Myosin denaturation in pale, soft, and exudative (PSE) porcine muscle tissue as studied by differential scanning calorimetry

Stabursvik, Eva; Fretheim, K.; Frøystein, T.

doi:10.1002/jsfa.2740350218

Cited by 91 publications

(45 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…some denaturation took place [51,52]. It appears that the heat sensitive protein components are somewhat more sensitive also to frozen storage than the actin [53][54][55]. CryoprotectanLs such as a sucrose:sorbitol mixture -due to a protein-carbohydrate/polyol interactionretarded the denaturation process during the frozen storage and probably increased somewhat the denaturation temperature during heating, as has been reported also for egg white proteins [39].…”

Section: -85~mentioning

confidence: 55%

Application of differential scanning calorimetry in food research and food quality assurance

Fárkas¹,

Mohácsi-Farkas²

1996

Journal of Thermal Analysis

View full text Add to dashboard Cite

Differential scanning calorimetry (DSC) is the most widely used thermal analytical technique in food research and it has a great utility in quality assurance of food. Proteins are the most studied food components by thermal analysis including studies on conformation changes of food proteins as affected by various environmental factors, thermal denaturation of tissue proteins, food enzymes and enzyme praparations for the food industry, as well as effects of various additives on their thermal properties. Freezing-induced denaturation of food proteins and the effect of cryoprotectants are also monitored by DSC. Polymer characterization based on DSC of polysaccharides, gelatinization behaviour of starches and interaction of starch with other fbod components can be determined, and phase transitions during baking processes can be studied by DSC. Studies on crystallization and melting behaviour of fats observed by DSC indicate changes in lipid composition or help characterizing products. Thermal oxidative decomposition of edible oils examined by DSC can be used for predicting oil stability. Using DSC in the freezing range has a great potential for measuring and modelling frozen food thermal properties, and to estimate the state of water in foods and food ingredients. Research in food microbiology utilizes DSC in better understanding thermoadaptive mechanisms or heat killing of food-borne microorganisms. lsothermic mierocalorimetric techniques provide informative data regarding microbial growth and microbial metabolism.

show abstract

Section: -85~mentioning

confidence: 55%

Application of differential scanning calorimetry in food research and food quality assurance

Fárkas¹,

Mohácsi-Farkas²

1996

Journal of Thermal Analysis

View full text Add to dashboard Cite

show abstract

“…As the ATPase activity of myosin is confined to the head, this suggests that it is the myosin-S1 that is denatured, although Stabursvik et al (1984) suspected that the myosin tail (LMM) could also be involved. Penny (1967a) suggested that in prerigor muscle, myosin (which is bound to actin in the post-rigor myofibril) is more resistant to denaturation by low pH.…”

Section: Myofibrillar Proteins and Myosin Atpase Activitymentioning

confidence: 99%

Influence of high pre-rigor temperature and fast pH fall on muscle proteins and meat quality: a review

Kim

Warner

Rosenvold³

2014

Anim. Prod. Sci.

205

104

View full text Add to dashboard Cite

Abstract. The impacts of accelerated pH decline combined with high muscle temperature on post-mortem muscle metabolism and subsequent meat quality attributes have been extensively studied. Traditionally, this phenomenon has been observed in pork muscles, primarily due to the relatively fast post-mortem glycolysis rate and its relationships to stress susceptibility of pigs before slaughter. However, the protein-denaturing condition of high temperature/rapid pH fall and subsequent PSE (pale, soft and exudative)-like abnormal meat quality characteristics have been observed in muscles from other species such as beef, lamb, venison and even poultry. Various pre-rigor conditions including the application of electrical stimulation, hot-boning, and/or pre-rigor carcass chilling temperatures in various muscles, in conjunction with carcass stretching/hanging methods, can also contribute to muscle-protein denaturation pre-rigor. This review considers the influence of a faster than normal pH fall at a higher than normal pre-rigor temperature on glycolysis, post-mortem muscle proteins and subsequently meat quality attributes. Gaps in current knowledge are identified and recommendations made for additional research.

show abstract

“…Table 2 lists the denaturation temperature of muscle protein fractions obtained in different studies. DSC and DTA are powerful analytical tools commonly employed to study thermodynamics of protein denaturation [20,33,34]. Three major transitions ( Fig.…”

Section: Thermal Analysis Of Meatmentioning

confidence: 99%

“…This method could be applied for solid meat products. With the use of DSC, investigations on thermal properties of meat proteins from pork, fish, and beef were carried out [20,33,34]. Kinetics of protein denaturation was also studied by a few [35,133,134].…”

Section: Thermal Transitions Of Fat Affecting Stability and Qualitymentioning

confidence: 99%

“…Thermal profile of proteins from these muscles will be of great help in avoiding usage of faulty meat. Reduced WHC of PSE meat is primarily due to denaturation of myosin [60] and partly due to the degradation of cytoskeletal proteins [61]. Voutila et al [62] used DSC to determine role of connective tissue in texture of PSE meat in pork muscles.…”

Section: Pse and Dfd Meatmentioning

confidence: 99%

See 1 more Smart Citation

Thermal analysis of meat and meat products

Tamilmani

Pandey

2015

J Therm Anal Calorim

View full text Add to dashboard Cite

The application of thermal analysis to meat products, like all materials, is governed by energy transfer, from which invaluable information on thermodynamics of processes is obtained. Various meat systems have been analyzed with different success ratios. Proteins in meat formed the key area of interest due to their effect on product quality, shelf life, functionality and also their ability to interact with other components. Initially success rates were low owing to lack of sensitivity, results with complex curves, complications in interpretation and a large number of factors affecting the biological system. Later with developments in instrumentation and computer models for better resolution and reproducibility, wider horizons could be covered with easy solutions to complex results. Though thermal analysis has been used exhaustively in meat, research in this area has become stagnant and new areas are being left untouched. This review emphasizes the importance of thermal analysis in the meat industry and also the need to use more advanced equipment for better understanding of the biological changes occurring in muscle during processing and storage.

show abstract

Myosin denaturation in pale, soft, and exudative (PSE) porcine muscle tissue as studied by differential scanning calorimetry

Cited by 91 publications

References 18 publications

Application of differential scanning calorimetry in food research and food quality assurance

Application of differential scanning calorimetry in food research and food quality assurance

Influence of high pre-rigor temperature and fast pH fall on muscle proteins and meat quality: a review

Thermal analysis of meat and meat products

Contact Info

Product

Resources

About