1998
DOI: 10.1111/j.1365-2621.1998.tb17895.x
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Discoloration of Fresh Pork as Related to Muscle and Display Conditions

Abstract: Pale, soft, exudative (PSE), normal, and dark, firm, dry (DFD) pork was held 7 days at 4°C under light or dark then color was evaluated instrumentally and visually. Change in reflectance (R630-R580) was used to estimate color changes due to oxymyoglobin. PSE pork was lighter (high L*) than normal and DFD pork, but did not change over time. An increase in a* and R630-R580 occurred the first day for normal and DFD, but not for PSE samples. A subsequent increase in hue angle and decrease in R630-R580 (loss of red… Show more

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Cited by 95 publications
(39 citation statements)
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“…In PSE meats, the pH decreases rapidly during the first hours after slaughter while temperature is still high, resulting in excessive protein denaturation (Offer and Knight, 1988), so the water-holding capacity is decreased , light scattering is increased and L* coordinate is increased . On the other hand, DFD meats present an L* coordinate similar to RFN meats during the 24 hours after slaughter as it was reported by Zhu and Brewer (1998). Above 24 hours postmortem, RFN meats present higher L* coordinate than DFD meats, which remains almost constant and lower.…”
Section: Colour Evolution During Ageingsupporting
confidence: 63%
“…In PSE meats, the pH decreases rapidly during the first hours after slaughter while temperature is still high, resulting in excessive protein denaturation (Offer and Knight, 1988), so the water-holding capacity is decreased , light scattering is increased and L* coordinate is increased . On the other hand, DFD meats present an L* coordinate similar to RFN meats during the 24 hours after slaughter as it was reported by Zhu and Brewer (1998). Above 24 hours postmortem, RFN meats present higher L* coordinate than DFD meats, which remains almost constant and lower.…”
Section: Colour Evolution During Ageingsupporting
confidence: 63%
“…With increasing storage time, the peak intensity increase of two broad bands near at 485 and 635 nm and the peak intensity reduction of the broad band around 560 nm are clearly observed. In the present study, the carcasses were well-bled and thus myoglobin is the primary heme pigmentation responsible for the color of meats (Fennema, 1996;Francis & Clydesdale, 1975;Kinsman et al, 1994;Lawrie, 1985;Price & Schweigert, 1987;Zhu & Brewer, 1998). Spectral intensity variations of the peaks at 485, 560, and 635 nm likely indicate a dynamic conversion and decomposition for a number of myoglobin derivatives.…”
Section: Visible Spectra Of Cold Stored Chicken Meatsmentioning
confidence: 99%
“…deoxymyoglobin (DeoxyMb), metmyoglobin (MetMb), and oxymyoglobin (OxyMb; Fennema, 1996;Francis & Clydesdale, 1975;Kinsman, Kotula, & Breidenstein, 1994;Lawrie, 1985;Price & Schweigert, 1987;Zhu & Brewer, 1998). During external processes such as cooking, storage, and irradiation, the three forms of myoglobin interconvert and are degraded through oxygenation, oxidation and reduction reactions, ultimately influencing the appearance of meat color.…”
Section: Introductionmentioning
confidence: 99%
“…Ledward (1992) reported that vacuum-aged meat blooms more rapidly than fresh meat when exposed to air, and the rapid bloom development was due to reductions in the activity of oxygen-utilizing enzymes (Ledward, 1992) and oxygen consumption rates (Zhu and Brewer, 1998). Conversely, McKenna et al (2005) reported that resistance to induced MMb formation, nitric oxide MMb reducing ability, and oxygen consumption rate were similar among beef LT, SM, and TB, but beef TB, especially the long head, had greater myoglobin concentrations than either the LT or SM, which may explain some of the observed discrepancies in bloom patterns between TB and SM steaks in the current study.…”
Section: Asymptotic Values For Color Development Curvesmentioning
confidence: 99%