Relationship Between Thermal Denaturation of Porcine Muscle Proteins and Water‐holding Capacity

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.

Effects of l-Arginine on water holding capacity and texture of heat-induced gel of salt-soluble proteins from breast muscle

“…This was basically in agreement with the previous finding (Sun et al, 2012). 52.08 C transition may be attributed to myosin head, the 61.46 C transition can be ascribed to myosin tail and/or sarcoplasmic proteins, and the 73.46 C transition may be related to actin (Deng et al, 2002;Sun et al, 2012).…”

Application of an ultrasonic assisted curing technique for improving the diffusion of sodium chloride in porcine meat

“…Increased interfilament space permits the water uptake of the muscle, thus causing improved tenderness. Water absorption, however, is limited by the denaturation of proteins (Deng et al, 2002;Hullberg and Lundström, 2004). In general, the distance between filaments increased with both treatment time and ultrasonic intensity.…”

Protein Denaturation in Pork Longissimus Muscle of Different Quality Groups

“…Thermal Transitions and Enthalpy of Denaturation Zhu et al 2004;Deng et al 2002). Total denaturation enthalpy (ΔH total ) of the RFN samples was 3.91±0.44 J/g (mean ± SD).…”

“…Therefore, assessing the level of protein denaturation in pork could indicate some underlying mechanisms for the difference in color, texture, and exudation among some of the quality groups including PFN. Differential scanning calorimetry (DSC) is by far the most common and widely used method to study thermal transitions and protein denaturation of muscle tissues (Deng et al 2002;Fernandez-Martin et al 2000;Zhu et al 2004;Brunton et al 2006;Tironi et al 2009). Myosin, which constitutes about 43% of the myofibrillar (contractile) proteins in the muscle tissue (Keeton and Eddy 2004), is the least heatstable protein and generally denatures in the temperature range of 40-60°C (Brunton et al 2006;Li et al 2009).…”