Relation between TMAOase activity and content of formaldehyde in fillet minces and bellyflap minces from gadoid fishes

Rehbein, Hartmut and Schubring, Reinhard and Havemeister, W. and Gonzales-Sotelo, C. and Nielsen, M.K. and Jorgensen, B. and Jessen, F. (1997) Relation between TMAOase activity and content of formaldehyde in fillet minces and bellyflap minces from gadoid fishes. Informationen für die Fischwirtschaft aus der Fischereiforschung, 44(3), pp. 114-118.

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Abstract

Minced fish is a significant component of a number of frozen fishery products like fish fingers, cakes and patties. Predominately minced fish is produced from gadoid species (Alaska pollack, cod, saithe, hake and others) possessing the enzyme trimethylamine oxide demethylase (TMAOase, E.C. 4.1.2.32) (Rehbein and Schreiber 1984). TMAOase catalyses the degradation of trimethylamine oxide (TMAO) to formaldehyde (FA) and dimethylamine (DMA), preferentially during frozen storage of products (Hultin 1992). In most gadoid species light muscle contains only low activity of TMAOase, the activity of red muscle and bellyflaps being somewhat higher. In contrast, the TMAOase activity in blood, kidney and other tissues, residues of which may contaminate minced fish flesh, may be higher for several orders of magnitude (Rehbein and Schreiber 1984).

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