Production of Interesting Peptide Fractions by Enzymatic Hydrolysis of Tuna Dark Muscle By-Product Using Alcalase

References

• Adler-Nissen, J. 1982. Limited enzymic degradation of proteins: A new approach in the industrial application of hydrolases. J. Chem. Technol. Biotechnol. 32: 138–156.
   Web of Science ®Google Scholar
• AOAC. 2005. Official Methods of Analysis of the Association of Official Analytical Chemists (16th ed.). Washington, DC: Author.
   Google Scholar
• Balti, R., Nedjar-Arroume, N., Bougatef, A., Guillochon, D., and Nasri, M. 2010. Three novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) using digestive proteases. Food Res. Int. 43: 1136–1143.
   Google Scholar
• Benjakul, S., and Morrissey, M. T. 1997. Protein hydrolysates from Pacific whiting solid wastes. J. Agric. Food Chem. 45: 3423–3430.
   Web of Science ®Google Scholar
• Benyounis, K. Y., Olabi, A. G., and Hashmi, M. S. J. 2005. Effect of laser welding parameters on the heat input and weld-bead profile. J. Mater. Process. Technol. 164–165:978–985.
   Web of Science ®Google Scholar
• Bhaskar, N., Benila, T., Radha, C., and Lalitha, R. G. 2008. Optimization of enzymatic hydrolysis of visceral waste proteins of catla (Catla catla) for preparing protein hydrolysate using a commercial protease. Bioresour. Technol. 99: 335–343.
   PubMed Web of Science ®Google Scholar
• Bhaskar, N., and Mahendrakar, N. S. 2008. Protein hydrolysate from visceral waste proteins of catla (Catla catla): Optimization of hydrolysis conditions for a commercial neutral protease. Bioresour. Technol. 99: 4105–4111.
   PubMed Web of Science ®Google Scholar
• Box, G. E. P., and Wilson, K. B. 1951. On the experimental attainment of optimum condition. J. R. Stat. Soc. B. 13: 1–38.
   Google Scholar
• Cao, W., Zhang, C., Hong, P., and Ji, H. 2008. Response surface methodology for autolysis parameters optimization of shrimp head and amino acids released during autolysis. Food Chem.109: 176–183.
   PubMed Web of Science ®Google Scholar
• Diniz, F. M., and Martin, A. M. 1997. Fish protein hydrolysates by enzymatic processing. Agro Food Ind. Hi Tec. 8: 9–13.
   Web of Science ®Google Scholar
• Duarte, J., Vinderola, G., Ritz, B., Perdigón, G., and Matar, C. 2006. Immunomodulating capacity of commercial fish protein hydrolysate for diet supplementation. Immunobiology 211: 341–350.
   PubMed Web of Science ®Google Scholar
• Dufosse, L., De La Broise, D., and Guerard, F. 1997. Fish protein hydrolysates as nitrogen sources for microbial growth and metabolite production. Recent Res. Dev. Microbiol. 1: 365–381.
   Google Scholar
• Espe, M., and Lied, E. 1999. Fish silage prepared from different cooked and uncooked raw materials: Chemical changes during storage at different temperatures. Sci. Food Agric. 79: 327–332.
   Web of Science ®Google Scholar
• Evans, M. 2003. Optimization of Manufacturing Processes: A Response Surface Approach. London, UK: Carlton House Terrace.
   Google Scholar
• FAO. 2006. Year Book of Fishery Statistics. Rome, Italy: Author.
   Google Scholar
• FAO/WHO. 1999. Energy and Protein Requirements: Report of Joint FAO/WHO/UNU Expert Consultation Technical Report (FAO/WHO and United Nations University, Series No. 724). Geneva, Switzerland: Author. Pp. 116–129.
   Google Scholar
• Fujita, H., Yokoyama, K., and Yoshikawa, M. 2000. Classification and antihyprertensive activity of angiotensin-I-converting enzyme inhibitory activity derived from food proteins. J. Food Sci. 65: 564–569.
   Web of Science ®Google Scholar
• Gildberg, A. 2002. Enhancing return from greater utilization. In: Safety and Quality Issues in Fish Processing. Bremner, H. A. (Ed.). Cambridge, UK: Woodhead Publishing & CRC Press. Pp. 425–449.
   Google Scholar
• Giovanni, M. 1983. Response surface methodology and product optimization. Food Technol. 37: 41–45.
   Web of Science ®Google Scholar
• Guérard, F., Dufossé, L., De La Broise, D., and Binet, A. 2001. Enzymatic hydrolysis of proteins from yellowfin tuna (Thunnus albacares) wastes using Alcalase. J. Molecul. Cataly. B: Enzym. 11: 1051–1059.
   Web of Science ®Google Scholar
• Guérard, F., Sumaya-Martinez, M. T., Laroque, D., Chabeaud, A., and Dufossé, L. 2007. Optimization of free radical scavenging activity by response surface methodology in the hydrolysis of shrimp processing discards. Process Biochem. 42: 1486–1491.
