The Influence of Heating and Cooling Process on the Water Binding in Transglutaminase-Modified Chicken Protein Preparation, Assessed Using Low-Field NMR
作者： Jerzy Stangierski , Hanna Maria Baranowska
DOI: 10.1007/S11947-015-1618-5
关键词: Microbial transglutaminase 、 Water binding 、 Chromatography 、 Activation energy 、 Atmospheric temperature range 、 Myofibril 、 Tissue transglutaminase 、 Chemistry 、 Relaxation (NMR) 、 Enzyme
摘要: The study analysed mechanically deboned chicken meat subjected to washing and separation of fat connective tissue in order produce a preparation myofibrillar proteins (MP). was modified using microbial transglutaminase (MTG). For this purpose, MP supplemented with 3 g/kg MTG at 6–7 °C for 5 h. Changes the dynamics water binding, which occurred course heating cooling within temperature range 20–70–20 °C, were tested systems. Relaxation times T1 T2 determined low-field nuclear magnetic resonance (NMR). Enzymatic modification resulted significant changes bulk binding protein Due presence preparation, begin end lower temperatures. Analysis relaxation time showed that addition enzyme causes sample up 48 h after gel cooling. reduces energy barrier determined, based on activation energy.
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HANNA M. BARANOWSKA, MAREK SIKORA, MAGDALENA KRYSTYJAN, PIOTR TOMASIK, Analysis of the formation of starch - hydrocolloid binary gels and their structure based on the relaxation times of the water molecules Polimery. ,vol. 56, pp. 478- 483 ,(2011) , 10.14314/POLIMERY.2011.478
S.F. WANG, D.M. SMITH, J.F. STEFFE, Effect of pH on the Dynamic Rheological Properties of Chicken Breast Salt-Soluble Proteins During Heat-Induced Gelation Poultry Science. ,vol. 69, pp. 2220- 2227 ,(1990) , 10.3382/PS.0692220
William Renzo Cortez-Vega, Gustavo Graciano Fonseca, Carlos Prentice, Optimization of parameters for obtaining surimi-like material from mechanically separated chicken meat using response surface methodology Journal of Food Science and Technology-mysore. ,vol. 52, pp. 763- 772 ,(2015) , 10.1007/S13197-013-1056-1
Jerzy Stangierski, Jan Zabielski, Bożena Grześ, Modification of functional quality of raw myofibril preparation obtained from water-washed mechanically recovered chicken meat European Food Research and Technology. ,vol. 236, pp. 449- 458 ,(2013) , 10.1007/S00217-012-1905-6
H. Y. Carr, E. M. Purcell, Effects of Diffusion on Free Precession in Nuclear Magnetic Resonance Experiments Physical Review. ,vol. 94, pp. 630- 638 ,(1954) , 10.1103/PHYSREV.94.630
J. Stangierski, J. Kijowski, Optimization of conditions for myofibril preparation from mechanically recovered chicken meat. Nahrung-food. ,vol. 44, pp. 333- 338 ,(2000) , 10.1002/1521-3803(20001001)44:5<333::AID-FOOD333>3.0.CO;2-G
Anne B. Smyth, Denise M. Smith, Virginia Vega-Warner, Eileen O'Neill, Thermal denaturation and aggregation of chicken breast muscle myosin and subfragments Journal of Agricultural and Food Chemistry. ,vol. 44, pp. 1005- 1010 ,(1996) , 10.1021/JF950581P
Samira Kazemi, Michael O. Ngadi, Claude Gariépy, Protein Denaturation in Pork Longissimus Muscle of Different Quality Groups Food and Bioprocess Technology. ,vol. 4, pp. 102- 106 ,(2011) , 10.1007/S11947-009-0201-3
Joachim Goetz, Peter Koehler, Study of the thermal denaturation of selected proteins of whey and egg by low resolution NMR Lwt - Food Science and Technology. ,vol. 38, pp. 501- 512 ,(2005) , 10.1016/J.LWT.2004.07.009
C.-T. Li, Myofibrillar protein extracts from spent hen meat to improve whole muscle processed meats. Meat Science. ,vol. 72, pp. 581- 583 ,(2006) , 10.1016/J.MEATSCI.2005.08.008