Proteome Analysis of the Sarcoplasmic Fraction of Pig Semimembranosus Muscle:  Implications on Meat Color Development

Abstract

Two-dimensional electrophoresis was used to investigate sarcoplasmic protein expression in pig Semimembranosus muscles sampled 20 min after slaughter. Two groups (light and dark) of 12 animals were selected from 1000 pigs, based on meat L values measured 36 h postmortem. Twenty-two proteins or fragments (p < 0.05) were differentially expressed. Muscles leading to darker meat had a more oxidative metabolism, indicated by more abundant mitochondrial enzymes of the respiratory chain, hemoglobin, and chaperone or regulator proteins (HSP27, alphaB-crystallin, and glucose-regulated protein 58 kDa). Conversely, enzymes of glycolysis were overexpressed in the lighter group. Such samples were also characterized by higher levels of glutathione S-transferase omega, which can activate the RyR calcium channels, and higher levels of cyclophilin D. This protein pattern is likely to have severe implications on postmortem metabolism, namely, acceleration of ATP depletion and pH fall and subsequent enhanced protein denaturation, well-known to induce discoloration.

Technological and sensory pork quality in relation to muscle and drip loss protein profiles

“…In the present study, the B chain of hemoglobin was found in the drip loss. Sayd et al [54] found more hemoglobin in meat classified as belonging to the dark group, which is also characterized by increased oxidative metabolism. These authors also suggested that the higher abundance of hemoglobin may be linked to higher blood flow in muscles, higher hemoglobin content in the blood, and/or degree of bleeding.…”

“…The protein identification by mass spectrometry of W12 revealed a mixture of proteins as follows (Table 5): the B or D chain of hemoglobin and fatty acid-binding protein (FABP). Sayd et al [54] reported that FABP may be a marker for a low L* value in meat. However, these authors studied soluble proteins extracted from muscles.…”

Food Proteomics: Mapping Modifications

“…They were able to identify up to eight proteins that appeared to be significantly related to water holding capacity; the most clearly related were creatine phosphokinase Mtype (CPK), desmin and a transcription activator. Another proteomic study provided evidence for pig muscles that were darker in colour having more abundant mitochondrial enzymes of the respiratory chain, haemoglobin and chaperone or regulator proteins (Sayd et al, 2006). Lighter coloured meats, in contrast were found to have more glycolytic enzymes.…”

Efeito da adição de ractopamina e da imunocastração na carne <i>in natura</i> de suínos

“…A degradação proteolítica destas provoca o enfraquecimento das miofibrilas, levando ao amaciamento (TAYLOR et al, 1995;KOOHMARAIE, 1996 O proteoma sarcoplasmático é responsável por aproximadamente um terço do total das proteínas em músculos esqueléticos e compreende proteínas solúveis e enzimas que interagem com mioglobina e tem influência na cor da carne (SCOPES, 1970;JOSEPH et al, 2012;SUMAN et al, 2014a, b A enzima triose fosfato isomerase e sua relação com a maciez da carne foi averiguada por Lametsch et al (2003), que demonstraram que a proteina é um potencial biomarcador para maciez de carne. Laville et al (2007) averiguaram que a triose fosfato isomerase e outras oito proteínas foram super expressas em carne cozida com características de alta dureza quando comparado com carne macia, e pode também ser usada como biomarcador para a cor da carne (JOO et al, 1999 MIRAULT, 1987;ALMGREN;OLSON, 1999;PUOLANNE;ERTBJERG, 2015;SAYD et al, 2006;BERNARD et al, 2007).…”

“…Estudos demonstraram correlação negativa entre a HSP 27 e concentrações αβ-cristalina e maciez da carne, suculência, cor e sabor (SAYD et al, 2006;BERNARD et al, 2007). Outros estudos como os desenvolvidos por…”