Effect of Sodium Pyruvate on the Texture of Frozen Stored Cod Fillets

Tran, V. D.

doi:10.1111/j.1365-2621.1975.tb00583.x

Cited by 6 publications

(2 citation statements)

References 11 publications

(2 reference statements)

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“…Most studies on frozen fish have been undertaken on myofibrillar proteins, which show rapid denaturation of myosin followed by actin (4,7). However, increasing evidence suggests that connective tissue proteins such as collagen may also be denatured; this would affect muscle integrity and rheological properties of frozen lean fish fillets (4,(9)(10)(11). Collagen is the major protein component of connective tissue which makes up about 2-5% of muscle.…”

Section: Introductionmentioning

confidence: 99%

“…Collagen, a glycoprotein (MW ∼300,000 Da), has been characterized as Types 1,11,and 111 and consists of a central triple helix with small nonhelical peptides (telopeptides) at each end (12). Type 1 collagen molecules are made up of three chains which may be predominantly R 1 and R 2 whereas Types 11 and 111 each contain only one chain type R 1 (11) and R 1 (111), respectively. The R chains vary depending on the tissue.…”

Section: Introductionmentioning

confidence: 99%

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Elucidation of the Effect of Formaldehyde and Lipids on Frozen Stored Cod Collagen by FT-Raman Spectroscopy and Differential Scanning Calorimetry

Badii

Howell

2003

J. Agric. Food Chem.

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The effect of frozen storage (-10 and -30 degrees C), formaldehyde, and fish oil on collagen, isolated from cod muscle, was investigated. Salt- and acid-soluble collagen fractions as well as insoluble collagen indicated changes in solubility on frozen storage. Differential scanning calorimetry (DSC) showed a highly cooperative transition at 28.2 degrees C for isolated collagen. Changes in the thermodynamic properties of collagen were observed on frozen storage at -10 degrees C compared with the control at -30 degrees C because of changes in structure. In the presence of formaldehyde, there were no changes in the DSC collagen transition; however, in the presence of fish oil there was an increase in enthalpy and an extra peak was observed at 44.6 degrees C, indicating collagen-fish oil interaction. Structural changes resulted in a decrease in the solubility of collagen in salt and acid solution. FT-Raman spectra obtained for collagen at -10 degrees C and -30 degrees C confirmed the alteration of the conformation of collagen not only at -10 degrees C but also in the presence of formaldehyde and fish oil.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Elucidation of the Effect of Formaldehyde and Lipids on Frozen Stored Cod Collagen by FT-Raman Spectroscopy and Differential Scanning Calorimetry

Badii

Howell

2003

J. Agric. Food Chem.

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Fluorescence of fish muscle: Causes of change occuring during frozen storage

Davis¹,

Reece²

1982

J Sci Food Agric

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The causes of two fluorescent emissions which develop in fish muscle during frozen storage have been investigated. Both appear to be predominantly associated with proteins via reaction between free amino groups and carbonyl compounds. Under favourable conditions, a white or pale blue emission is produced throughout the white muscle as the result of reactions involving sugars and sugar phosphates in lowtemperature browning reactions. A bright yellow fluorescence arises from reactions involving formaldehyde produced by enzymic degradation of trimethylamine oxide.

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Review

Piñeiro

1995

Z Lebensm Unters Forch

106

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Proteins of fish muscle undergo chemical and physical changes during frozen storage which may result in, under certain conditions (i.e. long periods of storage, poor freezing practices, temperature fluctuations, etc), loss of quality, reflected mainly by an unacceptable texture as well as an undesirable flavour, odour and colour. In frozen gadoid fish species, most of these changes are caused by the production of formaldehyde in the muscle. Formaldehyde is produced, along with dimethylamine, by the enzymatic reduction of trimethylamine oxide (TMAO). Many aspects of formaldehyde production by TMAO demethylase (TMAOase) have been studied throughout the last decade. In addition, different approaches have been used to investigate the effect of formaldehyde production on protein denaturation and the associated muscle textural changes. Some insight into the reaction between protein and formaldehyde has clarified the possible mechanism of formaldehyde-mediated denaturation. However, evidence of covalent bonding between proteins and formaldehyde, to form crosslinks, has not explained fully the changes observed in fish proteins during frozen storage. The study of cold-induced denaturation of proteins might give new clues for further investigation of the problem. The implications of formaldehyde in toxicological and nutritional issues is also reviewed, as general concern about the safety of food products is a growing field in food science. Finally, different approaches have been proposed to avoid the detrimental action of formaldehyde during frozen storage of gadoid fish; they are some of the practical applications of the knowledge acquired after years of study of different workers in the field.

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Effect of Sodium Pyruvate on the Texture of Frozen Stored Cod Fillets

Cited by 6 publications

References 11 publications

Elucidation of the Effect of Formaldehyde and Lipids on Frozen Stored Cod Collagen by FT-Raman Spectroscopy and Differential Scanning Calorimetry

Elucidation of the Effect of Formaldehyde and Lipids on Frozen Stored Cod Collagen by FT-Raman Spectroscopy and Differential Scanning Calorimetry

Fluorescence of fish muscle: Causes of change occuring during frozen storage

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