The Indian Journal of Nutrition and Dietetics

Open Access Open Access  Restricted Access Subscription Access
Open Access Open Access Open Access  Restricted Access Restricted Access Subscription Access

Selective Extraction of Surface-Active and Antioxidant Hydrolysates from Yellowfin Tuna Red Meat Protein using Papain by Response Surface Methodology


Affiliations
1 ICAR-Central Institute of Fisheries Technology, Kochi - 682 029, India
2 ICAR-Central Institute of Fisheries Technology, Kochi, India
3 Mumbai Research Centre, ICAR-CIFT, Vashi, Navi Mumbai - 400 703, India
     

   Subscribe/Renew Journal


The present study was focused on the selective extraction of surface-active and antioxidant hydrolysates from yellowfin tuna (Thunnus albacares) red meat based on separate hydrolytic conditions using papain. The effect of key processing variables viz., enzyme-substrate ratio (0.25-1.5 %) and hydrolysis time (30-240 min) under optimized temperature and pH, on the protein recovery, surface-active and antioxidative properties, was determined using Response Surface Methodology (RSM) with a central composite design. Single and combined effects of the variables on the responses were studied by formulating 13 experimental runs. The coefficient of determination (R2) ranged between 0.73 – 0.99 indicating the suitability of the fitted regression models. The optimum hydrolytic conditions to get hydrolysates having superior surface-active properties were enzyme-substrate ratio (E/S) of 0.41 % and 30 minutes hydrolysis time with a desirability of 0.611. Similarly, the optimum conditions to exhibit the highest antioxidative properties with a desirability of 0.932 were: 1.28 % E/S and 240 minutes hydrolysis time.

Keywords

Yellowfin Tuna, Fish Protein Hydrolysate, Surface-Active Properties, Antioxidative Properties, Response Surface Methodology.
User
Notifications

  • Herpandi, N.H., Rosma, A. and Wan-Nadiah, W.A. The tuna fishing industry: A new outlook on fish protein hydrolysates. Compr. Rev. Fd. Sci. Fd. Saf., 2011, 10, 195-207.

  • He, S., Franco, C. and Zhang, W. Functions, applications and production of protein hydrolysates from fish processing co-products (FPCP). Fd. Res. Int., 2013, 50, 289-297.

  • Chalamaiah, M., Dinesh, K.B., Hemalatha, R. and Jyothirmayi, T. Fish protein hydrolysates: proximate composition, amino acid composition, antioxidant activities and applications: A review. J. Fd. Chem., 2012, 135, 3020-3038.

  • Awuor, O.L., Kirwa, M.E., Jackim, M.F. and Betty, M. Optimization of alcalase hydrolysis conditions for production of dagaa (Rastrineobola argentea) hydrolysate with anti-oxidative properties. Ind. Chem., 2017, 3, 122. doi: 10.4172/2469-9764.1000122

  • Guerard, F., Sumaya-Martinez, M.T., Laroque, D., Chabeaud, A. and Dufosse, L. Optimization of free radical scavenging activity by response surface methodology in the hydrolysis of shrimp processing discards. Process Biochem., 2007, 42, 1486–1491.

  • Wangtueai, S., Siebenhandl-Ehn, S. and Haltrich, D. Optimization of the preparation of gelatin hydrolysates with anti-oxidative activity from Lizardfish (Saurida spp.) scales gelatin. Chiang Mai J. Sci., 2016, 43, 1122-1133.

  • Jamil, N.H., Halim, N.R.A. and Sarbon, N. M. Optimization of enzymatic hydrolysis condition and functional properties of eel (Monopterus sp.) protein using response surface methodology (RSM). Int. Fd. Res. J., 2016, 23, 1-9.

  • Shankar, T.J., Sokhansanj, S., Bandyopadhyay, S. and Bawa, A.S. A case study on optimization of biomass flow during single-screw extrusion cooking using genetic algorithm (GA) and response surface methodology (RSM). Fd. Bioprocess Technol., 2008, 3, 498-510, doi:10.1007/s11947-008-0172-9.

