ATPase activity, surface hydrophobicity, sulfhydryl content and protein degradation in refrigerated seabass muscle in modified atmosphere packaging

Journal of Food Biochemistry

Volumn 28, Issue 1, 2004, Pages 43-60

  Masniyom, Payap ^a   Benjakul, Soottawat ^a   Visessanguan, Wonnop ^b  

^a PRINCE OF SONGKLA UNIVERSITY   (Thailand)

^b NATIONAL SCIENCE AND TECHNOLOGY DEVELOPMENT AGENCY   (Thailand)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; DEGRADATION; ENZYMES; FOOD STORAGE; HYDROPHOBICITY; MICROORGANISMS; MUSCLE; PACKING PLANTS; POLYPEPTIDES; REFRIGERATION; SOLUBILITY;

MICROBIALLY INDUCED ACTIVITY; MODIFIED ATMOSPHERIC PACKAGING (MAP); MUSCLE PROTEINS;

MEATS;

EID: 1842783296     PISSN: 01458884     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1745-4514.2004.tb00054.x     Document Type: Article

References (40)

1. AZUMA, Y. and KONNO, K. 1998. Freeze denaturation of carp myofibrils compared with thermal denaturation. Fish. Sci. 64, 287-290.
2. BENJAKUL, S. and MORRISSEY, M.T. 1997. Protein hydrolysates from Pacific whiting solid wastes. J. Agric. Food Chem. 45, 3423-3431.
3. BENJAKUL, S., SEYMOUR, T.A., MORRISSEY, M.T. and AN, H. 1997. Physicochemical changes in Pacific whiting muscle proteins during iced storage. J. Food Sci. 62, 729-733.
4. BENJAKUL, S., VISESSANGUAN, W., RIEBROY, S., ISHIZAKI, S. and TANAKA, M. 2002. Gel-forming properties of surimi produced from bigeye snapper, Priacanthus tayenus and P. macracanthus, stored in ice. J. Sci. Food Agric. 82, 1442-1451.
5. DANIEL, J.A., KRISHNAMURTHI, R. and RIZUI, S.S.H. 1985. A review of the effects of carbon dioxide on microbial growth and food quality. J. Food Prot. 38, 303-305.
6. EBASHI, S., KODAMA, A. and EBASHI, F. 1968. Troponin I. Preparation and physiological function. J. Biochem. 64, 465-477.
7. ELLMAN, G.L. 1959. Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82, 70-77.
8. FAIRBAIRN, D. and LOW, B.A. 1986. Proteinases of psychrotrophic bacteria: Their origin production, properties, effects and control. J. Dairy Sci. 53, 139-177
9. FISKE, C.H. and SUBBAROW, Y. 1925. The colorimetric determination of phosphorus. J. Biol. Chem. 66, 375-400
10. GOMEZ-GUILLEN, M.C. and BATISTA, I. 1997. Seasonal changes and preliminary characterization of cathepsin D-like activity in sardine (Sordina pilchardus) muscle. Intern. J. Food Sci. Technol. 32, 255-260.
11. HAARD, N.F. 1992. Technical aspects of extending prime quality of seafood: a review. J. Aquat. Food Prod. Technol. 1(3/4), 9-28.
12. HAYAKAWA, S. and NAKAI, S. 1985. Contribution of hydrophobicity, net charge and sulfhydryl groups to thermal properties of ovalbumin. Can. Inst. Food Sci. Technol. J. 18, 290-295.
13. HILL, A.R., IRVINE, D.M. and BULLOCK, D.H. 1982. Precipitation and recovery of whey proteins. A review. Can. Inst. Food Sci. Techol. J. 75, 155-160.
14. JIANG, S.T., WANG, Y.T. and CHEN, C.S. 1991. Purification and some properties of calpain II from tilabia muscle (Tilapia nilotica X Tilapia aurea). J. Agric. Food Chem. 39, 237-241.
15. LAEMMLI, U.K. 1970. Cleavage of structural proteins during the assemble of head of bacteriophage. Nature 227, 680-685.
16. LI-CHAN, E., NAKAI, S. and WOOD, D.F. 1985. Relationship between functional (fat binding, emulsifying) and physicochemical properties of muscle proteins. Effect of heating, freezing, pH and species. J. Food Sci. 50, 1034-1040.
17. LOWRY, O.H., ROSEBROUGH, N.J., FAN, A.L. and RANDALL, R.J. 1951. Protein measurement with Folin phenol reagent. J. Biol. Chem. 193, 256-275.
18. MASNIYOM, P., BENJAKUL, S. and VISESSANGUAN, W. 2002. Shelf-life extension of refrigerated seabass slices under modified atmosphere packaging. J. Sci. Food Agric. 82, 873-880.
19. MORRISSEY, M.T., WU, J.W., LIN, D.D. and AN, H. 1993. Protease inhibitor effect on torsion measurements and autolysis of Pacific whiting of surimi. J. Food Sci. 58, 1050-1054.
