Physicochemical changes and mechanism of heat-induced gelation of arrowtooth flounder myosin.
Physicochemical changes of myosin during heating were investigated to elucidate the mechanism of heat-induced gelation of arrowtooth flounder (ATF) myosin at high ionic strength. Changes in dynamic properties indicated ATF myosin formed a gel in three different stages as shown by the first increase in G' (storage modulus) at 28 degrees C, followed by the decrease at 35 degrees C and the second increase at 42 degrees C. DSC thermogram showed the onset of myosin denaturation at 25 degrees C with two maximum transition temperatures at 30 and 36 degrees C. The decrease in alpha-helical content indicated ATF myosin began to unfold at 15 degrees C and the unfolding continued until it reached 65 degrees C. Turbidity measurement showed myosin began to aggregate at 23 degrees C and the aggregation was complete at 40 degrees C. Surface hydrophobicity increased consistently in the temperature range studied, 20-65 degrees C. Sulfhydryl contents decreased significantly at 20-30 degrees C due to the formation of disulfide linkages but remained constant at temperatures >30 degrees C. ATF myosin was shown to be extremely sensitive to heat, resulting in denaturation at lower temperature than other fish myosin. Denaturation was initiated by unfolding of the alpha-helical region in myosin followed by exposure of hydrophobic and sulfhydryl residues, which are subsequently involved in aggregation and gelation processes.
Visessanguan
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Oregon State University Seafood Laboratory, Astoria, Oregon 97103-3427, USA.
Ogawa
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Nakai
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D000818:Animals; D002152:Calorimetry, Differential Scanning; D005432:Flounder; D005782:Gels; D006358:Hot Temperature; D018482:Muscle, Skeletal / Q000737:chemistry*; D009218:Myosins / Q000737:chemistry*; D009994:Osmolar Concentration; D013816:Thermodynamics
D005782:Gels; D009218:Myosins