Peptides in rainbow trout (Oncorhynchus mykiss) muscle subjected to ice storage and cooking

Food Chemistry

Volumn 100, Issue 4, 2007, Pages 1566-1572

  Bauchart, Caroline ^a,b   Chambon, Christophe ^a   Mirand, Philippe Patureau ^b   Savary Auzeloux, Isabelle ^c   Rémond, Didier ^b   Morzel, Martine ^a  

^a UR370 QuaPA   (France)

^b CEMAGREF   (France)

^c UMR1213 HERBIVORES   (France)

Author keywords

Cooking; Muscle; Peptides; Post mortem; Proteolysis; Trout

Indexed keywords

AMINO ACID; ANSERINE; GLUTATHIONE; PEPTIDE;

AMINO ACID ANALYSIS; ANIMAL TISSUE; ARTICLE; CADAVER; CONTROLLED STUDY; COOKING; CRYOPRESERVATION; FISH; FOOD FREEZING; FOOD STORAGE; MASS SPECTROMETRY; MOLECULAR WEIGHT; MUSCLE; NONHUMAN; PEPTIDE ANALYSIS; PROTEIN STABILITY; QUANTITATIVE ANALYSIS; RAINBOW TROUT; REPRODUCIBILITY;

ONCORHYNCHUS MYKISS; SALMONIDAE;

EID: 33746522377     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2005.12.023     Document Type: Article

References (32)

