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http://dx.doi.org/10.5851/kosfa.2014.34.2.207

Effects of pH-Shift Processing and Microbial Transglutaminase on the Gel and Emulsion Characteristics of Porcine Myofibrillar System  

Hong, Geun-Pyo (Department of Food Bioengineering, Jeju National University)
Chun, Ji-Yeon (Department of Bioindustrial Technologies, Konkuk University)
Jo, Yeon-Ji (Department of Bioindustrial Technologies, Konkuk University)
Choi, Mi-Jung (Department of Bioresources and Food Science, Konkuk University)
Publication Information
Food Science of Animal Resources / v.34, no.2, 2014 , pp. 207-213 More about this Journal
Abstract
This study investigated the effects of microbial transglutaminase (MTGase) and pH-shift processing on the functional properties of porcine myofibrillar proteins (MP). The pH-shift processing was carried out by decreasing the pH of MP suspension to 3.0, followed by re-adjustment to pH 6.2. The native (CM) and pH-shifted MP (PM) was reacted with and without MTGase, and the gelling and emulsion characteristics were compared. To compare the pH-shifted MTGase-treated MP (PT), deamidation (DM) was conducted by reacting MTGase with MP at pH 3.0. Rigid thermal gel was produced by MTGase-treated native MP (CT) and PT. PM and DM showed the lowest storage modulus (G') at the end of thermal scanning. Both MTGase and pH-shifting produced harder MP gel, and the highest gel strength was obtained in PT. All treatments yielded lower than CM, and CT showed significantly higher yield than PM and DM treatments. For emulsion characteristics, pH-shifting improved the emulsifying ability of MP-stabilized emulsion, while the treatments had lower emulsion stability. PM-stabilized emulsion exhibited the lowest creaming stability among all treatments. The emulsion stability could be improved by the usage of MTGase. The results indicated that pH-shifting combined with MTGase had a potential application to modify or improve functional properties of MP in manufacturing of meat products.
Keywords
transglutaminase; myofibrillar; pH-shifting; deamidation; functional properties;
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  • Reference
1 Hamm. (1986) Functional properties of the myofibrillar system and their measurements. In: Muscle as food.P. J. Bechtel (ed.), pp. 135-199. New York: Academic Press, Inc.
2 Dickinson, E. (2003) Hydrocolloids at interface and the influence on the properties of dispersed systems. Food Hydrocolloid. 17, 25-39.   DOI   ScienceOn
3 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.
4 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, 185-193.   DOI   ScienceOn
5 Hong, G. P., and Xiong, Y. L. (2012) Microbial transglutaminase- induced structural and rheological changes of cationic and anionic myofibrillar proteins. Meat Sci. 91, 36-42.   DOI   ScienceOn
6 Ingadottir, B. and Kristinsson, H. G. (2010) Gelation of protein isolates extracted from tilapia light muscle by pH shift processing. Food Chem. 118, 789-798.   DOI   ScienceOn
7 Ionescu, A., Aprodu, I., Daraba, A., and Porneala, L. (2008) The effects of transglutaminase on the functional properties of the myofibrillar protein concentrate obtained from beef heart. Meat Sci. 79, 278-284.   DOI   ScienceOn
8 Jiang, J., Chen, J., and Xiong, Y. L. (2009) Structural and emulsifying properties of soy protein isolates subjected to acid and alkaline pH-shifting processes. J. Agric. Food Chem. 57, 7576-7583.   DOI   ScienceOn
9 Orru, S., Caputo, I., D'Amato, A., Ruoppolo, M., and Esposito, C. (2003) Proteomics identification of acyl-acceptor and acyl-donor substrates for transglutaminase in a human intestinal epithelial cell line. J. Biol. Chem. 278, 31766-31773.   DOI   ScienceOn
10 Kristinsson, H. G. and Hultin, H. O. (2003) Changes in conformation and subunit assembly of cod myosin at low and high pH and after subsequent refolding. J. Agric. Food Chem. 51, 7187-7196.   DOI   ScienceOn
11 Kuraish, C., Sakamoto, K., 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.   DOI   ScienceOn
12 Tadpitchayangkoon, P., Park, J. W., Mayer, S. G., and Yongsawatdigul, J. (2010) Structural changes and dynamic rheological properties of sarcoplasmic proteins subjected to pHshift method. J. Agric. Food Chem. 58, 4241-4249.   DOI   ScienceOn
13 Pearce, K. N., and Kinsella, J. E. (1978) Emulsifying properties of proteins: Evaluation of a turbidimetric technique. J. Agric. Food Chem. 26, 716-723.   DOI
14 Perez-Mateos, M. and Lanier, T. C. (2006) Comparison of Atlantic menhaden gels from surimi processed by acid or alkaline solubilisation. Food Chem. 101, 1223-1229.
15 Ramirez-Suarez, J. C. and Xiong, Y. L. (2003) Rheological properties of mixed muscle/nonmuscle protein emulsions treated with transglutaminase at two ionic strengths. Int. J. Food Sci. Technol. 38, 777-785.   DOI   ScienceOn
16 Trevino, S. R., Scholtz, J. M., and Pace, C. N. (2007) Amino acid contribution to protein solubility: Asp, Glu, and Ser contribute more favorable than the other hydrophilic amino acids in RNase Sa. J. Mol. Biol. 366, 449-460.   DOI   ScienceOn
17 Xiong, Y. L. (1992) A comparison of the rheological characteristics of different fractions of chicken myofibrillar proteins. J. Food Biochem. 16, 217-227.   DOI   ScienceOn
18 Xiong, Y. L. and Blanchard, S. P. (1994) Myofibrillar protein gelation: viscoelastic changes related to heating procedures. J. Food Sci. 59, 734-738.   DOI   ScienceOn
19 Rawdkuen, S., Sai-Ut, S., Khamsorn, S., Chaijan, M., and Benjakul, S. (2009) Biochemical and gelling properties of tilapia surimi and protein recovered using an acid-alkaline process. Food Chem. 112, 112-119.   DOI   ScienceOn
20 Kristinsson, H. G. and Liang, Y. (2006) Effect of pH-shift processing and surimi processing on Atlantic croaker (Micropogonias undulates) muscle proteins. J. Food Sci. 71, C304-C312.   DOI   ScienceOn
21 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.   DOI   ScienceOn