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E. Childs (1973)
Electrophoresis of Fish Myofibrillar Proteins With Sodium-Dodecyl Sulfate-Polyacrylamide GelWsq: Women's Studies Quarterly, 30
H. Buttkus (1970)
ACCELERATED DENATURATION OF MYOSIN IN FROZEN SOLUTIONJournal of Food Science, 35
H. Buttkus (1967)
The Reaction of Myosin with MalonaldehydeJournal of Food Science, 32
E. Childs (1973)
QUANTITATIVE CHANGES IN WHOLE MYOFIBRILS AND MYOFIBRILLAR PROTEINS DURING FROZEN STORAGE OF TRUE CODJournal of Food Science, 38
W. Dyer (1951)
PROTEIN DENATURATION IN FROZEN AND STORED FISHaJournal of Food Science, 16
J. Babbitt, D. Crawford, D. Law (1972)
Decomposition of trimethylamine oxide and changes in protein extractability during frozen storage of minced and intact hake (Merluccius productus) muscleJournal of Agricultural and Food Chemistry, 20
Harada Harada, Yamada Yamada (1971)
Some properties of a formaldehyde and dimethylamine forming enzyme from Barbatia virescensJ. Shimon. Univ. Fish., 19
Babbitt Babbitt, Crawford Crawford, Law Law (1972)
Decomposition of trimethylamine oxide and changes in protein extractability during frozen storage of minced and intact hake muscleAg. Fd. Chem., 20
C. Castell (1971)
Metal-catalyzed lipid oxidation and changes of proteins in fishJournal of the American Oil Chemists Society, 48
Ravesi Ravesi, Anderson Anderson (1969)
Effect of varying the extraction procedure on the protein extractability of frozen‐stored fish muscleFish. Ind. Res., 5
Dyer Dyer (1951)
Protein denaturation in frozen and stored fishFood Res., 16
J. Connell (1968)
The Effect of Freezing and Frozen Storage on the Proteins of Fish Muscle
INTRODUCTION DURING FROZEN STORAGE of fish muscle there is a progressive decrease in (a) extractable whole myofibrils (Childs, 1973b) and (b) protein extractable in high ionic strength salt solutions (Dyer, 195 1). Much work has been performed in an attempt to explain this latter phenomena and a great deal of effort has been expended in observations on the interactions of breakdown products such as free fatty acid with fish muscle (see review by Connell, 1968). In some fish of trimethylamine reduction species, oxide yields formaldehyde (Harada and Yamada, 197 1 ), which has been shown to cause a marked decrease in the amount of protein soluble in 0.50~ saline solutions (Castell, 1971). It thus appears plausible that formaldehyde may play some role in in situ protein, and myofibril, insolubilization in fish muscle. This study was undertaken to determine the quantitative and qualitative effects of formaldehyde on salt soluble proteins and whole myofibrils in vitro, and to obtain possible insights to its in situ effects. fer + FA were placed in a Virtis homogenizing flask equipped with a baffle plate to prevent foaming. The sample was homogenized for 3 min at medium speed and the homogenate then centrifuged for
Journal of Food Science – Wiley
Published: Sep 1, 1973
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