Relationship Between Contractility and Some Biochemical Properties of Myofibrils Prepared From Normal and Pse Porcine Muscle

Sung, Sam Kyung; Ito, Tetsuhide; Fukazawa, Toshiyuki

doi:10.1111/j.1365-2621.1976.tb01112.x

Cited by 18 publications

(5 citation statements)

References 19 publications

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“…Hypoxanthine of the sample with citric acid was lowest and its inosine content was the highest. This aspect might be caused by the initial pH in the early period of fermentation which may have inactivated the enzymatic activity resulting in inosine levels of the sample with citric acid being higher than that of the other treatments (Sung et al, 1976). Depletion of ATP in muscle is due to postmortem time, but the results are not in agreement with the changes expected.…”

Section: Resultsmentioning

confidence: 76%

Efficiency of Hurdle Technology Applied to Raw Cured Meat (Si-Raw) Processing

Chen¹,

Lin²,

Tsai³

et al. 2002

Asian Australas. J. Anim. Sci

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Si-Raw is a raw cured meat (raw, cured meat fermented with steamed rice) produced by the aboriginal people of Taiwan. In order to prevent food poisoning or intoxication from botulism, new methods of monitoring the production base on hurdle technology were investigated. New methods investigated incorporated citric acid, sodium hypophosphite, Monascus anka mash, plum paste or lactic acid bacteria inoculum added separately to meat with steamed rice and salt to lower the Aw (water activity) and pH values of the products to control the microbial growth. Results showed that anaerobic bacterial counts, lactic acid bacterial counts and aerobic bacterial counts for the products of all treatments were less than 10 6 , 10 5 and 10 2 cfu/g, respectively. Sodium chloride content of all products was above 5.46%, water activity was below 0.939 and pH value was below 4.27. IMP was lower and ATP and hypoxanthine were higher. ATP concentrations were higher in the samples which contained the anka mash. Result of sensory panel test indicated that most people preferred the products with added sodium hypophosphite. Except for the fact that the content of tryptamine in the sample with Monascus anka mash was higher, the amine concentrations for all treatments were lower than those of other fermented meat products. The amino acid nitrogen content was higher in the product made from raw meat treated with citric acid, but lower in the other products. Neither Clostridium botulinum nor Trichinella spiralis were detected in any of the treatments. The result may indicate that hurdle technology is effective for hygiene and safe producing Si-Raw.

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Section: Resultsmentioning

confidence: 76%

Efficiency of Hurdle Technology Applied to Raw Cured Meat (Si-Raw) Processing

Chen¹,

Lin²,

Tsai³

et al. 2002

Asian Australas. J. Anim. Sci

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“…Extractability of Myofibrillar Proteins from Myofibrils. Extractability of myofibrillar proteins from myofibrils was essentially carried out according to the method described by Sung et al (1976). Myofibrillar proteins were extracted from myofibrils for 15 min at 5 °C with the following solutions: (1) Hasselbach-Schneider solution (0.6 M KC1, 10 mM sodium pyrophosphate, 0.1 M potassium phosphate, and 1 mM MgCl2, pH 6.4) and…”

Section: Methodsmentioning

confidence: 99%

Change in the properties of myofibrillar proteins during post-mortem storage of muscle at high temperature

Ikeuchi¹,

Ito²,

Fukazawa³

1980

J. Agric. Food Chem.

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Changes in the properties of myofibrillar proteins prepared from muscles stored at 37 °C for varying periods of time were investigated. The extractability of myofibrillar proteins did not change during the first 2 h after death but decreased during 2-6 h, while the pH value of longissimus muscle decreased rapidly to 6.5 after 2 h and to 5.6 after 4 h. The degradation of myofibrillar proteins, especially myosin and troponin, occurred during storage. Myofibrillar ATPase activities in the presence of calcium ions were decreased, while in the absence of calcium ions the activities gradually increased, resulting in a decrease in Ca2+ sensitivity of myofibrils during storage. The enzymatic activities of myosin and the affinity of actin for myosin were decreased with increasing storage time. The polymerization rate of actin was increased at first and then decreased with increasing storage time, but the molecular weight of actin and its ability to activate myosin ATPase activity changed little during 12 h of post-mortem storage at 37 °C.Post-mortem changes in muscle are effected by genetic, physiological, and nutritional conditions of live animals and post-mortem conditioning (Cassens et al., 1975;Cassens, 1977). Bendall (1973) has precisely described physical and chemical changes which take place during the rigor process under various conditions. There are many extensive studies regarding the changes in myofibrillar proteins under the various post-mortem storage conditions, especially in relation to storage temperature, pH, and time, and a significant correlation between storage conditions of muscle after death and the properties of myofibrillar proteins has been established (Wolfe and Samejima and Yamamoto et al., 1977; Parrish, 1978,1979). Also, it has been well-known that myofibrillar proteins undergo the following specific changes during post-mortem storage: (1) alteration of the actin-

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“…Higher transmission value is considered indicative of a greater extent of denatured sarcoplasmic proteins. The contractility ofmyofibrils was measured by the method of Sung et al 14 ) Color measurement. Each of the PSE-like muscles was tightly packed into a grass cell 35 mm in diameter and 12mm in depth and covered with fitted black cap.…”

Section: Extractability Of Sarcoplasmic Proteins and Contractility Ofmentioning

confidence: 99%

“…Four muscles were PSE and intermediate, while the remaining 10 were normal. These judgements were based on the method of Sung et al 14 ) and Hart. 12 ) From the quadratic regression curve obtained by statistical analysis, it was found that decreasing pH24 tended to decrease CFR, and the CFR of extremely PSE porcine muscles were relatively lower (69 '" 71 %) than those of the normal muscles.…”

Section: Extractability Of Sarcoplasmic Proteins and Contractility Ofmentioning

confidence: 99%