pH-Solubilzation Process as an Alternative to Enzymatic Hydrolysis Applied to Shrimp Waste

Yıl 2013, Cilt: 13 Sayı: 4, - , 01.08.2013

Julio H. Cã³rdova-murueta Fernando L. Garcã­a-carreã±o María de los Ángeles Navarretedel- Toro

https://doi.org/10.4194/1303-2712-v13_4_09

Öz

Waste materials derived from shrimp processing signify 40 to 45% of the weight of the catch or harvest. For Biotechnology, waste materials are secondary material, as contrast of raw materials, to generate value-added products, such as chitin, protein, and pigments. We used the pH-shift and enzymatic autohydrolysis processes to obtain protein concentrates from the cephalothorax of whiteleg shrimp (Penaeus vannamei). Protein recovery by auto-hydrolysis and pH-shift was 83.3 % (sum of two fractions) and 87.5 respectively. Functional properties from protein concentrates were assayed. The protein concentrates obtained were: precipitated protein at pH=4.0 (PP4), remaining soluble protein at pH=4.0 (SP4), and hydrolyzed protein (3HP). Precipitated protein (PP4) had 50 % foam stability; soluble protein (SP4) 31.5 %, and hydrolyzed protein had no foam stability. Emulsion capacity of the protein concentrates was not different from egg albumin (control protein). Hydrolyzed protein had higher emulsion stability than the other protein concentrates. Protein concentrates from the pH-shift process had good balance of amino acids. Histidine and valine was not detected in hydrolyzed protein. The pH-shift process demonstrated to be an alternative for protein hydrolysis to recover protein from shrimp cephalothorax.

