Evaluation of mungbean protein isolates at various levels as a substrate for microbial transglutaminase and water binding agent in pork myofibrillar protein gels

International Journal of Food Science and Technology

Volumn 48, Issue 5, 2013, Pages 1086-1092

  Lee, Hong C ^a   Chin, Koo B ^a  

^a Chonnam National University   (South Korea)

Author keywords

Microbial transglutaminase; Mungbean protein isolates; Pork myofibrillar protein; Rheological property

Indexed keywords

MICROBIAL TRANSGLUTAMINASE; MICROBIAL TRANSGLUTAMINASE (MTGASE); MUNG-BEAN PROTEINS; MYOFIBRILLAR PROTEINS; PROTEIN GELATIONS; RHEOLOGICAL PROPERTY; SULPHATE-POLYACRYLAMIDE GEL ELECTROPHORESIS; WATER BINDING CAPACITY;

DIFFERENTIAL SCANNING CALORIMETRY; ELECTROPHORESIS; GELATION; GELS; MEATS; SCANNING ELECTRON MICROSCOPY;

PROTEINS;

EID: 84876325715     PISSN: 09505423     EISSN: 13652621     Source Type: Journal    
DOI: 10.1111/ijfs.12066     Document Type: Article

References (33)

1. Anwar, E., Latif, S., Przybylski, R., Sultana, B. & Ashraf, M. (2007). Chemical composition and antioxidant activity of seeds of different cultivars of mungbean. Journal of Food Science, 72, 503-510.
2. Bertram, H.C., Meyer, R.L., Wu, Z., Zhou, X. & Andersen, H.J. (2008). Water distribution and microstructure in enhanced pork. Journal of Agriculture and Food Chemistry, 56, 7201-7207.
3. Bhumiratana, A. (1978). Mungbean and its utilization in Thailand. In: Proceedings of 1st International Mungbean Symposium (edited by R. Cowell). Pp. 46. Shanhua, Taiwan: Asian Vegetable Research and Development Center.
4. Boye, J., Zare, F. & Pletch, A. (2010). Pulse proteins: processing, characterization, functional properties and applications in food and feed. Food Research International, 43, 414-431.
5. Chin, K.B., Go, M.Y. & Xiong, Y.L. (2009). Konjac flour improved textural and water retention properties of transglutaminase-mediated, heat-induced porcine myofibrillar protein gel: effect of salt level and transglutaminase incubation. Meat Science, 81, 565-572.
6. Deng, Y., Rosenvold, K., Karlsson, A.H. et al. (2002). Relationship between thermal denaturation of porcine muscle proteins and water holding capacity. Journal of Food Science, 67, 1642-1647.
7. Feng, J. & Xiong, Y.L. (2002). Interaction of myofibrillar and preheated soy proteins. Journal of Food Science, 67, 2851-2856.
8. Gornall, A.G., Bardawill, C.Y. & David, M.M. (1949). Determination of serum proteins by means of the biuret reaction. Journal of Biological Chemistry, 177, 751-756.
9. Haga, S. & Ohashi, T. (1984). Heat induced gelation of a mixture of myosin B and soybean protein. Agriculture and Biological Chemistry, 48, 1001-1007.
10. Hong, G.P. & Chin, K.B. (2010). Effects of microbial transglutaminase and sodium alginate on cold-set gelation of porcine myofibrillar protein with various salt levels. Food Hydrocolloids, 24, 444-451.
11. Hwang, J.S., Lee, H.C. & Chin, K.B. (2008). Rheological properties of pork myofibrillar protein and sodium caseinate mixture as affected by transglutaminase with various incubation temperatures and times. Korean Journal for Food Science of Animal Resources, 28, 154-159.
12. Kuraishi, C., Sakamoto, J., Yamazaki, K., Susa, Y., Kuhara, C. & Soeda, T. (1997). Production of restructured meat using microbial transglutaminase without salt or cooking. Journal of Food Science, 62, 488-490, 515.
13. Kye, I.S., Jun, Y.S. & Cheigh, H.S. (1989). Functional properties of mungbean protein isolates. Journal of the Korean Society of Food Science and Nutrition, 18, 300-306.
14. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
15. Langton, M., Astrom, A., Strading, M. & Hermansson, A.M. (1997). Food colloids - proteins, lipids and polysaccharides. In: Effect of Microstructure on Sensory Perception of Particulate Gels (edited by E. Dickinson & B. Bergenstahl). Pp. 18-28. Cambridge: The Royal Society of Chemistry.