   Web of Science ®Google Scholar
• Hoyle, N. T., and Merritt, J. H. 1994. Quality of fish protein hydrolysates from herring (Clupea harengus). J. Food Sci. 59: 76–79.
   Web of Science ®Google Scholar
• Kristinsson, H. G., and Rasco, B. A. 2000a. Fish protein hydrolysates: Production, biochemical, and functional properties. Crit. Rev. Food Sci. Nutr. 40: 43–81.
   PubMed Web of Science ®Google Scholar
• Kristinsson, H. G., and Rasco, B. A. 2000b. Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline proteases. J. Agric. Food Chem. 48: 657–666.
   PubMed Web of Science ®Google Scholar
• Layne, E. 1957. Spectrophotometric and Turbidimetric Methods for Measuring Proteins. New York, NY: Academic Press.
   Google Scholar
• Liaset, B., Lied, E., and Espe, M. 2000. Enzymatic hydrolysis of by-products from the fish-filleting industry; chemical characterisation and nutritional evaluation. J. Sci. Food Agric. 80: 581–589.
   Web of Science ®Google Scholar
• Martin, A. M., Porter, D., and George, C. 1995. Studies on the hydrolysis of fish protein by enzymatic treatment. In: Developments in Food Science. Amsterdam, The Netherlands: Elsevier. Pp. 1395–1404.
   Google Scholar
• Mendis, E., Rajapakse, N., and Kim, S. K. 2005. Antioxidant properties of a radical-scavenging peptide purified from enzymatically prepared fish skin gelatin hydrolysate. J. Agric. Food Chem. 53: 581–587.
   PubMed Web of Science ®Google Scholar
• Montgomery, D. 1991. Design and Analysis of Experiments (3rd ed.). New York, NY: John Wiley and Sons. 649 p.
   Google Scholar
• Morel, G. 2011. Biochemical and nutritional analysis for Group 3: Procédure pour la détermination des acides aminés libres. Deliverable number: D.1.2.3.13.
   Google Scholar
• Nilsang, S., Lertsiri, S., Suphantharika, M., and Assavanig, A. 2005. Optimization of enzymatic hydrolysis of fish soluble concentrate by commercial proteases. J. Food Eng. 70: 571–578.
   Web of Science ®Google Scholar
• NRC. 1993. Nutrient Requirements of Fish. Washington, DC: National Academy of Sciences. 124 p.
   Google Scholar
• Quaglia, G. B., and Orban, E. 1987. Enzymic solubilisation of proteins of sardine (Sardina pilchardus) by commercial proteases. J. Sci. Food Agric. 38: 263–269.
   Web of Science ®Google Scholar
• Rousseau, M., Batista, I., Le, G. Y., and Fouchereau-Péron, M. 2001. Purification of a functional competitive antagonist for calcitonin gene related peptide action from sardine hydrolysate. Electron. J. Biotechnol. 4: 25–32.
   Google Scholar
• Shahidi, F., Han, X.-Q., and Synowiecki, J. 1995. Production and characteristics of protein hydrolysates from capelin (Mallotus villosus). Food Chem. 53: 285–293.
   Web of Science ®Google Scholar
• Sikorski, Z. E., and Naczk, M. 1981. Modification of technological properties of fish protein concentrates. Crit. Rev. Food Sci. Nutr. 14: 201–230.
   Web of Science ®Google Scholar
• Simpson, B. K., Nayeri, G., Yaylayan, V., and Ashie, I. N. A. 1998. Enzymatic hydrolysis of shrimp meat. Food Chem. 61: 131–138.
   Web of Science ®Google Scholar
• Tacon, G. J. 1994. Feed Ingredients for Carnivorous Fish Species: Alternatives to Fish Meal and Other Fishery Resources (FAO Fishery Circular 881). Rome, Italy; FAO. 39 p.
   Google Scholar
• Vidotti, R. M., Viegas, E. M. M., and Carneiro, D. J. 2003. Amino acid composition of processed fish silage using different raw materials. Anim. Feed Sci. Technol. 105: 199–204.
   Google Scholar
• Viera, G. H. F., Martin, A. M., Sampaiao, S. S., Omar, S., and Gonsalves, R. C. F. 1995. Studies on the enzymatic hydrolysis of Brazilian lobster (Panulirus spp.) processing wastes. J. Sci. Food Agric. 69: 61–65.
   Web of Science ®Google Scholar
• Walton, M., Cowey, C., Coloso, R., and Adron, J. 1986. Dietary requirements of rainbow trout for tryptophan, lysine and arginine determined by growth and biochemical measurements. Fish Physiol. Biochem. 2: 161–169.
   Google Scholar
• Xia, S. H., Wang, Z., and Xu, S. Y. 2007. Characteristics of Bellamya purificata snail foot protein and enzymatic hydrolysates. Food Chem. 101: 1188–1196.
   Web of Science ®Google Scholar