DOI QR코드

DOI QR Code

Preparation and characterization of protein isolate from Yellowfin tuna Thunnus albacares roe by isoelectric solubilization/precipitation process

  • Lee, Hyun Ji (Department of Food and Nutrition/Institute of Marine Industry, Gyeongsang National University) ;
  • Lee, Gyoon-Woo (Department of Food and Nutrition/Institute of Marine Industry, Gyeongsang National University) ;
  • Yoon, In Seong (Department of Food and Nutrition/Institute of Marine Industry, Gyeongsang National University) ;
  • Park, Sung Hwan (Department of Food and Nutrition/Institute of Marine Industry, Gyeongsang National University) ;
  • Park, Sun Young (Department of Seafood Science and Technology/Institute of Marine Industry, Gyeongsang National University) ;
  • Kim, Jin-Soo (Department of Seafood Science and Technology/Institute of Marine Industry, Gyeongsang National University) ;
  • Heu, Min Soo (Department of Food and Nutrition/Institute of Marine Industry, Gyeongsang National University)
  • Received : 2016.05.12
  • Accepted : 2016.05.12
  • Published : 2016.05.31

Abstract

Isoelectric solubilization/precipitation (ISP) processing allows selective, pH-induced water solubility of proteins with concurrent separation of lipids and removal of materials not intended for human consumption such as bone, scales, skin, etc. Recovered proteins retain functional properties and nutritional value. Four roe protein isolates (RPIs) from yellowfin tuna roe were prepared under different solubilization and precipitation condition (pH 11/4.5, pH 11/5.5, pH 12/4.5 and pH 12/5.5). RPIs contained 2.3-5.0 % moisture, 79.1-87.8 % protein, 5.6-7. 4 % lipid and 3.0-3.8 % ash. Protein content of RPI-1 and RPI-2 precipitated at pH 4.5 and 5.5 after alkaline solubilization at pH 11, was higher than those of RPI-3 and RPI-4 after alkaline solubilization at pH 12 (P < 0.05). Lipid content (5.6-7.4 %) of RPIs was lower than that of freeze-dried concentrate (10.6 %). And leucine and lysine of RPIs were the most abundant amino acids (8.8-9.4 and 8.5-8.9 g/100 g protein, respectively). S, Na, P, K as minerals were the major elements in RPIs. SDS-PAGE of RPIs showed bands at 100, 45, 25 and 15 K. Moisture and protein contents of process water as a 2'nd byproduct were 98.9-99.0 and 1.3-1.8 %, respectively. Therefore, yellowfin tuna roe isolate could be a promising source of valuable nutrients for human food and animal feeds.

