IN SILICO APPROACH OF COLLAGEN FROM TUNA FISH BY-PRODUCT AS ANGIOTENSIN-CONVERTING ENZYME INHIBITOR
DOI:
https://doi.org/10.22159/ajpcr.2019.v12i10.34816Keywords:
In silico, Valorization, Tuna, By-product, Angiotensin-converting enzyme inhibitorAbstract
Objective: This study explores the sustainable valorization of by-products from tuna fish based on in silico approach.
Methods: In silico approaches (BIOPEP database, PeptideRanker database, peptide calculator [PepCalc] database, and toxin prediction [ToxinPred] database) were employed to evaluate the potential of collagens from tuna as a potential source of bioactive peptides. Furthermore, primary structure, biological potential, physicochemical, sensory, and toxicity characteristics of the theoretically released angiotensin-converting enzyme (ACE) inhibitor collagen peptides were predicted.
Results: Tuna collagen was selected as a potential precursor of bioactive peptides based on in silico analysis. Most notable among these are ACE inhibitory peptides. First, the potential of tuna collagen for the releasing bioactive peptides was evaluated by determining the frequency of occurrence of fragments with a given activity. Through the BIOPEP database analysis, there are many bioactive peptides in tuna collagen sequences. Then, an in silico proteolysis using selected enzymes (papain and pepsin) to obtained ACE inhibitory peptides was investigated and then analyzed using PeptideRanker and PepCalc. Cytotoxicity analysis using the online toxic prediction tool ToxinPred revealed that all in silico proteolysis-derived ACE inhibitory peptides are non-cytotoxic.
Conclusions: Overall, the present study highlights that the tuna collagens could be a promising precursor of bioactive peptides that have an antihypertensive effect (ACE inhibitory activities) for developing functional food or nutraceutical products.
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Pal GK, Suresh PV. Physico-chemical characteristics and fibril-forming capacity of carp swim bladder collagens and exploration of their potential bioactive peptides by in silico approaches. Int J Biol Macromol 2017;101:304-13.
Fu Y, Young JF, Løkke MM, Lametsch R, Aluko RE, Therkildsen M. Revalorisation of bovine collagen as a potential precursor of angiotensin I-converting enzyme [ACE] inhibitory peptides based on in silico and in vitro protein digestions. J Funct Foods 2016;24:196-206.
Mine Y, Li-Chan E, Jiang B. Bioactive Proteins and Peptides as Functional Foods and Nutraceuticals. Hoboken, New Jersey: John Wiley and Sons; 2010.
Lacroix IM, Li-Chan EC. Evaluation of the potential of dietary proteins as precursors of dipeptidyl peptidase [DPP]-IV inhibitors by an in silico approach. J Funct Foods 2012;4:403-22.
Gu Y, Majumder K, Wu J. QSAR-aided in silico approach in evaluation of food proteins as precursors of ACE inhibitory peptides. Food Res Int 2011;44:2465-74.
Ranjini HS, Pue G, Kamath SU, Setty M, Hadapad B, Kamath A. An in vitro Study of Cinnamomum zeylanicum as natural inhibitor of angiotengsin-converting enzyme [ACE] on sheep [ovis aries] tissues. Asian J Pharm Clin Res 2016;9:9-12.
Mun’im AM, Munadhil MA, Puspitasari N, Yanuar A. Angiotensin converting enzyme inhibitory activity of melinjo [Gnetum gnemon L.] seed extracts and molecular docking of its stilbene constituets. Asian J Pharm Clin Res 2017;10:243-8.
Abdelhedi O, Nasri R, Jridi M, Mora L, Oseguera-Toledo ME, Aristoy MC, et al. In silico analysis and antihypertensive effect of ACE-inhibitory peptides from smooth-hound viscera protein hydrolysate: Enzyme-peptide interaction study using molecular docking simulation. Process Biochem 2017;58:145-59.
Gangopadhyay N, Wynne K, O’Connor P, Gallagher E, Brunton NP, Rai DK, et al. In silico and in vitro analyses of the angiotensin-I converting enzyme inhibitory activity of hydrolysates generated from crude barley (Hordeum vulgare) protein concentrates. Food Chem 2016;203:367-74.
Lee S, Qian Z, Kim S. A novel angiotensin I converting enzyme inhibitory peptide from tuna frame protein hydrolysate and its antihypertensive effect in spontaneously hypertensive rats. Food Chem 2010;118:96-102.
Atef M, Ojagh SM. Health benefits and food applications of bioactive compounds from fish byproducts : A review. J Funct Foods 2017;35:673-81.
Karayannakidis PD, Zotos A. Fish processing by-products as a potential source of gelatin. A review fish processing by-products as a potential source of gelatin : A review. J Aquat Food Prod Technol 2016;25:65-92.
Garg S, Apostolopoulos V, Nurgali K, Mishra VK. Evaluation of in silico approach for prediction of presence of opioid peptides in wheat. J Funct Foods 2018;41:34-40.
Lo WM, Li-Chan EC. Angiotensin I converting enzyme inhibitory peptides from in vitro pepsin-pancreatin digestion of soy protein. J Agric Food Chem 2005;53:3369-76.
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