  • Wu, Y., Cui, S.W., Tang, J. and Gu, X. Optimization of extraction process of crude polysaccharides from boat-fruited sterculia seeds by response surface methodology. Fd. Chem., 2007, 105, 1599–1605.

  • AOAC. Official Methods of Analysis. 19th ed. Association of Official Analytical Chemists, Washington DC, 2012.

  • Taylor, W.H. Formal titration: An evaluation of its various modifications. Analyst, 1957, 82, 488–498.

  • Sathe, S.K. and Salunkhe, D.K. Functional properties of the Great Northern Bean (Phaseolus vulgaris L.) proteins: emulsion, foaming, viscosity and gelation properties. J. Fd. Sci., 1981, 46, 71–74, 81.

  • Pearce, K.N. and Kinsella J.E. Emulsifying properties of proteins: evaluation of a turbidimetric technique. J. Agric. Fd. Chem., 1978, 26, 716–723.

  • Shahidi, F., Han, X.Q. and Synowiecki, J. Production and characteristics of protein hydrolysates from capelin (Mallotus villosus). Fd. Chem., 1995, 53, 285–293.

  • Nilsang, S., Lertsiri, S., Suphantharika, M. and Assavanig, A. Optimization of enzymatic hydrolysis of fish soluble concentrate by commercial proteases. J. Fd. Eng., 2005, 70, 571–578.

  • Shimada, K., Fujikawa, K., Yahara, K. and Nakamura, T. Antioxidative properties of xanthone on the auto oxidation of soybean in cylcodextrin emulsion. J. Agric. Fd. Chem., 1992, 40, 945–948.

  • Benzie, I.F.F. and Strain, J.J. The ferric reducing ability of plasma (FRAP) as a measure of ‘‘antioxidant power’’: the FRAP assay. Anal. Biochem., 1996, 239, 70–76.

  • Oyaiza, M. Studies on products of browning reaction: Antioxidative activity of products of browning reaction prepared from glucosamine. J. Nutr., 1986, 44, 307–315.

  • Re, R., Pellegrini, N., Proteggente, A., Pannala, A., Yang, M. and Rice-Evans, C. Antioxidant activity applying an improved ABTS radical cation decolorization assay. Free Radic. Biol. Med., 1999, 26, 1231–1237.

  • Kristinsson, H.G. and Rasco, B.A. Fish protein hydrolysates: Production, biochemical, and functional properties. Crit. Rev. Fd. Sci. Nutr., 2000, 40, 43–81.

  • Ren, J., Zhao, M., Shi, J., Wang, J., Jiang, Y., Cui, C. and Xue, S.J. Purification and identification of antioxidant peptides from grass carp muscle hydrolysates by consecutive chromatography and electrospray ionization-mass spectrometry. Fd. Chem., 2008, 108, 727-736.

  • Ovissipour, M., Kenari, A.A., Motamedzadegan, A. and Nazari, R.M. Optimization of enzymatic hydrolysis of visceral waste proteins of yellowfin tuna (Thunnus albacares). Fd. Bioprocess Tech., 2012, 5, 696–705.

  • Motamedzadegan, A., Davarniam, B., Asadi, G., Abedian, A. and Ovissipour, M. Optimization of enzymatic hydrolysis of yellowfin tuna Thunnus albacares viscera using Neutrase. Int. Aquat. Res., 2010, 2, 173-181.

  • Guerard, F., Guimas, L. and Binet, A. Production of tuna waste hydrolysates by a commercial neutral protease preparation. J. Mol. Catal. B: Enzym., 2002, 19-20, 489-498.

  • Myers, R.H., Montgomery, R.C. and Anderson-Cook, C.M. Response surface methodology, process and product optimization using design experiments. Wiley, New York, 2009.

  • Vander Ven, C., Gruppen, H., de Bont, D.B. and Voragen, A.G. Correlations between biochemical characteristics and foam-forming and -stabilizing ability of whey and casein hydrolysates. J. Agric. Fd. Chem., 2002, 50, 2938-2946.

  • Chen, W., Li, X., Rahman, Md.R.T., Al-Hajj, N.Q.M., Dey, K.C. and Raqib, S.M. Review: Emulsification properties of soy bean protein. Nus. Biosci., 2014, 6, 196-202.