1. Abe H. Distribution of free l-histidine and related dipeptides in the muscle of fresh-water fish. Comparative Biochemistry and Physiology 76B (1983) 35-39
2. Abe H., Bobson G.P., Hoeger U., and Parkhouse W.S. Role of histidine-related compounds to intracellular buffering in fish skeletal muscle. American Journal of Physiology 249 (1985) R449-R454
3. Aristoy M.-C., Soler C., and Toldrá F. A simple fast and reliable methodology for the analysis of histidine dipeptides markers of the presence of animal origin proteins in feeds for ruminants. Food Chemistry 84 (2004) 485-491
4. Astier C., Labbe J.P., Roustan C., and Benyamin Y. Sarcomeric disorganization in post-mortem fish muscles. Comparative Biochemistry and Physiology B 100 (1991) 459-465
5. Botta J.R. Freshness quality of seafoods: A review. In: Shahidi F., and Botta J.R. (Eds). Seafoods: Chemistry, processing technology and quality (1994), Blackie Academic and Professional, London 140-167
6. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72 (1976) 248-254
7. Bremner H.A. Fish flesh structure and the role of collagen - its postmortem aspects and implications for fish processing. In: Huss H.H., Jacobsen M., and Liston J. (Eds). Quality assurance in the fish industry (1992), Elsevier, Amsterdam 39-62
8. Claeys E., De Smet S., Balcaen A., Raes K., and Demeyer D. Quantification of fresh meat peptides by SDS-PAGE hi relation to ageing time and taste intensity. Meat Science 67 (2004) 281-288
9. Geist G.M., and Crawford D.L. Muscle cathepsins in three species of Pacific sole. Journal of Food Science 39 (1974) 548-551
10. Gokoglu N., Yerlikaya P., and Cengiz E. Effects of cooking methods on the proximate composition and mineral contents of rainbow trout (Oncorhynchus mykiss). Food Chemistry 84 (2004) 19-22
11. Kaushik S., and Luquet P. Influence of dietary amino acids patterns on the free amino acids contents of blood and muscle of rainbow trout (Salmo Gairderii R.). Comparative Biochemistry and Physiology 64B (1979) 175-180
12. Kitts D., and Weiler K. Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation and recovery. Current Pharmaceutical Design 9 (2003) 1309-1323
13. Kjærsgård I., and Jessen F. Proteome analysis post-mortem changes in cod (Gadus morhua) muscle proteins. Journal of Agricultural and Food Chemistry 51 (2003) 3985-3991
14. Kohama Y., Matsumoto S., Oka H., Teramoto T., Okabe M., and Mimura T. Isolation of angiotensin-converting enzyme inhibitor from tuna muscle. Biochemical and Biophysical Research Communications 155 (1988) 332-337
15. Korhonen H., and Pihlanto A. Food-derived bioactive peptides - opportunities for designing future foods. Current Pharmaceutical Design 9 (2003) 1297-1308
16. Ladrat C., Verrez-Bagnis V., and 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 Chemistry 81 (2003) 517-525
17. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
18. Masniyom P., Benjakul S., and Vissanguan W. ATPase activity, surface hydrophobicity, sulfhydryl content and protein degradation in refrigerated seabass muscle in modified atmosphere packaging. Journal of Food Chemistry 28 (2004) 43-60
19. Maynard L.M., Boissonneault G.A., Chow C.K., and Bruckner G.G. High levels of dietary carnosine are associated with increased concentrations of carnosine and histidine in rat soleus muscle. Journal of Nutrition 131 2 (2001) 287-290
20. Papa I., Alvarez C., Verrez-Bagnis V., Fleurence J., and Benyamin Y. Post mortem release of fish white muscle alpha-actinin as a marker of disorganisation. Journal of the Science of Food and Agriculture 72 (1996) 63-70
21. Passi S., Ricci R., Cataudella S., Ferrante I., DeSimone F., and Rastrelli L. Fatty acid pattern, oxidation product development, and antioxidant loss in muscle tissue of rainbow trout and Dicentrarchus labrax during growth. Journal of Agricultural and Food Chemistry 52 (2004) 2587-2592
22. Robinson M., Rounds J., Hong R., Jacobs D., and Wilmore D. Glutathione deficiency increases organ dysfunction after hemorrhagic shock. Surgery 112 (1992) 140-147
23. Ruiz-Capillas C., and Moral A. Changes in free amino acids during chilled storage of hake (Merluccius merluccius L.) in controlled atmospheres and their use as a quality control index. European Food Research Technology 212 (2001) 302-307
24. Ruiz-Capillas C., and Moral A. Free amino acids and biogenic amines in red and white muscle of tuna stored in controlled atmospheres. Amino Acids 26 2 (2003) 125-132
25. Sato K., Ando M., Kubota S., Origasa K., Kawase H., Toyohara H., et al. Involvement of type V collagen in softening of fish muscle during short-term chilled storage. Journal of Agricultural and Food Chemistry 45 (1997) 343-348
26. Sikorski Z.E., Kolakowska A., and Burt J.R. In: Sikorski Z.E. (Ed). Postharvest biochemical and microbial changes (1990), Bocakaton, CRC Press Inc., Florida 55-75
27. Sylvestre M.N., Feidt C., and Brun-Bellut J. Post-mortem evolution of non-protein nitrogen and its peptide composition in growing lamb muscles. Meat Science 58 (2001) 363-369
28. Tsuchiya H., Kita S., and Seki N. Postmortem changes in α-actinin and connectin in carp and rainbow trout muscles. Nippon Suisan Gakkaishi 58 (1992) 793-798
29. Venugopal V., and Shahidi F. Structure and composition of fish muscle. Food Review International 12 (1996) 175-197
30. Verrez-Bagnis V., Ladrat C., Morzel M., Noel J., and Fleurence J. Protein changes in post mortem sea bass (Dicentrarchus labrax) muscle monitored by one- and two-dimensional gel electrophoresis. Electrophoresis 22 (2001) 1539-1544
31. Yamashita M., and Konagaya S. Hydrolytic action of salmon cathepsin B and L to muscle structural proteins in respect of muscle softening. Nipppon Suisan Gakkaishi 57 10 (1991) 1917-1922
32. Yokoyama M., and Nakazoe J.-I. Effects of dietary protein levels on free amino acid and glutathione contents in the tissues of rainbow trout. Comparative Biochemistry and Physiology 99A (1991) 203-206