Abstract

Differential scanning calorimetry was used to investigate denaturation characteristics of pork muscle proteins from carriers and noncarriers of the RN-gene. Pork from RN-carriers deviated from noncarriers in maximum denaturation temperatures and denaturation enthalpy, with proteins of RN-carriers being the most heat-labile. Correlation studies on the results showed that water-holding capacity was significantly correlated to changes in enthalpy of the population mainly representing myosin tails and sarcoplasmic proteins (p < 0.001). Finally, the influence of ultimate pH and preheating on thermal characteristics of porcine muscle proteins was studied. Myosin tails and sarcoplasmic proteins were most sensitive to pH changes, while myosin heads were most sensitive to preheating simulating stress-induced temperature increases.

Keywords

differential scanning calorimetry; muscle; pig; protein denaturation; RN-gene

Published in

Journal of Food Science
2002, Volume: 67, number: 5, pages: 1642-1647
Publisher: INST FOOD TECHNOLOGISTS

UKÄ Subject classification

Food Science


Publication identifier

DOI: https://doi.org/10.1111/j.1365-2621.2002.tb08698.x

Permanent link to this page (URI)

https://res.slu.se/id/publ/85639