Keywords

References

  1. Agboola S, Ng D, Mills D. Characterization and functional properties of Australia rice protein isolates. J Cereal Sci. 2005;41:283-90. https://doi.org/10.1016/j.jcs.2004.10.007
  2. Al-Holy MA, Rasco BA. Characterisation of salmon (Oncorhynchus keta) and sturgeon (Acipenser transmontanus) caviar proteins. J Food Biochem. 2006;30:422-8. https://doi.org/10.1111/j.1745-4514.2006.00069.x
  3. AOAC (Association of Analytical Chemists). Official Methods of Analysis. 16th ed. Washington DC: Association of Analytical Chemists; 1995. p. 69-74.
  4. Azadian M, Nasab MM, Abedi E. Comparison of functional properties and SDSPAGE patterns between fish protein isolate and surimi produced from silver carp. Eur Food Res Technol. 2012;235:83-90. https://doi.org/10.1007/s00217-012-1721-z
  5. Belitz HD and Grosch W. 2001. Schieberle, P. Lehrbuch der Lebensmittelchemie, ISBN 3-540-41096-1 5. Aufl. Springer-Verlag Berlin, Heidelberg, New York
  6. Chalamaiah M, Narsing Rao G, Govardhana Rao D, Jyothirmayi T. Protein hydrolysates from meriga (Cirrhinus mrigala) egg and evaluation of their functional properties. Food Chem. 2010;120:652-7. https://doi.org/10.1016/j.foodchem.2009.10.057
  7. Chalamaiah M, Balaswamy K, Narsing Rao G, Prabhakara Rao PG, Jyothirmayi T. Chemical composition and functional properties of mrigal (Cirrhinus mrigala) egg protein concentrates and their application in pasta. J Food Technol. 2013;50:514-20. https://doi.org/10.1007/s13197-011-0357-5
  8. Chanarat S, Benjakul S. Impact of microbial transglutaminase on gelling properties of Indian mackerel fish protein isolates. Food Chem. 2013;136:929-37. https://doi.org/10.1016/j.foodchem.2012.09.021
  9. Chen YC, Jaczynski J. Gelation of protein recovered from Antarctic krill (Euphausia superba) by isoelectric solubilization/precipitation as affected by function additives. J Agric Food Chem. 2007a;55:1814-22. https://doi.org/10.1021/jf0629944
  10. Chen YC, Jaczynski J. Protein recovery from rainbow trout (Oncorhynchus mykiss) processing by-products via isoelectric solubilization/precipitation and its gelation properties as affected by functional additives. J Agric Food Chem. 2007b;55:9079-88. https://doi.org/10.1021/jf071992w
  11. Collette BB, Nauen CE. FAO Species Catalogue. Vol. 2 Scombrids of the World: An Annotated and Illustrated Catalogue of Tunas, Mackerels, Bonitos, and Related Species Known to Date. Rome: FAO; 1983. p. 137. Fish. Synop., 125.
  12. Foh MBK, Wenshui X, Amadou I, Jiang Q. Influence of pH shift on functional properties of protein isolated of tilapia (Oreochromis niloticus) muscles and of soy protein isolate. Food Bioprocess Technol. 2012;5:2192-200. https://doi.org/10.1007/s11947-010-0496-0
  13. Gokoglu N, Yerlikaya P. Determination of proximate composition and mineral contents of blue crab (Callinectes sapidus) and swim crab (Portunus pelagicus) caught off the Gulf of Antalya. Food Chem. 2003;80:495-8. https://doi.org/10.1016/S0308-8146(02)00318-7
  14. Gokoglu N, Yerlikaya P, Cengiz E. Effect of cooking methods on the proximate composition and mineral contents of rainbow trout (Oncorhynchus mykiss). Food Chem. 2004;84:19-22. https://doi.org/10.1016/S0308-8146(03)00161-4
  15. Horax R, Hettiarachchy NS, Chen P, Jalaluddin M. Preparation and characterization of protein isolate from cowpea (Vigna unguiculata L. Walp.). J Food Sci. 2004;69:FCT114-8.
  16. Horax R, Hettiarachchy N, Kannan A, Chen P. Protein extraction ptimisation, characterisation, and functionalities of protein isolate from bitter melon (Momordica charantia) seed. Food Chem. 2011;124:545-50. https://doi.org/10.1016/j.foodchem.2010.06.068
  17. Huda N, Abdullah A, Babji AS. Functional properties of surimi powder from three Malaysian marine fish. Int J Food Sci Technol. 2001;36:401-6. https://doi.org/10.1046/j.1365-2621.2001.00473.x
  18. Intarasirisawat R, Benjakul S, Visessanguan W. Chemical compositions of the roes from skipjack, tongol and bonito. Food Chem. 2011;124:1328-34. https://doi.org/10.1016/j.foodchem.2010.07.076
  19. Ji SJ, Lee JS, Shin JH, Park KH, Kim JS, Kim KS, Heu MS. Distribution of protease inhibitors from fish eggs as seafood processing byproducts. Kor J Fish Aquat Sci. 2011;44:8-17.
  20. Ju ZY, Hettiarachchy NS, Rath N. Extraction, denaturation, and hydrophobic properties of rice flour proteins. J Food Sci. 2001;66:229-32. https://doi.org/10.1111/j.1365-2621.2001.tb11322.x
  21. Kim HJ, Kim KH, Song SM, Kim IY, Park SH, Gu EJ, Lee HJ, Kim JS, Heu MS. Fractionation and characterization of protease inhibitors from fish eggs based on protein solubility. Kor J Fish Aquat Sci. 2013a;46:119-28.
  22. Kim JS, Kim KH, Kim HJ, Kim MJ, Park SH, Lee HJ, Heu MS. Chromatographic fractionation of protease inhibitors from fish eggs. Kor J Fish Aquat Sci. 2013b;46:351-8.
