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Identification of bioactive peptide from Oreochromis niloticus skin gelatin

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Abstract

Fish skin, one type of wastes generated from Nile tilapia processing, is still a good source of collagen and gelatin. Bioactive peptides can be obtained from Nile tilapia skin gelatin by trypsin digestion. Trypsin hydrolysate was subsequently purified by gel filtration chromatography. Trypsin A fraction showed the greatest reducing power (5.138 ± 1.060 μM trolox/mg peptide) among all hydrolysate fractions, while trypsin B fraction from gel filtration column was found to exhibit the best radical scavenging and angiotensin-I-converting enzyme (ACE) inhibitory activities 8.16 ± 2.18 μg trolox/mg peptide and 59.32 ± 9.97 % inhibition, respectively. The most active fraction was subjected to MALDI-TOF/TOF MS/MS. After annotation by Mascot sequence matching software (Matrix Science) with Ludwig NR Database, two peptide sequences were identified; GPEGPAGAR (MW 810.87 Da) and GETGPAGPAGAAGPAGPR (MW 1490.61 Da). The docking analysis suggested that the shape of the shorter peptide may be slightly more proper, to fit into the binding cleft of the ACE. However, the binding affinities calculated from the docking showed no significant difference between the two peptides. In good agreement with the in silico data, results from the in vitro ACE inhibitory activity with synthetic peptides also showed no significant difference. Both peptides are thus interesting novel candidates suitable for further development as ACE inhibitory and antioxidant agents from the natural source.

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References

  • Alemán A, Giménez B, Montero P, Gόmez-Guillén MC (2011a) Antioxidant activity of several marine skin gelatins. LWT Food Sci Technol 44:407–413

    Article  Google Scholar 

  • Alemán A, Pérez-Santín E, Bordenave-Juchereau S, Arnaudin I, Gómez-Guillén MC, Montero P (2011b) Squid gelatin hydrolysates with antihypertensive, anticancer and antioxidant activity. Food Res Int 44:1044–1051

    Article  Google Scholar 

  • Arts MJTJ, Haenen GRMM, Voss HP, Bast A (2004) Antioxidant capacity of reaction products limits the applicability of the trolox equivalent antioxidant capacity (TEAC) assay. Food Chem Toxicol 42:45–49

    Article  CAS  Google Scholar 

  • Chalé FGH, Ruiz JCR, Fernández JJA, Ancona DAB, Campos MRS (2014) ACE inhibitory, hypotensive and antioxidant peptide fractions from mucuna pruriens proteins. Process Biochem 49:1691–1698

    Article  Google Scholar 

  • Cheung IWY, Cheung LKY, Tan NY, Li-Chan ECY (2012) The role of molecular size in antioxidant activity of peptide fractions from Pacific hake (merluccius productus) hydrolysates. Food Chem 134:1297–1306

    Article  CAS  Google Scholar 

  • Chi CF, Wang B, Wang YM, Zhang B, Deng SG (2015) Isolation and characterization of three antioxidant peptides from protein hydrolysate of Bluefin leatherjacket (navodon septentrionalis) heads. J Funct Foods 12:1–10

    Article  Google Scholar 

  • Choonpicharn S, Jaturasitha S, Rakariyatham N, Suree N, Niamsup H (2015) Antioxidant and antihypertensive activity of gelatin hydrolysate from Nile tilapia skin. J Food Sci Technol 52:3134–3139

    Article  Google Scholar 

  • De Gobba C, Tompa G, Otte J (2014) Bioactive peptides from caseins released by cold active proteolytic enzymes from arsukibacterium ikkense. Food Chem 165:205–215

    Article  Google Scholar 

  • Dekkers E, Raghavan S, Kristinsson HG, Marshall MR (2011) Oxidative stability of Mahi mahi red muscle dipped in tilapia protein hydrolysates. Food Chem 124:640–645

    Article  CAS  Google Scholar 

  • Espejo-Carpio FJ, De Gobba C, Guadix A, Guadix EM, Otte J (2013) Angiotensin I-converting enzyme inhibitory activity of enzymatic hydrolysates of goat milk protein fractions. Int Dairy J 32:175–183

