4.7 Article

Effect of pre-rigor temperature incubation on sarcoplasmic protein solubility, calpain activity and meat properties in porcine muscle

Journal

LWT-FOOD SCIENCE AND TECHNOLOGY
Volume 55, Issue 2, Pages 483-489

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.lwt.2013.10.001

Keywords

Early pH decline; Glycogen phosphorylase; Creatine kinase; Water-holding capacity; Sarcoplasmic protein precipitation

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The aim of the study was to investigate the effect of pre-rigor temperature incubation on sarcoplasmic protein characteristics in relation to meat properties within porcine muscle. Porcine Longissimus dorsi muscles were incubated at temperatures of 0, 10, 20, 30 and 40 degrees C to 6 h post mortem. Incubation at 40 degrees C induced a significant decrease of sarcoplasmic protein solubility and an increase in proteins in the myofibrillar fraction. The protein relocation was followed till 72 h post mortem but had largely been completed by the end of the temperature incubation at 6 h. SDS-PAGE and Western blot analyses suggested that phosphorylase and creatine kinase precipitated onto the myofilaments during incubation at 40 degrees C. Drip loss increased following incubation at 40 degrees C, indicating that the precipitation of phosphorylase and creatine kinase may be a factor of reduced water-holding capacity at the combination of high temperature and low pH. Incubation at 40 degrees C resulted in substantially lower shear force in parallel with loss of extractable activity of mu- and m-calpain, suggesting a rapid activation of both enzymes at high temperatures and low pH early post mortem. (C) 2013 Elsevier Ltd. All rights reserved.

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