Structural changes and functional properties of threadfin bream sarcoplasmic proteins subjected to ph-shifting treatments and lyophilization

Journal of Food Science

Volumn 75, Issue 3, 2010, Pages

  Yongsawatdigul, Jirawat ^a   Hemung, Bung Orn ^b  

^a SURANAREE UNIVERSITY OF TECHNOLOGY   (Thailand)

^b KHON KAEN UNIVERSITY   (Thailand)

Author keywords

FT IR; PH shift; Sarcoplasmic proteins; Threadfin bream; Water holding capacity

Indexed keywords

CANOLA OIL; EMULSIFYING AGENT; FISH PROTEIN; MONOUNSATURATED FATTY ACID; WATER; EMULSION; GEL; INDUSTRIAL WASTE;

ADSORPTION; ANIMAL; ARTICLE; CHEMISTRY; COMPARATIVE STUDY; ECONOMICS; EMULSION; FOOD INDUSTRY; FREEZE DRYING; GEL; HYDROPHOBICITY; INDUSTRIAL WASTE; INFRARED SPECTROSCOPY; ISOLATION AND PURIFICATION; METHODOLOGY; PERCIFORMES; PH; PROTEIN SECONDARY STRUCTURE; SARCOPLASMIC RETICULUM; SOLUBILITY; SURFACE PROPERTY; WASTE DISPOSAL; ANALYSIS; CHEMICAL PHENOMENA; PROCEDURES;

ADSORPTION; ANIMALS; EMULSIFYING AGENTS; EMULSIONS; FATTY ACIDS, MONOUNSATURATED; FISH PROTEINS; FOOD-PROCESSING INDUSTRY; FREEZE DRYING; GELS; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; INDUSTRIAL WASTE; PERCIFORMES; PROTEIN STRUCTURE, SECONDARY; REFUSE DISPOSAL; SARCOPLASMIC RETICULUM; SOLUBILITY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; SURFACE PROPERTIES; WATER; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS;

NEMIPTERIDAE; NEMIPTERUS;

EID: 77953895262     PISSN: 00221147     EISSN: 17503841     Source Type: Journal    
DOI: 10.1111/j.1750-3841.2010.01530.x     Document Type: Article

References (40)

