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Effect of NaCl, Gum Arabic and Microbial Transglutaminase on the Gel and Emulsion Characteristics of Porcine Myofibrillar Proteins
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 Title & Authors
Effect of NaCl, Gum Arabic and Microbial Transglutaminase on the Gel and Emulsion Characteristics of Porcine Myofibrillar Proteins
Davaatseren, Munkhtugs; Hong, Geun-Pyo;
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 Abstract
This study investigated the effect of gum arabic (GA) combined with microbial transglutaminase (TG) on the functional properties of porcine myofibrillar protein (MP). As an indicator of functional property, heat-set gel and emulsion characteristics of MP treated with GA and/or TG were explored under varying NaCl concentrations (0.1-0.6 M). The GA improved thermal gelling ability of MP during thermal processing and after cooling, and concomitantly added TG assisted the formation of viscoelastic MP gel formation. Meanwhile, the addition of GA decreased cooking yield of MP gel at 0.6 M NaCl concentration, and the yield was further decreased by TG addition, mainly attributed by enhancement of protein-protein interactions. Emulsion characteristics indicated that GA had emulsifying ability and the addition of GA increased the emulsification activity index (EAI) of MP-stabilized emulsion. However, GA showed a negative effect on emulsion stability, particularly great drop in the emulsion stability index (ESI) was found in GA treatment at 0.6 M NaCl. Consequently, the results indicated that GA had a potential advantage to form a viscoelastic MP gel. For the practical aspect, the application of GA in meat processing had to be limited to the purposes of texture enhancer such as restructured products, but not low-salt products and emulsion-type meat products.
 Keywords
myofibrillar;gum arabic;transglutaminase;ionic strength;functional properties;
 Language
English
 Cited by
 References
1.
Ali, B. H., Ziada, A., and Blunden, G. (2009) Biological effects of gum arabic: A review of some recent research. Food Chem. Toxicol. 47, 1-8. crossref(new window)

2.
Belitz, H. D., Grosch, W., and Schieberle, P. (2009) Food Chemistry. 4th ed, Springer-Verlag, Berlin, pp. 248-339.

3.
Chanamai, R. and McClements, D. J. (2002) Comparison of gum arabic, modified starch, and whey protein isolate as emulsifiers: Influence of pH, $CaCl_2$ and temperature. J. Food Sci. 67, 120-125. crossref(new window)

4.
Chin, K. B., Go, M. Y., and 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 Sci. 81, 565-572. crossref(new window)

5.
Chobert, J. M., Bertrand-Herb, C., and Nicolas, M. G. (1988) Solubility and emulsifying properties of caseins and whey proteins modified enzymatically by trypsin. J. Agr. Food Chem. 36, 883-892. crossref(new window)

6.
Colas, B., Caer, D., and Fournier, E. (1993) Transglutaminase-catalyzed glycosylation of vegetable proteins. Effect on solubility of pea legumin and wheat gliadins. J. Agr. Food Chem. 41, 1811-1815. crossref(new window)

7.
Djordjevic, D., Cercaci, L., Alamed, J., McClements, D. J., and Decker, E. A. (2008) Chemical and physical stability of protein- and gum arabic- stabilized oil-in-water emulsions containing limonene. J. Food Sci. 73, 167-172.

8.
Flanagan, J. and Singh, H. (2006) Conjugation of sodium caseinate and gum arabic catalyzed by transglutaminase. J. Agr. Food Chem. 54, 7305-7310. crossref(new window)

9.
Gornall, A. G., Bardawill, C. J., and David, M. M. (1949) Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177, 751-766.

10.
Hong, G. P. and Chin, K. B. (2010) Effects of microbial transglutaminase and sodium alginate on cold-set gelation of porcine myofibrillar protein with various salt levels. Food Hydrocolloid. 24, 444-451. crossref(new window)

11.
Hong, G. P., Min, S. G., and Chin, K. B. (2012) Emulsion properties of pork myofibrillar protein in combination with microbial transglutaminase and calcium alginate under various pH conditions. Meat Sci. 90, 188-193.

12.
Ionescu, A., Aprodu, I., Zara, M., Vasile, A., and Porneala, L. (2007) Evaluation of some functional properties of the myofibrillar protein concentrate from the beef heart. Sci. Stud. Res. 8, 155-168.

13.
Kato, A. (2002) Industrial applications of Maillard-type protein- polysaccharide conjugates. Food Sci. Technol. Res. 8, 193-199. crossref(new window)

14.
Kristinsson, H. G. and Hultin, H. O. (2003) Effect of low and high pH treatment on the functional properties of cod muscle proteins. J. Agr. Food Chem. 51, 5103-5110. crossref(new window)

15.
Kuraish, C., Sakamoto, J., Yamazaki, K., Susa, Y., Kuhara, C., and Soeda, T. (1997) Production of restructured meat using microbial transglutaminase without salt or cooking. J. Food Sci. 62, 488-490, 515.

16.
Montenegro, M. A., Boiero, M. L., Valle, L., and Borsarelli, C. D. (2012) Gum Arabic: More than an edible emulsifier. In: Products and applications of biopolymers. Verbeek, J. (ed) InTech, Croatia, pp. 3-26.

17.
Pearce, K. N. and Kinsella, J. E. (1978) Emulsifying properties of proteins: Evaluation of a turbidimetric technique. J. Agr. Food Chem. 26, 716-723. crossref(new window)

18.
Perez-Mateos, M. and Montero, P. (2000) Contribution of hydrocolloids to gelling properties of blue whiting muscle. Eur. Food Res. Technol. 210, 383-390. crossref(new window)

19.
Sang, L. Y., Zhou, X. H., Yun, F., and Zhang, G. L. (2009) Enzymatic synthesis of chitosan-gelatin antimicrobial copolymer and its characterization. J. Sci. Food Agric. 90, 58-64.

20.
Sato, R., Katayama, S., Sawabe, T., and Saeki, H. (2003) Stability and emulsion-forming ability of water-soluble fish myofibrillar protein prepared by conjugation with alginate oligosaccharide. J. Agr. Food Chem. 51, 4376-4381. crossref(new window)

21.
Sato, R., Sawabe, T., Kishimura, H., Hayashi, K., and Saeki, H. (2000) Preparation of neoglycoprotein from carp myofibrillar protein and alginate oligosaccharide: Improved solubility in low ionic strength medium. J. Agr. Food Chem. 48, 17-21. crossref(new window)

22.
Shang, Y. and Xiong, Y. L. (2010) Xanthan enhances water binding and gel formation of transglutaminase-treated porcine myofibrillar proteins. J. Food Sci. 75, 178-185.

23.
Todd, S. L., Cunningham, F. E., Claus, J. R., and Schwenke, J. R. (1989) Effect of dietary fiber on the texture and cooking characteristics of restructured pork. J. Food Sci. 54, 1190-1192. crossref(new window)

24.
Tolstoguzov, V. (2003) Some thermodynamic considerations in food formulation. Food Hydrocolloid. 17, 1-23. crossref(new window)

25.
Xiong, Y. L. (1993) A comparison of the rheological characteristics of different fractions of chicken myofibrillar proteins. J. Food Biochem. 16, 217-227.

26.
Xiong, Y. L. (2004) Muscle proteins. In: Proteins in food processing. Yada, R. (ed) Woodhead Publishing Ltd., Cambridge, pp. 100-122.

27.
Yadav, M. P., Manuel Igartuburu, J., Yan, Y., and Nothnagel, E. A. (2007) Chemical investigation of the structural basis of the emulsifying activity of gum Arabic. Food Hydrocolloid. 21, 297-308. crossref(new window)