Relationship between myosin denaturation and the colour of low-voltage-electrically-stimulated beef

Héctor, D; Brew‐Graves, Chris; Hassen, N.; Ledward, D.A.

doi:10.1016/0309-1740(92)90060-h

Cited by 36 publications

(13 citation statements)

References 5 publications

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“…The L ⁎ value of treatment 2 was significantly (pb 0.05) increased with increasing days of storage, which was not found in other treatments (Table 1). Protein denaturation and/or shrinkage of the myofibrils at higher rigor temperatures tends to increase light scattering giving higher L ⁎ values (Hector et al, 1992;MacDougall, 1982;Offer et al, 1989;Renerre & Bonhomme, 1991). Farouk and Swan (1997) reported that increased lightness may be due to lipid oxidation, which increases muscle protein denaturation leading to more light scattering.…”

Section: Meat Surface Colormentioning

confidence: 95%

“…Oxidation of cherry red oxymyoglobin to brown metmyoglobin results in meat discoloration. Meat color (myoglobin) is determined by the pre-rigor, post-rigor, and storage factors that affect muscle proteins (Hector, Brew-Graves, Hassen, & Ledward, 1992;Ledward, 1985;Offer, Knight, Jeacocke, Almond, & Cousins, 1989;Renerre & Bonhomme, 1991). Factors affecting meat protein include ice crystal formation, dehydration, increased solute concentration, fat hydrolysis and or oxidation, atmospheric gasses (particularly oxygen), protein oxidation and proteolysis, and rigor temperature (Matsumoto, 1979;Shenouda, 1980).…”

Section: Introductionmentioning

confidence: 98%

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Effect of freeze–thaw cycles on physicochemical properties and color stability of beef semimembranosus muscle

Jeong

Kim

Yang

et al. 2011

Food Research International

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Section: Meat Surface Colormentioning

confidence: 95%

Section: Introductionmentioning

confidence: 98%

Effect of freeze–thaw cycles on physicochemical properties and color stability of beef semimembranosus muscle

Jeong

Kim

Yang

et al. 2011

Food Research International

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“…However, processed meat, in which color is not an important quality, can gain other advantages by high-pressure treatment, such as better texture and WHC, even if 300 MPa of pressure with higher temperature and holding time is used. Although the changes in pressurized meat color were evidenced mainly by changes in the redox state and the unfolding of myoglobin (Carlez et al, 1995), the lightness of pork after pressurization was also affected by the denaturation of myofibrillar proteins (Hector et al, 1992). Eventually, the protein stability of pork under selected optimum pressure conditions was estimated by DSC (Fig.…”

Section: Optimizationmentioning

confidence: 99%

Modelization and Optimization of Quality Characteristics of Pork Treated Various Hydrostatic Pressure Conditions

Hong¹,

Chun²,

Lee³

et al. 2012

Korean Journal for Food Science of Animal Resources

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In this study, the effects of physical parameters (30-270 MPa of pressure, 3-57 min of time, and 1-49 o C of temperature) on pork quality were investigated. Response surface methodology was used in order to monitor and model the changes in pork quality under varied pressure conditions. As quality characteristics, shear force, water holding capacity (WHC) and the CIE color of pork were measured, and optimum pressure conditions were evaluated by statistical modeling. Pressure improved the WHC of pork at relatively low temperature (<25 o C); however, the opposite occurred with increasing temperature. Although pressure and temperature affected the tenderness of the meat, interaction effects among variations were not observed. At pressure levels higher than 200 MPa, the color of pork differed markedly from that of the untreated controls. In particular, differential scanning calorimetry (DSC) revealed marked evidence of myosin denaturation. The present study demonstrates that pork quality varies depending on pressure conditions.

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“…Colour: 35 C higher L* value, 25À35 C higher a* and b* values; WHC: 0À10 C similar WHC, 25À35 C lower WHC; ES: no effect on colour and WHC Farouk and Swan 1998 Excised semimembranosus +ES and pre-rigor excised muscle holding at fast and slow chilling for 24 h Colour: higher L* Hector et al 1992 Carcass biceps femoris, semimembranosus, semitendinosus +/ÀES and 15 v. 37 C until rigor Tenderness: 37 C tougher sensory at 15 days, not WBSF Hertzman et al 1993 Carcass longissimus +/ÀES applied to a side within a carcass, achieved high rigor temperature of 41 C (+ES) and 33 C with (-ES)…”

Section: Introductionmentioning

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.

198

104

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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.

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Relationship between myosin denaturation and the colour of low-voltage-electrically-stimulated beef

Cited by 36 publications

References 5 publications

Effect of freeze–thaw cycles on physicochemical properties and color stability of beef semimembranosus muscle

Effect of freeze–thaw cycles on physicochemical properties and color stability of beef semimembranosus muscle

Modelization and Optimization of Quality Characteristics of Pork Treated Various Hydrostatic Pressure Conditions

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

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