  • Gbogouri, G.A., Linder, M., Fanni, J. and Parmentier, M. Influence of hydrolysis degree on the functional properties of salmon byproducts hydrolysates. J. Fd. Sci., 2004, 69, C615-C622.

  • Klompong, V., Benjakul, S., Kantachote, D. and Shahidi, F. Antioxidative activity and functional properties of protein hydrolysate of yellow stripe travelly (Selaroides leptolepis) as influenced by the degree of hydrolysis and enzyme type. Fd. Chem., 2007, 102, 1317-1327.

  • Amiza, M.A., Kong, Y.L. and Faazaz, A.L. Effects of degree of hydrolysis on physicochemical properties of cobia (Rachycentron canadum) frame hydrolysate. Int. Food Res. J., 2012, 19, 199-206.

  • Dauksas, E., Slizyte, R., Rustad, T. and Storrø, I. Bitterness in fish protein hydrolysates and methods for removal. J. Aquat. Fd. Prod. Tech., 2004, 13, 101-114.

  • Kim, S.K. and Wijesekara, I. Development and biological activities of marine derived bioactive peptides: A review. J. Funct. Fds., 2010, 2, 1-9.

  • Adler-Nissen, J. Enzymic Hydrolysis of Food Proteins. Elsevier Applied Science Publishers, Barking, UK, 1986.

  • Saha, B.C. and Hayashi, K. Debittering of protein hydrolyzates. Biotechnol. Adv., 2001, 19, 355-370.

  • Klompong, V., Benjakul, S., Yachai, M., Visessanguan, W., Shahidi, F. and Hayes, K.D. Amino acid composition and antioxidative peptides from protein hydrolysates of yellow stripe trevally (Selaroides leptolepis). J. Fd. Sci., 2009, 74, C126-C133.


Abstract Views: 396

PDF Views: 4




  • Selective Extraction of Surface-Active and Antioxidant Hydrolysates from Yellowfin Tuna Red Meat Protein using Papain by Response Surface Methodology

Abstract Views: 396  |  PDF Views: 4

Authors

Parvathy Unnikrishnan
ICAR-Central Institute of Fisheries Technology, Kochi - 682 029, India
Binsi Puthenveetil Kizhakkethil
ICAR-Central Institute of Fisheries Technology, Kochi, India
Jeyakumari Annamalai
Mumbai Research Centre, ICAR-CIFT, Vashi, Navi Mumbai - 400 703, India
Joshy Chalil George
ICAR-Central Institute of Fisheries Technology, Kochi, India
Aliyamveetil Abubacker Zynudheen
ICAR-Central Institute of Fisheries Technology, Kochi, India
George Ninan
ICAR-Central Institute of Fisheries Technology, Kochi, India
Chandragiri Nagarajarao Ravishankar
ICAR-Central Institute of Fisheries Technology, Kochi, India

Abstract


The present study was focused on the selective extraction of surface-active and antioxidant hydrolysates from yellowfin tuna (Thunnus albacares) red meat based on separate hydrolytic conditions using papain. The effect of key processing variables viz., enzyme-substrate ratio (0.25-1.5 %) and hydrolysis time (30-240 min) under optimized temperature and pH, on the protein recovery, surface-active and antioxidative properties, was determined using Response Surface Methodology (RSM) with a central composite design. Single and combined effects of the variables on the responses were studied by formulating 13 experimental runs. The coefficient of determination (R2) ranged between 0.73 – 0.99 indicating the suitability of the fitted regression models. The optimum hydrolytic conditions to get hydrolysates having superior surface-active properties were enzyme-substrate ratio (E/S) of 0.41 % and 30 minutes hydrolysis time with a desirability of 0.611. Similarly, the optimum conditions to exhibit the highest antioxidative properties with a desirability of 0.932 were: 1.28 % E/S and 240 minutes hydrolysis time.

Keywords


Yellowfin Tuna, Fish Protein Hydrolysate, Surface-Active Properties, Antioxidative Properties, Response Surface Methodology.

References





DOI: https://doi.org/10.21048/%2Fijnd.2019.56.1.22125