1. Technical committee. Method for water hydration capacity of plant protein material. Cereal Foods World 1981, 26:291-3. AACC] American Assn. of Cereal Chemists
2. Ahmedna M, Prinyawiwatkul W, Rao RM. Solubilized wheat protein isolates: functional properties and potential food applications. J Agric Food Chem 1999, 47:1340-5.
3. Alizadeh-Pasdar N, Li-Chan ECY. Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes. J Agric Food Chem 2000, 48:328-443.
4. Bradford M. A rapid sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 1976, 72:248-52.
5. Chakraborty P. Coconut protein isolate by ultrafiltration. Food engineering and process applications 1986, 308-15. LeMeguer MJelen P. In, editors, New York, Elsevier Applied Science Publishers, p
6. Gratacos-Cubarsi M, Lametsch R. Determination of changes in protein conformation caused by pH and temperature. Meat Sci 2008, 80:545-9.
7. Haris PI, Severcan F. FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media. J Mol Catal B 1999, 7:207-21.
8. Hayakawa S, Nakai S. Relationship of hydrophobicity and net charge to the solubility of milk and soy proteins. J Food Sci 1985, 50:486-91.
9. Hultin HO, Kelleher SD. Process for isolating a protein composition from a muscle source and protein composition. 1999, U.S. Patent 6,005,073
10. Jafarpour A, Gorczyca EM. Characteristics of sarcoplasmic proteins and their interaction with surimi and kamaboko gel. J Food Sci 2009, 74:N16-22.
11. Karthikeyan M, Mathew S, Shamasundar BA, Prakash V. Fractionation and properties of sarcoplasmic proteins from oil sardine (Sardinella longiceps): influence on the thermal gelation behavior of washed meat. J Food Sci 2004, 69:FEP79-84.
12. Kim YS, Yongsawatdigul J, Park JW, Thawornchinsombut S. Characteristics of sarcoplasmic proteins and their interaction with myofibrillar proteins. J Food Biochem 2005, 29:517-32.
13. Krasaechol N, Ranguandeekul R, Duangmal K, Owusu-Apenten RK. Structure and functional properties of modified threadfin bream sarcoplasmic proteins. Food Chem 2008, 107:1-10.
14. Kristinsson HG, Hultin HO. Effect of low and high pH treatment on functional properties of cod muscle proteins. J Agric Food Chem 2003a, 51:5103-10.
15. Kristinsson HG, Hultin HO. Change in conformation and subunit assembly of cod myosin at low and high pH and after subsequent refolding. J Agric Food Chem 2003b, 51:7187-96.
16. Ladrat C, Verrez-Bagnis V, Noel J, Fleurence J. In vitro proteolysis of myofibrillar and sarcoplasmic proteins of white muscle of sea bass (Dicentrarchus labrax L.): effects of cathepsins B, D and L. Food Chem 2003, 81:517-25.
17. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-5.
18. Liang Y, Du F, Sanglier S, Zhou BR, Xia Y, Dorsselaer VA, Maechling C, Kilhoffer MC, Haiech J. Unfolding of rabbit muscle creatine kinase induced by acid study using electrospray ionization mass spectroscopy, isothermal titration calorimetry and fluorescence spectroscopy. J Biol Chem 2003, 278:30098-105.
19. Li-Chan E, Nakai S, Wood DF. Relationship between functional (fat binding, emulsifying) and physicochemical properties of muscle proteins. Effects of heating, freezing, pH and species. J Food Sci 1985, 50:1034-40.
20. Lin TM, Park JW. Protein solubility in Pacific whiting affected by proteolysis during storage. J Food Sci 1996, 61:536-9.
21. Line VLS, Remondetto GE, Subirade M. Cold gelation of β-lactoglobulin oil-in-water emulsions. Food Hydrocolloid 2005, 19:269-78.
22. Mahmoud MI, Malone WT, Cordle CT. Enzymatic hydrolysis of casein: effect of degree of hydrolysis on antigenicity and physical properties. J Food Sci 1992, 57:1223-9.
23. Morrisey MT, Lin J, Ismond A. Waste management and by-product utilization. Surimi and surimi seafood 2005, 279-323. Park JW, In, editor, Boca Raton, Fla., CRC Press, p
24. Nakagawa T, Watabe S, Hashimoto K. Identification of three major components in fish sarcoplasmic proteins. Nippon Suisan Gakkai Shi 1988a, 54:999-1004.
25. Nakagawa T, Watabe S, Hashimoto K. Electrophoretic analysis of sarcoplasmic proteins from fish muscle on polyacrylamide gels. Nippon Suisan Gakkai Shi 1988b, 54:993-8.
26. Nakai S, Li-Chan E, Hayakawa S. Contribution of protein hydrophobicity to its functionality. Nahrung 1986, 30:327-36.
27. Nakai S, Li-Chan E, Arteaga GE. Measurement of surface hydrophobicity. Methods of testing protein functionality 1996, 226-59. Hall GM, In, editor, London, Blackie Academic, p
28. Pearce KN, Kinsella JE. Emulsifying properties of proteins: evaluation of a turbimetric technique. J Agric Food Chem 1978, 26:716-22.
29. Piyadhammaviboon P, Yongsawatdigul J. Protein cross-linking ability of sarcoplasmic proteins extracted from threadfin bream. LWT Food Sci Technol 2009, 42:37-43.
30. Romero A, Cordobes F, Puppo MC, Guerrero A, Bengoechea C. Rheology and droplet size distribution of emulsions stabilized by crayfish flour. Food Hydrocolloid 2008, 22:1033-43.
31. Rosa P, Sala G, Vliet TV, van de Velde F. Cold gelation of whey protein emulsions. J Texture Stud 2006, 37:516-37.
32. Saguer E, Fort N, Alvarez PA, Sedmanand J, Ismail AA. Structure-functionality relationships of porcine plasma proteins probed by FT-IR spectroscopy and texture analysis. Food Hydrocolloid 2008, 22:459-67.
33. Sala G, Wijk RA, Velde FVD, Aken GA. Matrix properties affect the sensory perception of emulsion-filled gels. Food Hydrocolloid 2008, 22:353-63.
34. Tamm LK, Tatulian SA. Infrared spectroscopy of proteins and peptides in lipid bilayers. Q Rev Biophys 1997, 30:365-429.
35. Tsutsui T, Li-Chan E, Nakai S. A simple fluorometric method for fat-binding capacity as an index of hydrophobicity of proteins. J Food Sci 1986, 51:1268-72.
36. Vermeer AWP, Norde W. The thermal stability of immunoglobulin: unfolding and aggregation of a multi-domain protein. Biophys J 2000, 78:394-404.
37. Wong PYY, Kitts DD. A comparison of the buttermilk solids functional properties to nonfat dried milk, soy protein isolate, dried egg white, and egg yolk powders. J Dairy Sci 2003, 86:746-54.
38. Yongsawatdigul J, Park JW. Thermal denaturation and aggregation of threadfin bream actomyosin. Food Chem 2003, 83:409-16.
39. Yongsawatdigul J, Piyadhammaviboon P. Gel enhancing effect and protein cross-linking ability of tilapia sarcoplasmic proteins. J Sci Food Agric 2007, 87:2810-6.
40. Zurawski VR, Foster JF. Neutral transition and environment of sulfhydryl side chain of bovine plasma albumin. Biochemistry 1974, 13:3465-71.