Effects of high pressure processing on the thermal gelling properties of chicken breast myosin containing κ-carrageenan

Food Hydrocolloids

Volumn 40, Issue , 2014, Pages 262-272

  Chen, Xing ^a   Chen, Cong gui ^a   Zhou, Yan zi ^a   Li, Pei jun ^a   Ma, Fei ^a   Nishiumi, Tadayuki ^b   Suzuki, Atsushi ^b  

^a HEFEI UNIVERSITY   (China)

^b NIIGATA UNIVERSITY   (Japan)

Author keywords

Gel properties; High pressure processing; Myosin protein; Thermal gelling mechanism; Carrageenan

Indexed keywords

ANIMALS; FOURIER TRANSFORM INFRARED SPECTROSCOPY; GELATION; GELS; HIGH PRESSURE EFFECTS; HYDROGEN; HYDROGEN BONDS; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SCANNING ELECTRON MICROSCOPY;

CARRAGEENANS; GEL PROPERTIES; GEL STRENGTHS; GELLING MECHANISMS; HIGH-PRESSURE PROCESSING; MYOSIN PROTEIN; THERMAL GELLING; THERMAL GELLING MECHANISM; WATER-HOLDING CAPACITY; Κ-CARRAGEENAN;

PROTEINS;

EID: 84897941269     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2014.03.018     Document Type: Article

References (60)