16. Lee, H.C. & Chin, K.B. (2004). Reduction of tumbling time and improvement of shear value for the manufacture of restructured hams using transglutaminase. Korean Journal for Food Science of Animal Resources, 24, 23-28.
17. Lee, H.C. & Chin, K.B. (2009a). Effect of transglutaminase, acorn, and mungbean powder on quality characteristics of low-fat/salt pork model sausages. Korean Journal for Food Science of Animal Resources, 29, 374-381.
18. Lee, H.C. & Chin, K.B. (2009b). Effects of transglutaminase and mungbean powder on the functional and textural properties of low-fat/salt pork sausages. In: Proceedings of 62nd Reciprocal Meat Conference (edited by K. Johnson). Pp. 6. Arkansas, USA: Rogers.
19. Lee, H.C. & Chin, K.B. (2010). Evaluation of mungbean protein isolate as a substrate for microbial transglutaminase on heat-induced gelation of pork myofibrillar protein. In: Proceedings of 56th International Congress of Meat Science and Technology (edited by D. Ahn et al.). Pp. 203. Jeju, Korea: Jeju.
20. Lee, H.C. & Chin, K.B. (2011a). Evaluation of various salt levels and different dairy proteins in combination with microbial transglutaminase on the quality characteristics of restructured pork ham. International Journal of Food Science and Technology, 46, 1522-1528.
21. Lee, H.C. & Chin, K.B. (2011b). Effect of the combination of various NaCl levels and soy protein isolate on the quality characteristics of smoked pork loins. International Journal of Food Science and Technology, 46, 1038-1043.
22. Poehlman, J.M. (1991). The Mungbean. Pp. 312-343. Colorado, USA: Westview Press.
23. Pospiech, E., Greaser, M.L., Mikolajczak, B., Chiang, W. & Krzywdzinska, M. (2002). Thermal properties of titin from porcine and bovine muscles. Meat Science, 62, 187-192.
24. Sakamoto, H., Kumazawa, Y. & Motoki, M. (1994). Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions. Journal of Food Science, 59, 866-871.
25. Sebranek, J.G. (2009). Functional properties of muscle proteins: implications for processed meat product characteristics. In: Proceedings of 62nd Reciprocal Meat Conference (edited by K. Johnson). Pp. 39-45. Arkansas, USA: Rogers.
26. Tang, C.H. (2008). Thermal denaturation and gelation of vicilin-rich protein isolates from three Phaseolus legumes: a comparative study. LWT-Food Science and Technology, 41, 1380-1388.
27. Tang, C.H., Xiao, M.L., Chen, Z., Yang, X.Q. & Yin, S.W. (2009). Properties of cast films of vicilin-rich protein isolates from Phaseolus legumes: influence of heat curing. LWT-Food Science and Technology, 42, 1659-1666.
28. Tarte, R. & Amundson, C.M. (2006). Ingredient interactions - effects on food quality. In: Protein Interactions in Muscle Foods - Texture of Processed Meats (edited by A.G. Gaonkar & A. McPherson). Pp. 246-252. Boca Raton, FL: CRC Press.
29. Thompson, L.U. (1977). Preparation and evaluation of mungbean protein isolates. Journal of Food Science, 42, 202-206.
30. Tornberg, E. (2005). Effects of heat on meat proteins - Implications on structure and quality of meat products (review). Meat Science, 70, 493-508.
31. Wagner, J.R. & Anon, M.C. (1985). Effect of freezing rate on the denaturation of myofibrillar proteins. Journal of Food Technology, 20, 735-744.
32. Xiong, Y.L. (1993). A comparison of the rheological characteristics of different fraction of chicken myofibrillar proteins. Journal of Food Biochemistry, 16, 217-227.
33. Xiong, Y.L. & Delles, R.M. (2009). Impact of chemical ingredients and processing on muscle protein functionality. In: Proceedings of 62nd Reciprocal Meat Conference (edited by K. Johnson). Pp. 46-55. Arkansas, USA: Rogers.