J. Agric. Food Chem., 54 (5), 1740 -1746, 2006. 10.1021/jf0514726 S0021-8561(05)01472-X
Web Release Date: February 7, 2006

Copyright © 2006 American Chemical Society

Heat-Induced Changes in Myofibrillar Protein Structures and Myowater of Two Pork Qualities. A Combined FT-IR Spectroscopy and Low-Field NMR Relaxometry Study

Hanne Christine Bertram,* Achim Kohler, Ulrike Böcker, Ragni Ofstad, and Henrik J. Andersen

Department of Food Science, Danish Institute of Agricultural Sciences, Research Centre Foulum, P.O. Box 50, DK-8830 Tjele, Denmark, and MATFORSK, Norwegian Food Research Institute, Osloveien 1, N-1430 Ås, Norway

Received for review June 22, 2005. Revised manuscript received December 1, 2005. Accepted December 8, 2005. We thank The Danish Ministry of Food, Agriculture and Fisheries for funding the project entitled "Characterisation of technological and sensory quality in foods", the Danish Research Council SJVF for funding the project "Characterization of basic NMR properties in perimortal muscles and meat in relation to physical and metabolic changes", and the Norwegian research council, who supported this study through Grant No. 15338/140.

Abstract:

Low-field NMR T2 and Fourier transform infrared (FT-IR) measurements were performed on meat samples of two qualities (normal and high ultimate pH) during cooking from 28 C to 81 C. Pronounced changes in both T2 relaxation data and FT-IR spectroscopic data were observed during cooking, revealing severe changes in the water properties and structural organization of proteins. The FT-IR data revealed major changes in bands in the amide I region (1700-1600 cm-1), and a tentative assignment of these is discussed. Distributed NMR T2 relaxation data and FT-IR spectra were compared by partial least-squares regression. This revealed a correlation between the FT-IR peaks reflecting -sheet and -helix structures and the NMR relaxation populations reflecting hydration water (T2B ~ 0-10 ms), myofibrillar water (T21 ~ 35-50 ms), and also expelled "bulk" water (T2 relaxation times >1000 ms). Accordingly, the present study demonstrates that definite structural changes in proteins during cooking of meat are associated with simultaneous alterations in the chemical-physical properties of the water within the meat.

Keywords: Water distribution; muscle; protein denaturation; cooking; multivariate data analysis


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