    Article  CAS  Google Scholar 

  • Fernández-Musoles R, Salom JB, Martínez-Maqueda D, Lόpez-Díez JJ, Recio I, Manzanares P (2013) Antihypertensive effects of lactoferrin hydrolyzates: inhibition of angiotensin and endothelin-converting enzyme. Food Chem 139:994–1000

    Article  Google Scholar 

  • Fitzsimmons KM (2004) Development of new products and markets for the global tilapia trade. Proceedings of ISTA 6. Manila, Philippine, pp 624–633

  • Griffin SP, Bhagooli R (2004) Measuring antioxidant potential in corals using the FRAP assay. J Exp Mar Biol Ecol 302:201–211

    Article  CAS  Google Scholar 

  • Gόmez-Guillén MC, Giménez B, López-Caballero ME, Montero MP (2011) Functional and bioactive properties of collagen and gelatin from alternative sources: a review. Food Hydrocoll 25:1813–1827

    Article  Google Scholar 

  • Himaya SWA, Ngo DH, Ryu B, Kim SK (2012) An active peptide purified from gastrointestinal enzyme hydrolysate of Pacific cod skin gelatin attenuates angiotensin-1 converting enzyme (ACE) activity and cellular oxidative stress. Food Chem 132:1872–1882

    Article  CAS  Google Scholar 

  • Hsu K (2010) Purification of antioxidative peptides prepared from enzymatic hydrolysates of tuna dark muscle by-product. Food Chem 122:42–48

    Article  CAS  Google Scholar 

  • Jiang Z, Tian B, Brodkorb A, Huo G (2010) Production, analysis and in vivo evaluation of novel angiotensin-I-converting enzyme inhibitory peptides from bovine casein. Food Chem 123:779–786

    Article  CAS  Google Scholar 

  • Ko SC, Kang N, Kim EA, Kang MC, Lee SH, Kang SM, Lee JB, Jeon BT, Kim SK, Park SJ, Park PJ, Jung WK, Kim D, Jeon YJ (2012) A novel angiotensin I-converting enzyme (ACE) inhibitory peptide from a marine chlorella ellipsoidea and its antihypertensive effects in spontaneously hypertensive rats. Process Biochem 47:2005–2011

    Article  CAS  Google Scholar 

  • Kramer GJ, Mohd A, Schwager SL, Masuyer G, Acharya KR, Sturrock ED, Bachmann BO (2014) Interkingdom pharmacology of angiotensin-I converting enzyme inhibitor phosphonates produced by actinomycetes. ACS Med Chem Lett 5:346–351

    Article  CAS  Google Scholar 

  • Li Z, Wang B, Chi C, Gong Y, Luo H, Ding G (2013) Influence of average molecular weight on antioxidant and functional properties of cartilage collagen hydrolysates from Sphyrna lewini, dasyatis akeji and raja porosa. Food Res Int 51:283–293

    Article  CAS  Google Scholar 

  • Mao XY, Ni JR, Sun WL, Hao PP, Fan L (2007) Value-added utilization of yak milk casein for the production of angiotensin-I-converting enzyme inhibitory peptides. Food Chem 103:1282–1287

    Article  CAS  Google Scholar 

  • Memarpoor-Yazdi M, Mahaki H, Zare-Zardini H (2013) Antioxidant activity of protein hydrolysates and purified peptides from zizyphus jujube fruits. J Funct Foods 5:62–70

    Article  CAS  Google Scholar 

  • Mendis E, Rajapakse N, Kim SK (2005) Antioxidant properties of a radical-scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate. J Agric Food Chem 53:581–587

    Article  CAS  Google Scholar 

  • Park PJ, Je JY, Kim SK (2003) Angiotensin I converting enzyme (ACE) inhibitory activity of hetero-chitooligosaccharides prepared from partially different deacetylated chitosans. J Agric Food Chem 51:4930–4934

    Article  CAS  Google Scholar 

  • Prathapan A, Singh MK, Anusree SS, Kumar DRS, Sundaresan A, Raghu KG (2011) Antiperoxidative, free radical scavenging and metal chelating activities of boerhaavia diffusa L. J Food Biochem 35:1548–1554

