Development of a new method for determination of total haem protein in fish muscle
Journal article, 2015

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.

Method

Hemichrome

Sodium dodecyl sulphate

Myoglobin

Fish muscle

Haemoglobin

Oxidation

Haem proteins

Quantification

Author

Manat Chaijan

Chalmers, Biology and Biological Engineering, Food and Nutrition Science

Ingrid Undeland

Chalmers, Biology and Biological Engineering, Food and Nutrition Science

Food Chemistry

0308-8146 (ISSN)

Vol. 173 1133-1141

Subject Categories

Other Chemical Engineering

DOI

10.1016/j.foodchem.2014.11.010

More information

Created

10/8/2017