The influence of pH and temperature on the properties of myosin

Penny, I. F.

doi:10.1042/bj1040609

Cited by 65 publications

(28 citation statements)

References 12 publications

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“…One of the earliest events is the loss of ATPase activity (Oullet et a/ 1952;Yasui et a1 1960;Takahashi et a1 1962;Penny 1967). Since the rate of inactivation and rate of aggregation are, at least under some conditions, comparable, it has been suggested they have a common cause (Connell 1960;Penny 1967). By extrapolation of Penny's (1967) results to pH 6.5, the pH used in our experiments, about half the ATPase activity would have been lost in 30min at about 36°C.…”

Section: Head-head Aggregationmentioning

confidence: 79%

“…Since the rate of inactivation and rate of aggregation are, at least under some conditions, comparable, it has been suggested they have a common cause (Connell 1960;Penny 1967). By extrapolation of Penny's (1967) results to pH 6.5, the pH used in our experiments, about half the ATPase activity would have been lost in 30min at about 36°C. Under these conditions we did indeed observe significant aggregation.…”

Section: Head-head Aggregationmentioning

confidence: 83%

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The mechanism of formation of gels from myosin molecules

Sharp¹,

Offer

1992

J Sci Food Agric

103

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Heat-set myosin gels form the basis of the adhesive that binds particles of meat together in meat products. The manner in which a gel network is formed from myosin has been investigated by studying the aggregates produced when dilute solutions of rabbit skeletal myosin molecules in 0.6 M KC1, 20 mM potassium phosphate, pH 6.5, were heated at a single temperature between 30 and 60°C. The aggregates have been examined by transmission electron microscopy after either negative staining or rotary shadowing.After heating at 30°C for 30 min, no change in structure is detected. After heating at 35°C for 30 min, the two heads of some myosin molecules coalesce and some dimers are formed by aggregation through the heads. After heating at 40°C for 30 min, up to about 13 myosin molecules aggregate through their heads to form a globular mass up to 60 nm across with the tails radiating outwards. At higher temperatures such head-linked oligomers aggregate further. At 48°C oligomers coexist with aggregates formed by the coalescence of two or more oligomers. In such aggregates the globular masses are in close proximity and tails radiate from them. After heating myosin at 50"C, aggregates are formed by the coalescence of more oligomers and the tails are seen only indistinctly. At 60°C the particles formed contain a large number of globular masses and are typically 100 to 200 nm across, occasionally up to 1 pm. It is possible that the globules making up the strands of the gel networks in scanning electron micrographs are composed of similar particles. It is suggested that these globules are formed by head-head interactions but that tail-tail interactions may be important in forming the strands and cross-links of the gel network.When a heat-set myosin gel is compacted by centrifugation, the supernate contains essentially all the LCI and LC3 light chains of the parent molecule but only a small fraction of the LC2 light chains. We suppose that dissociation of the LCl and LC3 chains from the heads creates hydrophobic patches which cause intramolecular and intermolecular head association.

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Section: Head-head Aggregationmentioning

confidence: 79%

Section: Head-head Aggregationmentioning

confidence: 83%

The mechanism of formation of gels from myosin molecules

Sharp¹,

Offer

1992

J Sci Food Agric

103

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“…(2) The reduced solubility of the sarcoplasmic proteins in pork (Sayre and Briskey 1963), in lamb and in beef (Hunt and Hedrick 1977b). (3) The reduced activity of myofibrillar ATPase in rabbit (Penny 1967a(Penny , 1967b, in pork (Greaser et al 1969) and in lamb muscle , and of myosin ATPase activity in rabbit muscle (Penny 1967a(Penny , 1967b. (4) The reduced activity of some sarcoplasmic proteins (Fischer et al 1979).…”

Section: Impacts Of Accelerated Glycolysis At a Higher Than Normal Tementioning

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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“…Shimizu and Kaguri (1986) reported that probable reason for lowering gelling potential is the denaturation of myofibrillar proteins occuring more rapidly in acidic condition of pH 6.0 or less. Many workers agree that pH is the most important factor associated with changes in meat texture (Kramer and Peters, 1981), water holding capacity (Penny, 1967(Penny, , 1969Konagaya and Konagaya, 1979) and myofibrillar solubility (Konagaya and Konagaya, 1978). The findings of the present study also reveals that low pH of the raw fish muscle has direct impact on the quality of gel which is in full agrement with the observation as reported by the aforesaid authors.…”

Section: Resultsmentioning

confidence: 99%

Investigation on the Gel Forming Ability of Some Under-utilized Marine Fish and Shell Fish 6pecies of Bay of Bengal

Ahmed¹,

Kamal²,

Islam³

et al. 2000

Pakistan J. of Biological Sciences

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Abstract:Eighteen under-utilized marine fish and shell fish species were studied for their gel forming ability and surimi was prepared from all of the fish species. Difference in proximate composition and muscle pH of raw fish and the surimi products were also studied. Four species, namely, T. thalassinus. S. sihama, L. savala and C. macrolepidotus were found with extremely elastic gel forming ability (AA) and among others eight species were with moderately elastic gel (A). Two species, C. guttatum and M. cordyla were found with very poor gelling quality. Relation between muscle pH and water retention with the gelling quality of the fish has also studied.

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The influence of pH and temperature on the properties of myosin

Cited by 65 publications

References 12 publications

The mechanism of formation of gels from myosin molecules

The mechanism of formation of gels from myosin molecules

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

Investigation on the Gel Forming Ability of Some Under-utilized Marine Fish and Shell Fish 6pecies of Bay of Bengal

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