  23. Klomklao S, Benjakul S, Kishimura H. Optimum extraction and recovery of trypsin inhibitor from yellowfin tuna (Thunnus albacores) roe and its biochemical properties. Int J Food Sci Technol. 2013;49:168-73.
  24. Kristinsson HG, Ingadottir B. Recovery and properties of muscle proteins extracted from tilapia (Oreochromis niloticus) light muscle by pH shift processing. J Food Sci. 2006;71:132-41.
  25. Kristinsson HG, Rasco BA. Biochemical and functional properties of Atlantic salmon (Salmo salar) muscle proteins hydrolyzed with various alkaline proteases. J Agric Food Chem. 2000;48:657-66. https://doi.org/10.1021/jf990447v
  26. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227:680-5. https://doi.org/10.1038/227680a0
  27. Losso JN, Bogumil R, Nakai S. Comparative studies of phosvitin from chicken and salmon egg yolk. Comp Biochem Physiol B. 1993;106:919-23. https://doi.org/10.1016/0305-0491(93)90051-6
  28. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951;193:265-75.
  29. Martinez-Valverde I, Periago MJ, Santaella M, Ros G. The content and nutritional significance of minerals on fish flesh in the presence and absence of bone. Food Chem. 2000;71:503-9. https://doi.org/10.1016/S0308-8146(00)00197-7
  30. Mireles DeWitt CA, Gomez G, James JM. Protein extraction from beef heart using acid solubilization. J Food Sci. 2002;67:3335-41. https://doi.org/10.1111/j.1365-2621.2002.tb09588.x
  31. Narsing Rao G, Balaswamy K, Satyanarayana A, Prabhakara RP. Physico-chemical, amino acid composition, functional and antioxidant properties of roe protein concentrates obtained from Channa striatus and Lates calcarifer. Food chem. 2012;132:1171-6. https://doi.org/10.1016/j.foodchem.2011.11.055
  32. Nolsoe H, Undeland I. The acid and alkaline solubilization process for the isolation of muscle proteins. Food Bioprocess Technol. 2009;2:1-27. https://doi.org/10.1007/s11947-008-0088-4
  33. Orban E, Di Lena G, Ricelli A, Paoletti F, Casini I, Gambelli L, Caproni R. Quality characteristics of sharpsnout sea bream (Diplodus puntazzo) from different intensive rearing systems. Food Chem. 2000;70:27-32. https://doi.org/10.1016/S0956-7135(99)00112-7
  34. Orban E, Nevigato T, Masci M, Di Lena G, Casini I, Caproni R, Gambelli L, De angelis P, Rampacci M. Nutritional quality and safety of European perch (Perca fluviatilis) from three lakes of central Italy. Food Chem. 2007;100:482-90. https://doi.org/10.1016/j.foodchem.2005.09.069
  35. Paraman I, Hettiarachchy NS, Schaefer C, Beck MI. Hydrophobicity, solubility, and emulsifying properties of enzyme-modified rice endosperm protein. Cereal Chem. 2007;84:343-9. https://doi.org/10.1094/CCHEM-84-4-0343
  36. Pires C, Costa S, Batista AP, Nunes MC, Raymundo A, Batista I. Properties of protein powder prepared from Cape hake by-products. J Food Eng. 2012;108:268-75. https://doi.org/10.1016/j.jfoodeng.2011.08.020
  37. Sathivel S, Bechtel PJ. Properties of soluble protein powders from Alaska pollock (Theragra chalcogramma). Int J Food Sci Technol. 2006;41:520-9. https://doi.org/10.1111/j.1365-2621.2005.01101.x
  38. Sathivel S, Bechtel PJ, Babbitt JK, Prinyawiwatkul W, Negulescu II, Reppond KD. Properties of protein powders from arrowtooth flounder (Atheresthes stomias) and herring (Clupea harengus) byproducts. J Agric Food Chem. 2004;52:5040-6. https://doi.org/10.1021/jf0351422
  39. Sathivel S, Bechtel PJ, Babbitt JK, Prinyawiwatkul W, Patterson M. Functional, nutritional, and rheological properties of protein powders from arrowtooth flounder and their application in mayonnaise. J Food Sci. 2005;70:E57-63. https://doi.org/10.1111/j.1365-2621.2005.tb07091.x
  40. Sathivel S, Bechtel PJ, Prinyawiwatkul W. Physicochemical and rheological properties of salmon protein powders. Int J Food Eng. 2006;2:2.
  41. Sathivel S, Yin H, Bechtel PJ, King JM. Physical and nutritional properties of catfish roe spray dried protein powder and its application in an emulsion system. J Food Eng. 2009;95:76-81. https://doi.org/10.1016/j.jfoodeng.2009.04.011
  42. Shaviklo GR, Thorkelsson G, Arason S, Sveinsdottir K. Characteristics of freezedried fish protein isolated from saithe (Pollachius virens). J Food Sci Technol. 2011;49:309-18.
  43. Tahergorabi R, Beamer SK, Matak KE, Jaczynski J. Isoelectric solubilization/precipitation as a means to recover protein isolate from Striped Bass (Morone saxatilis) and Its physicochemical properties in a nutraceutical seafood product. J Agric Food Chem. 2012;60:5979-87. https://doi.org/10.1021/jf3001197
  44. Tahvonen R, Aro T, Nurmi J, Kallio H. Mineral content in Baltic herring and Baltic herring products. J Food Compos Anal. 2000;13:893-903. https://doi.org/10.1006/jfca.2000.0933
  45. Zudaire I, Murua H, Grande M, Korta M, Arrizabalaga H, Areso JJ, et al. Fecundity regulation strategy of the yellowfin tuna (Thunnus albacares) in the Western Indian Ocean. Fish Res. 2013;138:80-8. https://doi.org/10.1016/j.fishres.2012.07.022

