Advanced SearchSearch Tips
Effects of pH-treated Fish Sarcoplasmic Proteins on the Functional Properties of Chicken Myofibrillar Protein Gel Mediated by Microbial Transglutaminase
facebook(new window)  Pirnt(new window) E-mail(new window) Excel Download
 Title & Authors
Effects of pH-treated Fish Sarcoplasmic Proteins on the Functional Properties of Chicken Myofibrillar Protein Gel Mediated by Microbial Transglutaminase
Hemung, Bung-Orn; Chin, Koo Bok;
  PDF(new window)
pH adjustment would be of advantage in improving the water holding capacity of muscle proteins. The objective of this study was to evaluate the addition of fish sarcoplasmic protein (SP) solution, which was adjusted to pH 3.0 or 12.0, neutralized to pH 7.0, and lyophilized to obtain the acid- and alkaline-treated SP samples, on the functional properties of the chicken myofibrillar protein induced by microbial transglutaminase (MTG). The solubility of alkaline-treated SP was higher than that of the acid counterpart; however, those values of the two pH-treated samples were lower than that of normal SP (p<0.05). All SP solutions were mixed with myofibrillar proteins (MP) extracted from chicken breast, and incubated with MTG. The shear stresses of MP with acid- and alkaline-treated SP were higher than that of normal SP. The thermal stability of MP mixture reduced upon adding SP, regardless of the pH treatment. The breaking force of MP gels with acid-treated SP increased more than those of alkaline-treated SP, while normal SP showed the highest value. The MP gel lightness increased, but cooking loss reduced, with the addition of SP. Smooth microstructure of the gel surface was observed. These results indicated that adjusting the pH of SP improved the water holding capacity of chicken myofibrillar proteins induced by MTG.
fish sarcoplasmic proteins;acid and alkaline treatments;microbial transglutaacminase;cooking loss;chicken myofibrillar protein;
 Cited by
Effect of Fish Sarcoplasmic Protein on Quality Attributes of No-fat Chicken Sausages Mediated by Microbial Transglutaminase,;;

한국축산식품학회지, 2015. vol.35. 2, pp.225-231 crossref(new window)
Ahhmed, A. M., Kuroda, R., Kawahara, S., Ohta, K., Nakade, K., Aoki, T., and Muguruma, M. (2009) Dependence of microbial transglutaminase on meat type in myofibrillar protein cross-linking. Food Chem. 112, 354-361. crossref(new window)

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. crossref(new window)

AOAC (2000) Meat and meat products - Method 950.46.991.36. Maryland, USA. pp.1, 3, 7-8.

Cardoso, C., Mendes, R., Vaz-pires, P., and Nunes, M. L. (2010) Effect of salt and MTG on the production of high quality gels from farmed sea bass. J. Food Eng. 101, 98-105. crossref(new window)

Chaijan, M., Benjakul, S., Visessanguan, W. Lee, S., and Faustman, C. (2008) Interaction of fish myoglobin and myofibrillar proteins. J. Food Sci. 73, C292-298.

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. crossref(new window)

Folk, J. E. (1980) Transglutaminase. Ann. Rev. Biochem. 49, 517-531. crossref(new window)

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.

Hemung, B. and Chin, K. B. (2013) Effects of fish sarcoplasmic proteins on the properties of myofibrillar protein gels mediated by microbial transglutaminase. LWT. Food Sci. Tech. 53, 184-190. crossref(new window)

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. crossref(new window)

Jafarpour, A. and Gorczyca, E. M. (2009) Characteristics of sarcoplasmic proteins and their interactions with surimi and kamaboko gel. J. Food Sci. 74, N16-N22.

Karthikeyan, K., Mathew, S., Shamasundar, B. A., and Prakash, V. (2004) Fractionation and properties of sarcoplasmic proteins from oil sardine (Sardinella longiceps): Influence on the thermal gelation behavior of washed meat. J. Food Sci. 69, 79-83.

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, 517-531. crossref(new window)

Krasaechol, N., Sanguandeekul, R., Duangmal, K., and Owusu- Apenten, R. K. (2008) Structure and functional properties of modified threadfin bream sarcoplasmic protein. Food Chem. 107, 1-10. crossref(new window)

Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685. crossref(new window)

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.

Park, J. D. and Park, J. W. (2007) Extraction of sardine myoglobin and its effect on gelation properties of Pacific whiting surimi. J. Food Sci. 72, C202-206. crossref(new window)

Perez-Alvarez, J. A., Sayas-Barbera, M. E., Fernandez-Lopez, J., and Aranda-Catala, V. (1999) Physicochemical characteristics of Spanish-type dry-cured sausage. Food Res. Inter. 32, 599-607. crossref(new window)

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. Tech. 40, 915-920. crossref(new window)

Ramirez, J. A., Velazquez, G., Echevarria, G. L., and Torres, J. A. (2007) Effect of adding insoluble solids from surimi wash water on the functional and mechanical properties of pacific whiting grade A surimi. Biores. Tech. 98, 2148-2153. crossref(new window)

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. crossref(new window)

Ruiz-Carrascal, J. and Regenstein, J. (2002) Emulsion stability and water uptake ability of chicken breast muscle proteins as affected by microbial transglutaminase. J. Food Sci. 67, 734-739. crossref(new window)

Tadpitchayangkoon, P., Park, J. W., and Yongsawatdigul, J. (2010) Conformational changes and dynamic rheological properties of fish sarcoplasmic proteins treated at various pHs. Food Chem. 121, 1046-1052. crossref(new window)

Uresti, R. M., Téllez-Luis, S. J., Ramirez, J. A., and Vazquez, M. (2004) Use of dairy proteins and microbial transglutaminase to obtain low-salt fish products from filleting waste from silver carp (Hypophthalmichthys molitrix). Food Chem. 86, 257-262. crossref(new window)

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

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. crossref(new window)