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- W2010095388 abstract "Trimethylamine N-oxide (TMAO) is a natural, characteristic component of muscle tissues and visceral organs of sea fish and invertebrates. In about thirty species of fish and eight species of invertebrates TMAO is broken down post mortem to dimethylamine (DMA) and formaldehyde (FA). The enzyme catalysing this reaction is present in the muscles, skin and visceral organs. The available published information indicates that the enzymes differ in molecular weight and requirements of cofactors, depending upon the source of isolation. However, glutathione, ferrous chloride, ascorbic acid, methylene blue and flavonucleotide activate the demethylase from various sources. The optimum pH for TMAO demethylation is from 5·0 to 7·5. Freezing and frozen storage do not destroy the activity of TMAO demethylase. The rate of enzymatic cleavage of TMAO to FA and DMA depends on the substrate and FA. In numerous observations it was found that during frozen storage of fish belonging to the Gadoid family a progressive accumulation of DMA and FA takes place and is accompanied by a decrease in protein extractability and deterioration of the textural properties of the flesh." @default.
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- W2010095388 date "1982-10-01" @default.
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- W2010095388 title "Trimethylamine N-oxide demethylase: Its occurrence, properties, and rôle in technological changes in frozen fish" @default.
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- W2010095388 doi "https://doi.org/10.1016/0308-8146(82)90099-1" @default.
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