Anahtar Kelimeler

Shrimp head waste, protein, pH-shift, hydrolysis

Kaynakça

• AOAC, 1995. Official methods of analysis of AOAC International. AOAC International, Arlington, VA, USA.
• Armenta-López, R. and Guerrero, L.I., Huerta, S. 2002. Astaxanthin extraction from shrimp waste by lactic fermentation and enzymatic hydrolysis of the carotenoprotein complexsis. J. Food Sci., 67: 1002100 doi: 10.1111/j.1365-2621.2002.tb09443.x
• CONAPESCA, 2004. Statistical Year book of fisheries and aquaculture 2004 (In Spanish). CONAPESCA, Mazatlán, Sinaloa México.
• Córdova-Murueta, J.H., Garcia-Carreño, F.L. and Navarrete-del-Toro, M.A. 2003. Digestive enzymes present in crustacean feces as a tool for biochemical, physiological, and ecological studies. J. Exp. Mar. Biol. Ecol., 297: 43-56. doi: 10.1016/S00220981(03)00355-1
• Dauksas, E., Slizyte, R., Rustad, T. and Storro, I. 2004. Bitterness in Fish Protein Hydrolysates and Methods for Removal. Journal of Aquatic Food Product Technology, 13: 101-114. doi: 1300/J030v13n02_09
• Duarte-De-Holanda, H. and Netto, F.M. 2006. Recovery of components from shrimp (Xiphopenaeus kroyeri) processing waste by enzymatic hydrolysis. J. Food Sci., 71: C298-C303. doi: 1111/j.1750382006.00040.x
• Fox, C.J., Blow, P., Brown, J.H. and Watson, I. 1994. The effect of various processing methods on the physical and biochemical properties of shrimp head meals and their utilization by juvenile Penaeus monodon Fab. Aquaculture, 122: 209-226. doi: 10.1016/00448486(94)90511-8
• García-Carreño, F.L., Dimes, N. and Haard, N. 1993. Substrate-gel electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinase inhibitors. Anal. Biochem., 214: 65-69. doi: 1006/abio.1993.1457
• Heu, M.S., Kim, J.S., Shahidi, F., Jeong, Y. and Jeon, Y.J. 200 Extraction, fractionation and activity characteristics of proteases from shrimp processing discards. J. Food Biochem., 27: 221-2 doi: 1111/j.1745-4514.2003.tb00278.x
• Hill, S.E. 1996. Emulsions. In: G.M. Hall (Ed.), Methods of testing protein functionality. Blackie Academic and Professional, London, U. K.: 153-185.
• Hultin, H.O., Kristinsson, H.G., Lanier, T.C., Park, J.W. 200 Process for recovery of functional proteins by pH shifts. In: J.W. Park (Ed.), Surimi and Surimi Seafood. Taylor and Francis, Boca Raton: 108-133. Ibrahim, H.M., Salama, M.F. and El-Banna, H.A. 1999. Shrimp's waste: Chemical composition, nutritional value and utilization. Food/Nahrung, 43: 418-423. doi: 1002/(SICI)1521-3803(19991201)43:6<418:: AID-FOOD418>3.0.CO;2-6
• Kim, Y.S., Park, J.W. and Choi, Y.J. 2003. New approaches for the effective recovery of fish proteins and their physicochemical characteristics. Fish. Sci., 69: 123112 doi: 10.1111/j.0919-9268.2003.00750.x
• Kristinsson, H. 2001. Conformational and functional changes of hemoglobin and myosin induced by ph: functional role in fish quality. UMass, Amherst, Massachusetts, USA.
• Kristinsson, H.G. and Rasco, B.A. 2000. Fish protein hydrolysates: production, biochemical, and functional properties. Crit. Rev. Food Sci. Nutr., 40: 43-81. doi: 1080/10408690091189266
• Kristinsson, H.G. and Liang, Y. 2006. Effect of pH-shift processing and surimi processing on atlantic croaker (Micropogonias undulates) muscle proteins. J. Food Sci., 71: C304-C312. doi: 1111/j.1750-3841.2006.00046.x
• Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227: 680-685. doi:10.1038/227680a0
• Li-Chang, E. 1996. Separation and purification. In: S., Nakai, H.W., Modler (Eds.), Food proteins: properties and characterization. VCH, New York, N.Y.:429-503.
• Limam, Z., Sadok, S. and Abed, A.E., 2008. Enzymatic Hydrolysis of Shrimp Head Waste: Functional and Biochemical Properties. Food Biotechnol., 22: 352 3 doi: 10.1080/08905430802458461
• Matringe, E., Phan Tan Luu, R. and Lorient, D. 1999. Functional Properties of Milk-Egg Mixtures. J. Food Sci., 64: 787-7 doi: 1111/j.1365261999.tb15912.x
• Mizani, M., Aminlari, M. and Khodabandeh, M. 2005. An Effective Method for Producing a Nutritive Protein Extract Powder from Shrimp-head Waste. Food Sci. Technol. Int., 11: 49-54. doi: 1177/1082013205051271
• Palafox, H., Córdova-Murueta, J.H., Navarrete-del-Toro, M.A. and García-Carreño, F.L. 2009. Protein isolates from jumbo squid (Dosidicus gigas) by pH-shift processing. Process Biochem., 44: 584-587. doi: 1016/j.procbio.2009.02.011
• Sikorski, Z.E., 2002. Proteins. In: Z.E. Sikorski (Ed.), Chemical and Functional Properties of Food Components. CRC Press LLC, Boca Raton:133-167. STATGRAPHICS ® , 2000. Statgraphics Plus 5.1. StatPoint Technologies, Inc. (www.statgraphics.com).
• Torten, J. and Whitaker, J.R. 1964. Evaluation of the Biuret and dye-binding methods for protein determination in Meats. J. Food Sci., 29: 168-174. doi: 1111/j.1365-2621.1964.tb01713.x
• Trevino, S.R., Scholtz, J.M. and Pace, C.N. 2007. Amino Acid Contribution to Protein Solubility: Asp, Glu, and Ser Contribute more Favorably than the other Hydrophilic Amino Acids in RNase Sa. J. Mol. Biol., 366: 449-460. doi.org/10.1016/j.jmb.2006.10.026
• Vázquez-Ortiz, F.A., Caire, G., Higuera-Ciapara, I. and Hernández, G. 1995. High Performance Liquid Chromatographic Determination of Free Amino Acids in Shrimp. J. Liq. Chromatogr. Relat. Technol., 18: 2059 - 2068. doi: 10.1080/10826079508013960
• Wenhong, C., Chaohua, Z., Pengzhi, H. and Hongwu, J. 200 Response surface methodology for autolysis parameters optimization of shrimp head and amino acids released during autolysis. Food Chem., 109: 176-1 doi: 10.1016/j.foodchem.2007.11.080, Wenhong, C., Chaohua, Z., Pengzhi, H., Hongwu, J., Jiming, H. and Jing, Z., 2009. Autolysis of shrimp head by gradual temperature and nutritional quality of the resulting hydrolysate. LWT-Food Sci. Technol., 42: 244-249. doi: 10.1016/j.lwt.2008.05.026
• Wilde, P.J. and Clark, D.C. 1996. Foam formation and stability. In: G.M. Hall (Ed.), Methods of testing protein functionality. Blackie Academic and Professional, London, U.K.: 110-152.