Preparation of Monomeric Myosin from Alaska Pollack Frozen Surimi

Kimura, Ikuo; Takahashi, Michi; Nagahisa, Eizo; Fujita, Takao

doi:10.2331/suisan.48.251

Cited by 8 publications

(4 citation statements)

References 4 publications

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“…A direct answer could be obtained by studying the thermal inactivation of the reconstituted hybrid actomyosin preparations using myosin and actin from carp and walleye pollack. Preparative methods of walleye pollack myosin 22 or S‐1 23 has been established, however, they require an addition of a high concentration of sorbitol or sodium glutamate to prevent their denaturation during the preparation and storage because of its low stability. We did not employ the method because we did not like to consider the side‐effects of these additives.…”

Section: Resultsmentioning

confidence: 99%

Species-specific thermal denaturation pattern of fish myosin when heated as myofibrils as studied by myosin subfragment-1 and rod denaturation rates

et al. 2005

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Thermal denaturation of myofibrils from various species of fish was investigated by measuring ATPase inactivation, myosin aggregation, myosin subfragment-1 (S-1) and rod denaturation rates as studied by chymotryptic digestion. Decrease in monomeric myosin (myosin aggregation) was always faster than the ATPase inactivation for all myofibrils tested. The relative denaturation rate of rod to that of S-1 differed from species to species. Preceded denaturation of rod was observed with some species, and the opposite was true with other species. The denaturation pattern was explained by the different magnitude of S-1 stabilization by F-actin in myofibrils at low salt medium. Myofibrils which receive a great stabilization by F-actin as studied by ATPase inactivation showed the preceded rod denaturation pattern, and vice versa. S-1 portion, not F-actin, determined the different stabilization of S-1 by F-actin in myofibrils.

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Section: Resultsmentioning

confidence: 99%

Species-specific thermal denaturation pattern of fish myosin when heated as myofibrils as studied by myosin subfragment-1 and rod denaturation rates

et al. 2005

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“…Sugars are the prominent compounds used for the prevention of thermal and freeze denaturation of myosin [1][2][3][4]. Some amino acids and organic acids are well known to have an ability to suppress myosin denaturation [5][6][7][8][9]. In addition to organic compounds, sulfate ions have a striking suppressive effect on myosin denaturation [10].…”

Section: Introductionmentioning

confidence: 99%

Suppressing effect of neocarrabiose 4-O-sulfate on thermal and freeze denaturation of myosin subfragment-1 and myofibrils

et al. 2009

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Suppressive effects of neocarrabiose 4-O-sulfate on the thermal and freeze denaturation of myosin subfragment-1 (S-1) and on myofibrils were investigated. The compound strongly suppressed the thermal denaturation of S-1. Its suppressive effect was greater than that of sorbitol and similar to that of maltose. However, it tended to accelerate the denaturation of myofibrils, suggesting a loss of protection by F-actin upon its addition. The compound suppressed the freeze denaturation of myofibrils and S-1. The effect was similar to that of sorbitol or maltose, and completely different from that of Na-sulfate. The compound solubilized myofibrils at concentrations similar to KCl. Therefore, it was concluded that neocarrabiose 4-O-sulfate behaved as an ionic salt in the thermal treatment process, whereas it behaved as a sugar in the frozen storage process.

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“…As myosin denaturation leads to deterioration in the quality of the muscle‐based product, many efforts have been devoted to protect myosin from denaturation during storage. Sugars, sugar alcohols, some Na‐salts of organic acids, and amino acids exhibit a suppressive effect on myosin denaturation caused by heating, freezing, or freeze‐drying 3–11 . Ooizumi et al 8,9 extensively studied the quantitative protective effect of these compounds using thermal inactivation of myofibril Ca 2+ ‐ATPase as an index.…”

Section: Introductionmentioning

confidence: 99%

“…Sugars, sugar alcohols, some Na-salts of organic acids, and amino acids exhibit a suppressive effect on myosin denaturation caused by heating, freezing, or freezedrying. [3][4][5][6][7][8][9][10][11] Ooizumi et al 8,9 extensively studied the quantitative protective effect of these compounds using thermal inactivation of myofibril Ca 2 + -ATPase as an index. They found a linear relationship between the logarithm of ATPase inactivation rates and combined concentrations for all compounds examined except Na-glutamate.…”

Section: Introductionmentioning

confidence: 99%

Stabilization of myosin by ionic compounds as affected by F-actin

Hayashi

Konno

2006

Fisheries Sci

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Suppressive effects of non-ionic (sorbitol, maltose, and trehalose) and ionic (Naglutamate, Na-acetate, Na-sulfate, and ammonium sulfate) compounds on the thermal inactivation of myosin subframgent-1 (S-1) and myofibril Ca 2 + -ATPase were compared. All compounds suppressed S-1 denaturation. When myofibrils were used (at 0.1 M KCl), sugars and sugar alcohol (non-ionic compounds) suppressed denaturation similar to S-1, while Na-glutamate, Na-acetate, and Na-sulfate weakly suppressed them. Ammonium sulfate accelerated denaturation, but suppressed denaturation when heated in 2 M KCl, at which myosin lost protection by F-actin. It was thus concluded that ionic compounds affected the denaturation of myofibrils in two ways; suppression as established with S-1, and acceleration as a result of loss of protection by F-actin caused by increase in ionic strength.

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Preparation of Monomeric Myosin from Alaska Pollack Frozen Surimi

Cited by 8 publications

References 4 publications

Species-specific thermal denaturation pattern of fish myosin when heated as myofibrils as studied by myosin subfragment-1 and rod denaturation rates

Species-specific thermal denaturation pattern of fish myosin when heated as myofibrils as studied by myosin subfragment-1 and rod denaturation rates

Suppressing effect of neocarrabiose 4-O-sulfate on thermal and freeze denaturation of myosin subfragment-1 and myofibrils

Stabilization of myosin by ionic compounds as affected by F-actin

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