Molecular Properties of Post‐Mortem Muscle. 6. Effect of Temperature on Protein Solubility of Rabbit and Bovine Muscle

Chaudhry, H. M.; Parrish, F. C.; Goll, Darrel E.

doi:10.1111/j.1365-2621.1969.tb00915.x

Cited by 34 publications

(8 citation statements)

References 22 publications

(17 reference statements)

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“…Note that the pre-gelling protein solutions of all 3 muscles had the same "apparent viscosity" (calculated from G' and G", results not shown), which partially supported early findings by Chaudhry et al (1969). They reported no difference in viscosity of myofibrillar extracts between cold-shortened (WC) and control (16°C) muscles.…”

Section: Resultssupporting

confidence: 86%

Functional Properties of Myofibrillar Proteins from Cold‐Shortened and Thaw‐Rigor Bovine Muscles

Xiong

Blanchard

1993

Journal of Food Science

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Prcrigor bovine sternomandibularis muscles were stored at 15, 0 and -29°C to examine cold-shortening and thaw-rigor effects on myofibrillar protein extractability and gelation properties of myofibrils and salt-soluble protein (SSP). Frozen muscle that underwent severe contraction at thawing showed greater protein extractability (35%) than muscles stored at 0 and 15°C (27% extractability). Of the three tempered muscles, thaw-rigor muscle produced the strongest myofibril gel and cold-shortened muscle formed the most elastic SSP gel as determined by dynamic shear and penetration measurements. However, thermally induced changes in gel viscoelastic moduli for all protein samples followed similar patterns. Results indicated that physicochemical changes accompanying muscle contraction affected protein network formation during gelation.

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Section: Resultssupporting

confidence: 86%

Functional Properties of Myofibrillar Proteins from Cold‐Shortened and Thaw‐Rigor Bovine Muscles

Xiong

Blanchard

1993

Journal of Food Science

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“…Relative protein solubility was determined (Chaudhry et al, 1969;Boles et al, 1992) on fresh longissimus and semitendinosus samples aged 5 d postmortem at 4°C. All extraction, incubation, and centrifugation took place at 4°C.…”

Section: Protein Solubilitymentioning

confidence: 99%

Selection for lean growth efficiency in Duroc pigs influences pork quality.

Lonergan

Huff-Lonergan

Rowe

et al. 2001

Journal of Animal Science

200

127

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A unique line of Duroc pigs was established by intensive selection for increased lean growth efficiency. The objective of this study was to determine the influence of this selection strategy on fresh pork quality traits. Two lines of Duroc pigs originating from the same foundation herd were evaluated. One line was selected for lean growth efficiency over five generations (Select line), and the other was a contemporary line maintained from the foundation herd (Control line). All pigs in the trial tested negative for the halothane gene. Selection for lean growth efficiency resulted in improved lean gain, carcass lean, increased loin eye area, and less overall carcass fat. The Select line had significantly lower subjective firmness scores in longissimus and significantly greater amounts of moisture and protein lost as measurable drip in longissimus, semimembranosus, and semitendinosus. There were no differences in subjective color scores or in Hunter L, a, and b values between lines. No selection line differences were observed in glycolytic potential or ultimate pH. The longissimus and the semitendinosus exhibited significantly lower early postmortem pH values in Select line pigs. WarnerBratzler shear values were higher for Select line longissimus chops. Degradation of troponin-T was decreased in the Select line longissimus samples. This result suggests that reduced degradation of myofibrillar proteins may be associated with increased moisture and protein lost during storage. This research points out that elimination of the halothane gene will solve some but not all of the genetically influenced pork quality problems faced by the industry. The Select line of pigs appears to be more prone to producing pork that is soft and exudative, indicating a link between soft and exudative pork and some genetic selection strategies may exist. Therefore, it appears that selection for some economically important traits, such as feed efficiency or increased lean growth in the absence of the halothane gene, may compromise pork quality. ABSTRACT: A unique line of Duroc pigs was established by intensive selection for increased lean growth efficiency. The objective of this study was to determine the influence of this selection strategy on fresh pork quality traits. Two lines of Duroc pigs originating from the same foundation herd were evaluated. One line was selected for lean growth efficiency over five generations (Select line), and the other was a contemporary line maintained from the foundation herd (Control line). All pigs in the trial tested negative for the halothane gene. Selection for lean growth efficiency resulted in improved lean gain, carcass lean, increased loin eye area, and less overall carcass fat. The Select line had significantly lower subjective firmness scores in longissimus and significantly greater amounts of moisture and protein lost as measurable drip in longissimus, semimembranosus, and semitendinosus. There were no differences in subjective color scores or in Hunter L, a, and b values between lines. N...

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“…A similar situation was encountered by Chaudhry et al (1969) when extracting rabbit and bovine muscle sarcoplasm. For samples stored at 2"C, variation in amount of protein extractable in dilute buffer was considerable.…”

Section: Sarcoplasmic Extracts From Differing Musclesmentioning

confidence: 55%

Effect of Heating Temperature and Muscle Type on Porcine Muscle Extracts as Determined by Reverse Phase High Performance Liquid Chromatography

McCormick¹,

Kropf²,

Reeck³

et al. 1987

Journal of Food Science

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Samples from porcine longissimus muscles were heated to temperatures ranging from 4080°C to reach endpoint temperatures (0 min) or held at endpoint temperature for 30 min. Proteins in water-soluble extracts of these samples were separated and quantified by reverse phase high performance liquid chromatography (RP-HPLC). After heating to 60°C for 0 min or to 55°C and holding for 30 min, lactate dehydrogenase (LDH), pyruvate kinase (PK) and myoglobin appeared to comprise the bulk of the remaining soluble protein. RP-HPLC analysis of water soluble extracts from longissimus dorsi, serratus ventralis and psoas major muscles from barrows and sows indicated differences in proportions of LDH and myoglobin.

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Molecular Properties of Post‐Mortem Muscle. 6. Effect of Temperature on Protein Solubility of Rabbit and Bovine Muscle

Cited by 34 publications

References 22 publications

Functional Properties of Myofibrillar Proteins from Cold‐Shortened and Thaw‐Rigor Bovine Muscles

Functional Properties of Myofibrillar Proteins from Cold‐Shortened and Thaw‐Rigor Bovine Muscles

Selection for lean growth efficiency in Duroc pigs influences pork quality.

Effect of Heating Temperature and Muscle Type on Porcine Muscle Extracts as Determined by Reverse Phase High Performance Liquid Chromatography

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