1. Ayadi M.A., Kechaou A., Makni I., Attia H. Influence of carrageenan addition on turkey meat sausages properties. Journal of Food Engineering 2009, 93(3):278-283.
2. Balny C., Masson P. Effects of high pressure on proteins. Food Reviews International 1993, 9(4):611-628.
3. Barth A. Infrared spectroscopy of proteins. Biochimica et Biophysica Acta (BBA) - Bioenergetics 2007, 1767(9):1073-1101.
4. Bertram H.C., Andersen H.J., Karlsson A.H. Comparative study of low-field NMR relaxation measurements and two traditional methods in the determination of water holding capacity of pork. Meat Science 2001, 57(2):125-132.
5. Bertram H.C., Kohler A., Böcker U., Ofstad R., Andersen H.J. Heat-induced changes in myofibrillar protein structure and myowater of two pork qualities. A combined FT-IR spectroscopy and low-field NMR relaxometry study. Journal of Agricultural and Food Chemistry 2006, 54(5):1740-1746.
6. Bhattacharjee C., Saha S., Biswas A., Kundu M., Ghosh L., Das K.P. Structural changes of β-lactoglobulin during thermal unfolding and refolding-an FT-IR and circular dichroism study. The Protein Journal 2005, 24(1):27-35.
7. Boonyaratanakornkit B.B., Park C.B., Clark D.S. Pressure effects on intra-and intermolecular interactions within proteins. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 2002, 1595(1-2):235-249.
8. Cao Y.Y., Xia T.L., Zhou G.H., Xu X.L. The mechanism of high pressure-induced gels of rabbit myosin. Innovative Food Science & Emerging Technologies 2012, 16:41-46.
9. Carbonaro M., Nucara A. Secondary structure of food proteins by Fourier transform spectroscopy in the mid-infrared region. Amino Acids 2010, 38(3):679-690.
10. Chapleau N., Mangavel C., Compoint J.P., de Lamballerie-Anton M. Effect of high-pressure processing on myofibrillar protein structure. Journal of the Science of Food and Agriculture 2004, 84(1):66-74.
11. Chattong U., Apichartsrangkoon A., Bell A.E. Effects of hydrocolloid addition and high pressure processing on the rheological properties and microstructure of a commercial ostrich meat product "Yor" (Thai sausage). Meat Science 2007, 76(3):548-554.
12. Chen C.G., Wang R., Sun G.J., Fang H.M., Ma D.R., Yi S.L. Effects of high pressure level and holding time on properties of duck muscle gels containing 1% curdlan. Innovative Food Science & Emerging Technologies 2010, 11(4):538-542.
13. Chen H.H., Xu S.Y., Wang Z. Interaction between flaxseed gum and meat protein. Journal of Food Engineering 2007, 80(4):1051-1059.
14. Cierach M., Modzelewska-Kapituła M., Szaciło K. The influence of carrageenan on the properties of low-fat frankfurters. Meat Science 2009, 82(3):295-299.
15. DeFreitas Z., Sebranek J.G., Olson D.G., Carr J.M. Carrageenan effects on salt-soluble meat proteins in model systems. Journal of Food Science 1997, 62(3):539-543.
16. Dickinson E. Mixed biopolymers at interfaces: competitive adsorption and multilayer structures. Food Hydrocolloids 2011, 25(8):1966-1983.
17. Fang J.M., Fowler P.A., Tomkinson J., Hill C.A.S. The preparation and characterisation of a series of chemically modified potato starches. Carbohydrate Polymers 2002, 47(3):245-252.
18. Galazka V.B., Smith D., Ledward D.A., Dickinson E. Complexes of bovine serum albumin with sulphated polysaccharides: effects of pH, ionic strength and high pressure treatment. Food Chemistry 1999, 64(3):303-310.
19. Galazka V.B., Smith D., Ledward D.A., Dickinson E. Interactions of ovalbumin with sulphated polysaccharides: effects of pH, ionic strength, heat and high pressure treatment. Food Hydrocolloids 1999, 13(2):81-88.
20. Han M.Y., Zhang Y.J., Fei Y., Xu X.L., Zhou G.H. Effect of microbial transglutaminase on NMR relaxometry and microstructure of pork myofibrillar protein gel. European Food Research and Technology 2009, 228(4):665-670.
21. Hayakawa T., Yoshida Y., Yasui M., Ito T., Iwasaki T., Wakamatsu J., et al. Heat-induced gelation of myosin in a low ionic strength solution containing L-histidine. Meat Science 2012, 90(1):77-80.
22. He J.S., Mu T.H., Guo X.S., Zhu S.M., Azuma N., Kanno C. Comparison of the gel-forming ability and gel properties of α-lactalbumin, lysozyme and myoglobin in the presence of β-lactoglobulin under high pressure. Food Hydrocolloids 2013, 33(2):415-424.
23. Hills B.P., Takacs S.F., Belton P.S. The effects of proteins on the proton NMR transverse relaxation times of water: I. Native bovine serum albumin. Molecular Physics 1989, 67(4):903-918.
24. Hong G., Park S., Kim J., Min S. The effects of high pressure and various binders on the physico-chemical properties of restructured pork meat. Asian Australasian Journal of Animal Sciences 2006, 19(10):1484-1489.
25. Hsu K.C., Ko W.C. Effect of hydrostatic pressure on aggregation and viscoelastic properties of tilapia (Orechromis niloticus) myosin. Journal of Food Science 2001, 66(8):1158-1162.
26. Hwang J.S., Lai K.M., Hsu K.C. Changes in textural and rheological properties of gels from tilapia muscle proteins induced by high pressure and setting. Food Chemistry 2007, 104(2):746-753.
27. Ikeda S., Nishinari K. "Weak Gel"-Type rheological properties of aqueous dispersions of nonaggregated κ-carrageenan helices. Journal of Agricultural and Food Chemistry 2001, 49(9):4436-4441.
28. Ikeuchi Y., Tanji H., Kim K., Suzuki A. Mechanism of heat-induced gelation of pressurized actomyosin: pressure-induced changes in actin and myosin in actomyosin. Journal of Agricultural and Food Chemistry 1992, 40(10):1756-1761.
29. Iwasaki T., Washio M., Yamamoto K., Nakamura K. Rheological and morphological comparison of thermal and hydrostatic pressure-induced filamentous myosin gels. Journal of Food Science 2005, 70(7):e432-e436.
