioactive peptides. In addition, combinations of different enzymes in hydrolysis were observed to dispense higher numbers of bioactive peptides from proteins compared to using individual proteases. Results suggest the potential of protein isolated from C. sorokiniana could be a source of high value products with pharmaceutical and nutraceutical application potential.

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

2019 ◽  
Vol 20 (20) ◽  
pp. 5191 ◽  
Author(s):  
Honey Lyn R. Gomez ◽  
Jose P. Peralta ◽  
Lhumen A. Tejano ◽  
Yu-Wei Chang
Keyword(s):  
In Silico ◽  
Bioactive Peptides ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
In Silico Analysis ◽  
In Vitro Tests ◽  
Dpp Iv ◽  
Crassostrea Angulata ◽  
Vitro Analysis

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.

Sign in / Sign up

Export Citation Format

Share Document