Browse > Article
http://dx.doi.org/10.5851/kosfa.2015.35.2.225

Effect of Fish Sarcoplasmic Protein on Quality Attributes of No-fat Chicken Sausages Mediated by Microbial Transglutaminase  

Hemung, Bung-Orn (Faculty of Applied Science and Engineering, Khon Kaen University)
Chin, Koo Bok (Department of Animal Science and Functional Food Research Institute, College of Agriculture and Life Science, Chonnam National University)
Publication Information
Food Science of Animal Resources / v.35, no.2, 2015 , pp. 225-231 More about this Journal
Abstract
Fish sarcoplasmic protein (SP) obtaining from lyophilization was evaluated its effect on the qualities of the no-fat chicken sausages in the presence of microbial transglutaminase (MTG) as compared to sodium tripolyphosphate (STPP). The cooking yields of all sausage samples were not different. Expressible moisture (EM) of sausage samples was reduced by adding fish SP, while the lowest EM values were observed in sausage samples containing STPP. The pH values of sausage samples were increased with the addition of fish SP and STPP. Proximate analysis revealed that the moisture, fat, and protein contents of all samples were not different (p>0.05). Textural properties (TP), measured by texture profile analysis, showed that hardness of no-fat sausages increased upon adding fish SP. However, the highest TP values were found in sausage samples with STPP. The redness values were reduced in sausage samples with STPP, while other color values were not affected by STPP. Sensory evaluation revealed that sausages with fish SP were accepted at the higher level than that of control. However, sausage samples with STPP showed highest TP and acceptability. Thus, partial substitution of STPP by SP would be possible to reduce phosphate level in the chicken sausages.
Keywords
fish sarcoplasmic protein; quality attributes; no-fat chicken sausages; microbial transglutaminase;
Citations & Related Records
Times Cited By KSCI : 1  (Citation Analysis)
연도 인용수 순위
1 Ahhmed, A. M., Kawahara, S., Ohta, K., Kakade, K., Soeda, T., and Muguruma, M. (2007) Differentiation in improvements of gel strength in chicken and beef sausages induced by transglutaminase. Meat Sci. 76, 455-462.   DOI   ScienceOn
2 Ahhmed, A. M., Nasu, T., Huy, D. Q., Tomisaka, Y., Kawahara, S., and Muguruma, M (2009). Effect of microbial transglutaminase on the natural actomyosin cross-linking in chicken and beef. Meat Sci. 82, 170-178.   DOI   ScienceOn
3 Ando, H., Adachi, M., Umeda, K., Matsuura, M., Nonaka, M., Uchio, R., Tanaka, H., and Motoki, M (1989). Purification and characteristics of novel transglutaminase derived from microorganisms. Agric. Biol. Chem. 53, 2613-2617.   DOI
4 Association of official analytical chemists. 2000. Meat and meat products-Method 950. 46. 991. 36. Maryland, USA. pp. 1, 3, 7-8.
5 Chin, K. B., Keeton, J. T., Longnecker, M. T., and Lamkey, J. W. (1999) Utilization of soy protein isolate and konjac blends in a low-fat bologna (model system). Meat Sci. 53, 45-57.   DOI   ScienceOn
6 Hemung, B. and Chin, K. B. (2013) Effects of fish sarcoplasmic proteins on the properties of myofibrillar protein mediated by microbial transglutaminase. LWT-Food Sci. Technol. 53, 184-190.   DOI   ScienceOn
7 Dimitrakopoulou, M. A., Ambrosiadis, J. A., Zetou, F. K., and Bloukas, J. G. (2005) Effect of salt and transglutaminase (TG) level and processing conditions on quality characteristics of phosphate-free, cooked, restructured pork shoulder. Meat Sci. 70, 743-749.   DOI   ScienceOn
8 Folk, J. E. (1980) Transglutaminase. Ann. Rev. Biochem. 49, 517-531.   DOI   ScienceOn
9 Go, W. C. and Hwang, M. S. (1995) Contribution of milkfish sarcoplasmic protein to the thermal gelation of mofibrillar protein. Fish Sci. 61, 75-78.   DOI
10 Hemung, B. and Chin, K. B. (2014) Effect of pH-treated fish sarcoplasmic proteins on the functional properties of chicken myofibrillar protein gel mediated by microbial tranglutaminase. Korean J. Food Sci. An. 34, 1-9.   DOI   ScienceOn
11 Hong, G. P. and Chin, K. B. (2010) Effect of microbial transglutaminase and sodium alginate on cold set gelation of porcine myofibrillar protein with various salt levels. Food Hydrocolloid. 24, 444-451.   DOI   ScienceOn
12 Jafarpour, A. and Gorczyca, E. M. (2009) Characteristics of sarcoplasmic proteins and their interactions with surimi and kamaboko gel. J. Food Sci. 74, 16-22.