Cited by

  1. 등전점 용해/침전 공정으로 어류 알 분리단백질의 제조과정에서 발생하는 가공처리수에 대한 식품기능성 및 생리활성 vol.50, pp.6, 2016, https://doi.org/10.5657/kfas.2017.0694
  2. 어류 알로부터 알칼리 가용화공정을 통해 회수한 Collagenous Protein 획분의 식품 기능특성 vol.51, pp.4, 2016, https://doi.org/10.5657/kfas.2018.0351
  3. Food functionality of protein isolates extracted from Yellowfin Tuna ( Thunnus albacares ) roe using alkaline solubilization and acid precipitation process vol.7, pp.2, 2016, https://doi.org/10.1002/fsn3.793
  4. Physiochemical Properties and Functional Characteristics of Protein Isolates from the Scallop (Patinopecten yessoensis) Gonad vol.84, pp.5, 2016, https://doi.org/10.1111/1750-3841.14598
  5. Turning Invasive Green Crab (Carcinus maenas) into Opportunity: Recovery of Chitin and Protein Isolate Through Isoelectric Solubilization/Precipitation vol.11, pp.1, 2016, https://doi.org/10.1007/s12649-018-0398-3
  6. Food functionalities and bioactivities of protein isolates recovered from skipjack tuna roe by isoelectric solubilization and precipitation vol.8, pp.4, 2016, https://doi.org/10.1002/fsn3.1470
  7. Nutritional Characteristics of a Peruvian Anchovy (Engraulis ringens) Protein Concentrate vol.29, pp.7, 2016, https://doi.org/10.1080/10498850.2020.1789798
  8. Quality Appraisal of Labeo rohita Roe Protein Concentrate and Characterization of the Roe Protein Concentrate-Based Extruded Munchies vol.29, pp.9, 2020, https://doi.org/10.1080/10498850.2020.1818017
  9. Functional properties of gonad protein isolates from three species of sea urchin: a comparative study vol.85, pp.11, 2016, https://doi.org/10.1111/1750-3841.15464