Effect of peanut protein isolate on functional properties of chicken salt-soluble proteins from breast and thigh muscles during heat-induced gelation

Meat Science

Volumn 91, Issue 1, 2012, Pages 88-92

  Sun, Jingxin ^a   Wu, Zhen ^a   Xu, Xinglian ^b   Li, Peng ^a  

^a QINGDAO AGRICULTURAL UNIVERSITY   (China)

^b NANJING AGRICULTURAL UNIVERSITY   (China)

Author keywords

Functional properties; Heat induced gelation; Peanut protein isolate; Salt soluble proteins

Indexed keywords

FUNCTIONAL PROPERTIES; GEL PROPERTIES; GEL STRENGTHS; MIXED GEL; PEANUT PROTEINS; POTENTIAL PROTEINS; WATER HOLDING CAPACITY;

ANIMALS; COAGULATION; DIFFERENTIAL SCANNING CALORIMETRY; ELASTICITY; GELATION; GELS; MUSCLE; OILSEEDS; SCANNING ELECTRON MICROSCOPY;

PROTEINS;

ARACHIS HYPOGAEA;

FOOD ADDITIVE; MUSCLE PROTEIN; SEED STORAGE PROTEIN; WATER;

ANIMAL; ARTICLE; CHEMISTRY; CHICKEN; COMPARATIVE STUDY; DIFFERENTIAL SCANNING CALORIMETRY; FLOW KINETICS; FOOD HANDLING; GEL; HEAT; MEAT; MECHANICS; PEANUT; PHYSICAL CHEMISTRY; PROTEIN DENATURATION; PROTEIN STABILITY; SOLUBILITY; TRANSITION TEMPERATURE; ULTRASTRUCTURE; YOUNG MODULUS;

ANIMALS; ARACHIS HYPOGAEA; CALORIMETRY, DIFFERENTIAL SCANNING; CHICKENS; ELASTIC MODULUS; FOOD ADDITIVES; FOOD HANDLING; GELS; HOT TEMPERATURE; MEAT PRODUCTS; MECHANICAL PHENOMENA; MUSCLE PROTEINS; PHYSICOCHEMICAL PHENOMENA; PROTEIN DENATURATION; PROTEIN STABILITY; RHEOLOGY; SEED STORAGE PROTEINS; SOLUBILITY; TRANSITION TEMPERATURE; WATER;

EID: 84856397919     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2011.12.010     Document Type: Article

References (24)

1. Amity D.W., Jenni L.B., Steven M.L. Influence of muscle type on rheological properties of porcine myofibrillar protein during heat-induced gelation. Meat Science 2006, 72(4):697-703.
2. Asghar A., Morita J.I., Samejima K., et al. Biochemical and functional characteristics of myosin from red and white muscles of chicken as influenced by nutritional stress. Agricultural and Biological Chemistry 1984, 48(9):2217-2224.
3. Cheo I.S., Yammaoto K., Morita J.I., et al. The heat-induced gelation of myosin rods prepared from chicken leg and breast muscles. Agricultural and Biological Chemistry 1987, 53(3):625-630.
4. Comfort S., Howell K.N. Gelation properties of salt soluble meat protein and soluble wheat protein mixtures. Food Hydrocolloids 2002, 17:149-159.
5. Deng Y., Rosenvold K., Karlsson A.H., Horn J., Hedegarrd J., Steffensen C.L., et al. Relationship between thermal denaturation of porcine muscle proteins and water holding capacity. Journal of Food Science 2002, 67(5):1642-1647.
6. Edwards S.F., Lillford P.J., Blanshard J.M. Gels and networks in practice and theory. Food Structure and Behavior 1987, 1-12.
7. Egelandsdal B., Fretheim K., Samejima K. Myosins from red and white bovine muscles: Part 1-Gel strength (elasticity) and water-holding capacity of heat-induced gels. Food Chemistry 1986, 22(2):107-121.
8. Herreroa A.M., Carmonab P., Cofradesc S., et al. Raman spectroscopic determination of structural changes in meat batters upon soy protein addition and heat treatment. Food Research International 2008, 41(7):765-772.
9. Hongsprabhas P., Barbut S. Effect of pre-heated whey protein level and salt on texture development of poultry meat batters. Food Research International 1999, 32(2):145-149.
10. Lefévre F., Culioli J., Joandel-Monier S., et al. Muscle polymorphism and gelling properties of myofibrillar proteins from poultry, mammals, and fish. Quality attributes of muscle foods 1999, 365-391. Kluwer Academic/Plenum Publishers, New York. Y.L. Xiong, C.-T. Ho, F. Shahidi (Eds.).
11. Lesiόw T., Xiong Y.L. Mechanism of rheological changes in poultry myofibrillar proteins during gelation: a review. Poultry and Avian Biology Reviews 2001, 12(4):137-149.
12. Liu M.N., Foegeding E.A., Wang S.F., et al. Denaturation and aggregation of chicken myosin isoforms. Journal of Agricultural and Food Chemistry 1996, 44:1435-1446.
13. McCord A., Smyth A.B., O'Neill E. Heat-induced gelation properties of salt-soluble muscle proteins as affected by non-meat proteins. Journal of Food Science 1998, 63(4):5802-5831.
14. Palka K., Daun H. Changes in texture, cooking losses, and myofibrillar structure of bovine muscle semitendinosus during heating. Meat Science 1999, 51:237-243.
15. Ramirez-Suarez J.C., Xiong Y.L. Transglutaminase cross-linking of whey/myofibrillar proteins and the effect on protein gelation. Journal of Food Science 2002, 67:2885-2891.
16. Ramirez-Suarez J.C., Xiong Y.L., Wang B. Transglutaminase cross-linking of bovine cardiac myofibrillar proteins and its effect on protein gelation. Journal of Muscle Foods 2001, 12:85-96.
17. Sano T., Noguchi S.F., Tsuchiya T., et al. Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation. Journal of Food Science 1988, 53:924-928.
18. Stone A.P., Stanley D.W. Muscle protein gelation at low ionic strength. Food Research International 1994, 27:155-163.
19. Wagner J.R., Anon M.C. Denaturation kinetics of myofibrillar proteins in bovine muscle. Journal of Food Science 1985, 50:1547-1550. 1563.
20. Wang S.F., Smith D.M., Steffe J.F. Effect of pH on the dynamic rheological properties of chicken breast salt-soluble proteins during heat-induced gelation. Poultry Science 1990, 69(12):2220-2227.
21. Wright D.J., Wilding P. Differential calorimetric study of muscle and its proteins: Myosin and its subfragments. Journal of Food Science 1984, 35:357-372.
22. Xiong Y.L. A comparison of the rheological characteristics of different fraction of chicken myofibrillar proteins. Journal of Food Biochemistry 1993, 16(4):217-227.
23. Xiong Y.L. Myofibrillar protein from different muscle fiber types: implications of biochemical and functional properties in meat processing. CRC Critical Reviews in Food Science and Nutrition 1994, 34:293-320.
24. Youssef M.K., Barbut S. Effects of two types of soy protein isolates, native and preheated whey protein isolates on emulsified meat batters prepared at different protein levels. Meat Science 2011, 87(1):54-60.