Thermal stability of connective tissue from porcine muscles

Voutila, Liisa; Mullen, Anne Maria; Ruusunen, Marita; Troy, Declan J.; Puolanne, Eero

doi:10.1016/j.meatsci.2006.12.012

Cited by 23 publications

(9 citation statements)

References 39 publications

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“…Similar values were also found in the SM by Purchas et al (2009) and Voutila et al (2007). Warner et al (1993), however, found lower L * values 24 h after slaughter in selected leg muscles (ST: 52.6; SM: 46.4; BF: 45.6).…”

Section: Discussionsupporting

confidence: 82%

“…The muscles of the topside had a low proportion of fat (AD 1.7%; SM 3.1%). Voutila et al (2007) found a practically similar proportion of collagen in the SM (0.4%), though a lower content in the LT (0.25-0.31%) compared to the present study (0.51%). A proportion of fat of 2.31% and 2.52% and a total protein content of 22.4% and 23.6% were found in the SM of pigs fattened extensively and intensively in New Zealand (Purchas et al 2009).…”

Section: Discussioncontrasting

confidence: 54%

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Characteristics of selected pork muscles 45 min and 24 h post mortem

2018

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The muscles of the pork topside -musculus adductor (AD) and m. semimembranosus (SM), and of the silverside -m. biceps femoris (BF) and m. semitendinosus (ST) were analysed and their properties compared with the m. longissimus thoracis (LT) and m. supraspinatus (SS) muscles. Colour (CIE L*a*b*), D/L-lactic acid content, and pH values were measured 45 min and 24 h post mortem. The basic chemical composition of muscles was analysed 24 h after slaughtering. A significant correlation (r = -0.61, P < 0.001) was found between the pH values and the level of lactic acid 45 min post mortem, though not 24 h after slaughter (r = -0.25, P > 0.05). The results confirmed that a direct comparison cannot be made between the fall in pH values in meat and the increase in the level of lactic acid. The lightness L * 24 h post mortem was higher (P < 0.05) in AD, BF, ST and LT muscles than those in samples measured 45 min after slaughter. The toughest muscle was biceps femoris, with a mean value of shear force of 90.5 N. The differences in shear force between the individual analysed muscles were significant (P < 0.05). There were significant differences in the intramuscular fat content between the topside and silverside muscles (P < 0.05). The results of the present study are of value to meat producers who might intend to substitute these parts of the leg with one another during the production, particularly in the case of wholemuscle meat products. Lactic acid, pH value, colour, shear force, protein content, intramuscular fatColour, tenderness, and water-binding capacity are considered the most important characteristics of fresh meat (Hughes et al. 2014). England et al. (2015) believe the quality of pork meat to be determined by two basic factors -the speed at which the pH falls in the muscles and the final pH value attained post mortem. Joo et al. (2013) defined three groups of meat traits that are of interest to the consumer -appearance quality traits, eating quality traits, and reliance quality traits. These characteristics are particularly important in the retail during the selection and purchase of meat cuts by consumer. In production, producers prioritise properties that guarantee the uniformity of the products they produce. Colour, or more accurately the balance of colour tone of contiguous muscles (meat) in whole-muscle meat products (and hams in particular), is also important, in addition to the fore-mentioned features such as the water binding capacity and tenderness (McKeith and Pringle 2013).The proportion of fat and, in particular, protein, is also important. The legislation of many countries stipulates limits defining the minimum content of pure muscle protein in selected meat products (DLB 2010) or minimum values for the water : protein ratio (ÖLB 2012). The chemical composition of meat is important in these cases with regard to the balance between the content of total (crude) protein, collagen and fat. The speed and extent of the fall in pH values and the final pH value can, on the other hand, influence the co...

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Section: Discussionsupporting

confidence: 82%

Section: Discussioncontrasting

confidence: 54%

Characteristics of selected pork muscles 45 min and 24 h post mortem

2018

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“…Alternately, denaturation of connective tissue protein which is responsible to the longitudinal shrinkage of muscle accounted for most of the cooking loss of meat, mainly due to shortening of muscle fibers (Tornberg, 2005). It was reported that onset denaturation temperature of porcine connective tissue was 57.2°C–61.4°C in DSC analysis (Voutila et al, 2007) which would explain the increase in cooking loss of pork loin processed at 55°C.…”

Section: Resultsmentioning

confidence: 99%

Effects of Temperature and Time on the Cookery Properties of Sous-vide Processed Pork Loin

Hwang¹,

Lee²,

Hong³

2019

Food Sci Anim Resour

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This study investigated the effects of temperature (50°C, 55°C, and 60°C) and time (12 and 24 h) on the cookery properties of sous-vide (SV) processed pork loin. As an indicator of cookery properties, cooking loss, expressible moisture (EM), pH, differential scanning calorimetry (DSC), shear force, total plate count (TPC) and CIE color were measured and compared with fresh (FC) and cooked control (CC, 75°C for 30 min). SV treatments at 50°C showed higher tenderness and lower cooking loss comparing to CC. DSC result indicated that thermal transition of collagen was a key factor affecting the cooking loss and shear force of meat. In comparison of CC, risks of insufficient pasteurization and uncooked color generation were not shown in SV processed meat. Therefore, the results indicated that SV had a potential advantage to produce tender and moist meat, and the best SV condition of pork loin was estimated at 50°C for 24 h.

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“…With respect to connective tissue, apart from species difference, the amount of perimysium collagen varies among various muscles (Purslow ) and collagen solubility can differ between muscle types (Voutila and others ; Kolczak and others ), animals of different ages (Hill ) and breeds (Christensen and others ). Therefore, variations in sarcoplasmic protein and collagen content, as well as collagen solubility, may play a role in this discrepancy of findings on fiber cross‐section area after cooking.…”

Section: Protein Structure Modifications In Meat As a Results Of Cookingmentioning

confidence: 99%

Cooking‐Induced Protein Modifications in Meat

Morton

Clerens

et al. 2016

Comp Rev Food Sci Food Safe

186

115

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Food ingredients commonly undergo heat treatment. Meat, in particular, is typically consumed after some form of heating, such as boiling or roasting. Heating of meat can introduce a wide range of structural changes in its proteinaceous components. At the 3-dimensional structural level, meat proteins may denature and form aggregates upon heating. At the molecular level, primary structure (amino acid residue) alterations reported in cooked meat include protein carbonylation, modification of aromatic residues, and the formation of Maillard reaction products. Identification of these modifications is essential for determining the mechanism of thermal processing of meat and allowing better control of the nutritional and functional properties of products. This article reviews and summarizes the current state of understanding of protein modifications at the molecular level in commonly consumed mammalian food. In addition, relevant case studies relating to characterization of heat-induced amino acid residue-level modifications in other biological materials such as milk and wool are discussed to provide complementary insights.

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Thermal stability of connective tissue from porcine muscles

Cited by 23 publications

References 39 publications

Characteristics of selected pork muscles 45 min and 24 h post mortem

Characteristics of selected pork muscles 45 min and 24 h post mortem

Effects of Temperature and Time on the Cookery Properties of Sous-vide Processed Pork Loin

Cooking‐Induced Protein Modifications in Meat

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