Journal of Food Science · 1988 · 59 citations · 14 references
Life SciencesBiochemistryBiophysicsCellular BiochemistryEnzymologyFish PhysiologyDisulfide Bond FormationEnzyme CharacterizationEnzyme KineticsEnzyme StabilityLow-temperature PreservationDisulfide Bond Formation KineticsEnzyme Activity During Milk StorageFreezingFreezing-thawing DenaturationFrozen StorageSolubilityTemperature Dependence Of Enzyme ActivityTemperature Effects On Enzyme Activity
ABSTRACT The effects of frozen storage temperatures on the formation of disulfides and the denaturation of actomyosin (AM), extracted from milk‐fish ( Chanos chanos ) dorsal muscle, were investigated. The activities of Ca‐ATPase and Mg(Ca)‐ATPase, Ca‐sensitivity and AM solubility in 0.6M KCl decreased at a higher rate at −20°C than at −35°C. The total NaBH 4 ‐soluble and insoluble proteins increased at a much higher rate at −20°C than at −35°C. During the freezing process, the total SHs decreased significantly; the total SHs decreased with a faster note at −20°C than at −35°C, suggesting that more disulfides formed in samples at −20°C than at −35°C. During storage, disulfides formed at −20°C but not at −35°C.
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George L. Ellman · Archives of Biochemistry and Biophysics · 1959 · 26.2K citations
A micro-biuret method for estimating proteins
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PROTEIN DENATURATION IN FROZEN AND STORED FISH <sup>a</sup>
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