30. Iwasaki T., Yamamoto K. Changes in rabbit skeletal myosin and its subfragments under high hydrostatic pressure. International Journal of Biological Macromolecules 2003, 33(4):215-220.
31. Jimenez-Colmenero F., Cofrades S., Herrero A.M., Solas M.T., Ruiz-Capillas C. Konjac gel for use as potential fat analogue for healthier meat product development: effect of chilled and frozen storage. Food Hydrocolloids 2013, 30(1):351-357.
32. Kocher P.N., Foegeding E.A. Microcentrifuge-based method for measuring water holding of protein gels. Journal of Food Science 1993, 58(5):1040-1046.
33. 1H NMR studies of water in chicken breast marinated with different phosphates. Journal of Food Science 2000, 65(4):575-580.
34. Liu R., Zhao S.M., Xiong S.B., Xie B.J., Qin L.H. Role of secondary structures in the gelation of porcine myosin at different pH values. Meat Science 2008, 80(3):632-639.
35. Liu R., Zhao S.M., Yang H., Li D.D., Xiong S.B., Xie B.J. Comparative study on the stability of fish actomyosin and pork actomyosin. Meat Science 2011, 88(2):234-240.
36. 2 on properties of salt-soluble meat protein gels containing locust bean gum. Innovative Food Science & Emerging Technologies 2012, 14:31-37.
37. 2 and κ-carrageenan. Meat Science 2013, 95(1):22-26.
38. Mangione M.R., Giacomazza D., Bulone D., Martorana V., San Biagio P.L. Thermoreversible gelation of κ-Carrageenan: relation between conformational transition and aggregation. Biophysical Chemistry 2003, 104(1):95-105.
39. Montero P., Solas T., Perez-Mateos M. Pressure-induced gel properties of fish mince with ionic and non-ionic gums added. Food Hydrocolloids 2001, 15(2):185-194.
40. Muyonga J.H., Cole C.G.B., Duodu K.G. Fourier transform infrared (FTIR) spectroscopic study of acid soluble collagen and gelatin from skins and bones of young and adult Nile perch (Lates niloticus). Food Chemistry 2004, 86(3):325-332.
41. Nakai S., Li-Chan E. Hydrophobicity-functionality relationship of food proteins. Hydrophobic Interactions in Food Systems 1988, 23-41.
42. Naumann D. FT-infrared and FT-Raman spectroscopy in biomedical research. Applied Spectroscopy Reviews 2001, 36(2-3):239-298.
43. Pawlak A., Mucha M. Thermogravimetric and FTIR studies of chitosan blends. Thermochimica Acta 2003, 396(1):153-166.
44. Pérez-Mateos M., Solas T., Montero P. Carrageenans and alginate effects on properties of combined pressure and temperature in fish mince gels. Food Hydrocolloids 2002, 16(3):225-233.
45. Perisic N., Afseth N.K., Ofstad R., Kohler A. Monitoring protein structural changes and hydration in bovine meat tissue due to salt substitutes by Fourier transform infrared (FTIR) microspectroscopy. Journal of Agricultural and Food Chemistry 2011, 59(18):10052-10061.
46. Pietrasik Z., Li-Chan E.C.Y. Binding and textural properties of beef gels as affected by protein, κ-carrageenan and microbial transglutaminase addition. Food Research International 2002, 35(1):91-98.
47. Riebroy S., Benjakul S., Visessanguan W., Erikson U., Rustad T. Comparative study on acid-induced gelation of myosin from Atlantic cod (Gardus morhua) and burbot (Lota lota). Food Chemistry 2008, 109(1):42-53.
48. Ruiz-Capillas C., Triki M., Herrero A.M., Rodriguez-Salas L., Jiménez-Colmenero F. Konjac gel as pork backfat replacer in dry fermented sausages: processing and quality characteristics. Meat Science 2012, 92(2):144-150.
49. Samejima K., Ishioroshi M., Yasui T. Relative roles of the head and tail portions of the molecule in heat-induced gelation of myosin. Journal of Food Science 1981, 46(5):1412-1418.
50. Sano T., Noguchi S.F., Tsuchiya T., Matsumoto J.J. Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation. Journal of Food Science 1988, 53(3):924-928.
51. Sun J., Li X., Xu X.L., Zhou G.H. Influence of various levels of flaxseed gum addition on the water-holding capacities of heat-induced porcine myofibrillar protein. Journal of Food Science 2011, 76(3):C472-C478.
52. Tanaka N., Ikeda C., Kanaori K., Hiraga K., Konno T., Kunugi S. Pressure effect on the conformational fluctuation of apomyoglobin in the native state. Biochemistry 2000, 39(39):12063-12068.
53. Trius A., Sebranek J.G., Lanier T. Carrageenans and their use in meat products. Critical Reviews in Food Science & Nutrition 1996, 36(1-2):69-85.
54. Trout G.R. Techniques for measuring water-binding capacity in muscle foods-a review of methodology. Meat Science 1988, 23(4):235-252.
55. Verbeken D., Neirinck N., Van Der Meeren P., Dewettinck K. Influence of κ-carrageenan on the thermal gelation of salt-soluble meat proteins. Meat Science 2005, 70(1):161-166.
56. Visessanguan W., Ogawa M., Nakai S., An H. Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin. Journal of Agricultural and Food Chemistry 2000, 48(4):1016-1023.
57. Webb J.N., Webb S.D., Cleland J.L., Carpenter J.F., Randolph T.W. Partial molar volume, surface area, and hydration changes for equilibrium unfolding and formation of aggregation transition state: high-pressure and cosolute studies on recombinant human IFN-γ. Proceedings of the National Academy of Sciences 2001, 98(13):7259-7264.
58. Xiong Y.L., Noel D.C., Moody W.G. Textural and sensory properties of low-fat beef sausages with added water and polysaccharides as affected by pH and salt. Journal of Food Science 1999, 64(3):550-554.
59. Yamamoto S., Otsuka Y., Borjigin G., Masuda K., Ikeuchi Y., Nishiumi T., et al. Effects of a high-pressure treatment on the activity and structure of rabbit muscle proteasome. Bioscience, Biotechnology, and Biochemistry 2005, 69(7):1239-1247.
60. Zhang H., Li L., Tatsumi E., Kotwal S. Influence of high pressure on conformational changes of soybean glycinin. Innovative Food Science & Emerging Technologies 2003, 4(3):269-275.