20. MULTILANGI, W.A.M., PANYAM, D. and KILARA, A. 1996. Function properties of hydrolysate from proteolysis of heat-denatured whey protein isolate. J. Food Sci. 61, 270-274.
21. OKITANI, A., MATSUKURA, U., KATO, H. and FUJIMAKI, M. 1980. Purification and some properties of a myofibrillar protein-degradating protease, cathepsin L, from rabbit skeletal muscle. J. Biochem. 87, 1133-1143.
22. ORDONEZ, J.A., LOPEZ-GALVEZ, D.E., FERNANDEZ, M., HIERRO, E. and HOZ, L. 2000. Microbial and physicochemical modifications of hake (Merluccius merluccius) steaks stored under carbon dioxide enriched atmosphere. J. Sci. Food Agric. 80, 1831-1840.
23. PASTORIZA, L., SAMPEDRO, G., HERRERA, J.J. and CABO, M.L. 1996. Effect of modified atmosphere packaging on shelf life of iced fresh hake slices. J. Sci. Food Agric. 71, 541-547.
24. PEDROSA-MENABRITO, A. and REGENSTEIN, J.M. 1988. Shelf-life extension of fresh fish: A review. Part 1. Spoilage of fish. J. Food Quality 11, 117-127.
25. QUALI, A. and VALIN, C. 1981. Effect of muscle lysosomal enzymes and calcium activated neutral proteinase on myofibrillar ATPase activity: Relationship with aging changes. Meat Sci. 5, 233-245.
26. REDDY, N.R., ARMSTRONG, D.I., RHODEHAMEL, E.J. and KAUTTER, D.A. 1992. Shelf-life extension and safety concerns about fresh fishery products packed under modified atmospheres. A review of the effects of carbon dioxide on microbial growth and food quality. J. Food Prot. 38, 303-305.
27. ROURA, S.I. and CRUPKIN, M. 1995. Biochemical and functional properties of myofibrils from pre and post-spawned hake (Merluccius hubbsi Marini) stored on ice. J. Food Sci. 60, 269-272.
28. ROURA, S.I., SAAVEDRA, J.P., TRUCCO, R.E. and CRUPKIN, M. 1992. Conformational changes in actomyosin from post-spawned hake stored on ice. J. Food Sci. 57, 1109-1111.
29. SEKI, N., IKEDA, M. and NARITA, N. 1979. Changes in ATPase activities of carp myofibril during ice-storage. Bull. Japan Soc. Sci. Fish. 45, 791-799.
30. SEKI, N. and NARITA, N. 1980. Changes in ATPase activities and other properties of carp myofibrillar protein during ice-storage. Bull. Japan Soc. Sci. Fish. 46, 207-213.
31. SEKINE, T., BARNETT, L.M. and KIELLY, W.W. 1962. The active site of myosin adenosine triphosphatase. J. Bio. Chem. 237, 2769-2772.
32. SOMPONGSE, W., ITOH, Y. and OBATAKE, A. 1996. Role of SHa in the polymerization on myosin heavy chain during ice storage of carp actomyosin. Fish. Sci. 62, 110-113.
33. STEEL, R.G.D. and TORRIE, J.H. 1980. Principle and Procedures of Statistics, 2nd Ed., McGraw-Hill, New York.
34. TOKIWA, T. and MATSUMIYA, J. 1969. Fragmentation of fish myofibril. Effect of storage condition and muscle cathepsin. Bull. Japan Soc. Sci. Fish. 35, 1099-1109.
35. VENUGOPAL, V. 1990. Extracellular proteases of contaminant bacteria in fish spoilage: A review. J. Food Prot. 53, 341-350.
36. VENUGOPAL, V., ALUR, M.D. and LEWIS, N.F. 1983. Extracellular protease from Pseudomonas marinoglutinosa: Some properties and its action of fish actomyosin. J. Food Sci. 48, 671-675.
37. VISESSANGUAN, W., MENINO, A.R., KIM, S.M. and AN, H. 2001. Cathepsin L: A predominant heat-activated proteinase in Arrowtooth Flounder muscle. J. Agric. Food Chem. 49, 2633-2640.
38. WANG, J.H., MA, W.C., SU, J.C., CHEN, C.S. and JIANG, S.T. 1993. Comparison of the properties of m-calpain from tilapia and grass shrimp muscle. J. Agric. Food Chem. 41, 1379-1384.
39. 2+ uptake by sarcoplasmic reticulum. J. Food Sci. 54, 1107-1115.
40. YAMAGUCHI, M. and SEKINE, T. 1966. Sulfhydryl groups involved in the active site of myosin a adenosine triphosphatase. I. Specific blocking of the SH group responsible for the inhibitory phase in "B: phasic response" of the catalytic activity. J. Biochem. 59, 24-33.