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Development of a new method for determination of total haem protein in fish muscle

Manat Chaijan (Institutionen för biologi och bioteknik, Livsmedelsvetenskap) ; Ingrid Undeland (Institutionen för biologi och bioteknik, Livsmedelsvetenskap)
Food Chemistry (0308-8146). Vol. 173 (2015), p. 1133-1141.
[Artikel, refereegranskad vetenskaplig]

Using classic haem protein quantification methods, the extraction step in buffer or acid acetone often becomes limiting if muscle is oxidised and/or stored; haem-proteins then tend to bind to muscle components like myofibrils and/or biomembranes. The objective of this study was to develop a new haem protein determination method for fish muscle overcoming such extractability problems. The principle was to homogenise and heat samples in an SOS-containing phosphate buffer to dissolve major muscle components and convert ferrous/ferric haem proteins to hemichromes with a unique absorption peak at 535 nm. Hb-recovery tests with the new and classic methods showed that the new method and Hornsey's method performed significantly better on fresh fib-enriched cod mince than Brown's and Drabkin's methods; recovery was >= 98%. However, in highly oxidised samples and in cod protein isolates made with acid pH-shift processing, the new method performed better than Hornsey's method (63% and 87% vs. 50% and 68% recovery). Further, the new method performed well in fish muscle with <= 30% lipid, <5% NaCl and pH 5.5-7.0; it was also unaffected by freezing/frozen storage.

Nyckelord: Quantification, Method, Haem proteins, Haemoglobin, Myoglobin, Fish muscle, Oxidation, Hemichrome, Sodium dodecyl sulphate

Denna post skapades 2015-02-19.
CPL Pubid: 212862


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Institutionen för biologi och bioteknik, Livsmedelsvetenskap


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