13 Kim, Y. S., Yongsawatdigul, J., Park, J. W., and Thawornchinsombut, S. (2005) Characteristics of sarcoplasmic proteins and their interaction with myofibrillar proteins. J. Food Biochem. 29:517-31.   DOI   ScienceOn
14 Lin, T. M., Park, J. W., and Morrissey, M. T. (1995) Recovered proteins and reconditioned water from surimi processing waste. J. Food Sci. 50, 4-9.
15 Ruusunen, M., Vainionpaa, J., Puolanne, E., Lyly, M., Lahteenmaki, L., Niemisto, M., and Ahvenainen, R. (2003) Physical and sensory properties of low-salt phosphate-free frankfurters composed with various ingredients. Meat Sci. 63, 9-16.   DOI   ScienceOn
16 Serdaroglu, M. (2006) The characteristics of beef patties containing different levels of fat and oat flour. Inter. J. Food Sci. Tech. 41,147-153.   DOI   ScienceOn
17 Pietrasik, Z., Jarmoluk, A., and Shand, P. J. (2007) Effect of non meat proteins on hydration and textural properties of pork meat gels enhanced with microbial transglutaminase. LWT-Food Sci. Technol. 40, 915-920.   DOI   ScienceOn
18 Ramirez-Suarez, J. C. and Xiong, Y. L. (2003) Effect of transglutaminase-induced cross-linking on gelation of myofibrillar/soy protein mixtures. Meat Sci. 65, 899-907.   DOI   ScienceOn
19 Shahidi, F. and Synowiecki, J. (1997) Protein hydrolizates from seal meat as phosphate alternatives in food processing applications. Food Chem. 60, 29-32.   DOI   ScienceOn
20 Steinhauer, J. E. (1983) Food phosphates for use in the meat, poultry and seafood industry. Dairy Food Sanitation. 3, 244-247.
21 Trout, G. R. and Schmidt, G. R. (1984) Effect of phosphate type and concentration, salt level and method of preparation on binding in restructured beef rolls. J. Food Sci. 49, 687-694.   DOI
22 Tseng, T. F., Liu, D. C., and Chen, M. T. (2000) Evaluation of transglutaminase on the quality of low-salt chicken meatballs. Meat Sci. 55, 427-431.   DOI   ScienceOn
23 United States Department of Agriculture (USDA). (1982) Meat and poultry products: phosphates and sodium hydroxide. Federal Registration, 47, 10779.
24 Yongsawatdigul, J. and Hemung, B. (2010) Structural changes and functional properties of threadfin bream sarcoplasmic proteins subjected to pH-shifting treatments and lyophilization. J. Food Sci. 75, C251-257.   DOI   ScienceOn
25 Yang, H. S., Ali, M. S., Jeong, J. Y., Moon, S. H., Hwang, Y. H., Park, G. B., and Joo, S. T. (2009) Properties of duck meat sausages supplemented with cereal flours. Poultry Sci. 88, 1452-1458.   DOI   ScienceOn