    Article  CAS  Google Scholar 

  • Prathapan A, Vineetha VP, Abhilash PA, Raghu KG (2013) Boerhaavia diffusa L. attenuates angiotensin II-induced hypertrophy in H9c2 cardiac myoblast cells via modulating oxidative stress and down-regulating NF-κβ and transforming growth factor β1. Br J Nutr 110:1201–1210

    Article  CAS  Google Scholar 

  • Raghavan S, Kristinsson HG (2009) ACE-inhibitory activity of tilapia protein hydrolysates. Food Chem 117:582–588

    Article  CAS  Google Scholar 

  • Saidi S, Deratani A, Belleville MP, Amar RB (2014) Antioxidant properties of peptide fractions from tuna dark muscle protein by-product hydrolysate produced by membrane fractionation process. Food Res Int 65:329–336

    Article  CAS  Google Scholar 

  • Sharp SI, Aarsland D, Day S, Sonnesyn H, Ballard C, Syst A (2011) Hypertension is a potential risk factor for vascular dementia: systematic review. Int J Geriatr Psychiatry 26:661–669

    Article  Google Scholar 

  • Sudhakar S, Nazeer RA (2015) Preparation of potent antioxidant peptide from edible part of shortclub cuttlefish against radical mediated lipid and DNA damage. LWT Food Sci Technol 64:593–601

    Article  CAS  Google Scholar 

  • Trott O, Olson AJ (2010) AutoDock vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem 31:455–461

    CAS  Google Scholar 

  • Vandanjon L, Grignon M, Courois E, Bourseau P, Jaouen P (2009) Fractionating white fish fillet hydrolysates by ultrafiltration and nanofiltration. J Food Eng 95:36–44

    Article  CAS  Google Scholar 

  • Vercruysse L, Van CJ, Smagghie G (2005) ACE inhibitory peptides derived from enzymatic hydrolysates of animal muscle protein, a review. J Agric Food Chem 53:8106–8115

    Article  CAS  Google Scholar 

  • Wallace AC, Laskowski RA, Thornton JM (1995) LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng 8:127–134

    Article  CAS  Google Scholar 

  • Zhang YX, Zou AH, Manchu RG, Zhou YC, Wang SF (2008) Purification and antimicrobial activity of antimicrobial protein from brown-spotted grouper, epinephelusfario. J Zool Syst Evol Res 29:627–632

    CAS  Google Scholar 

  • Zhang Y, Duan X, Zhuang Y (2012) Purification and characterization of novel antioxidant peptides from enzymatic hydrolysates of tilapia (Oreochromis niloticus) skin gelatin. Peptides 38:13–21

    Article  Google Scholar 

Download references

Acknowledgments

The authors thank the National Research Council of Thailand, the Graduate School of Chiang Mai University, and the Faculty of Science Publication Boosting Grant for the financial support.

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Authors and Affiliations

  1. Department of Chemistry, Faculty of Science, Chiang Mai University, Chiang Mai, 50200, Thailand

    Sadabpong Choonpicharn, Suriya Tateing, Nuttee Suree & Hataichanoke Niamsup

  2. Department of Animal and Aquatic Sciences, Faculty of Agriculture, Chiang Mai University, Chiang Mai, 50200, Thailand

    Sanchai Jaturasitha

  3. Faculty of Public Health, Nation University, Lampang, 52000, Thailand

    Nuansri Rakariyatham

Authors
  1. Sadabpong Choonpicharn
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  2. Suriya Tateing
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  3. Sanchai Jaturasitha
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  4. Nuansri Rakariyatham
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  5. Nuttee Suree
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  6. Hataichanoke Niamsup
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Corresponding author

Correspondence to Hataichanoke Niamsup.

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Research highlights

• The research makes use of the fish skin waste with biotechnological knowledge.

• Peptides from Trypsin-digested gelatin are purified and sequenced.

• In silico ACE binding ability of the peptides was in agreement with in vitro ACE inhibitory assay.

• Two peptides were potential candidates for natural antihypertensive and antioxidant agents.

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Choonpicharn, S., Tateing, S., Jaturasitha, S. et al. Identification of bioactive peptide from Oreochromis niloticus skin gelatin. J Food Sci Technol 53, 1222–1229 (2016). https://doi.org/10.1007/s13197-015-2091-x

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  • DOI: https://doi.org/10.1007/s13197-015-2091-x

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