Effect of pH, ADP and muscle soluble components on cod hemoglobin characteristics and extractability

The effect of pH, ADP and the soluble components of the muscle on the extractability of cod hemoglobin was studied. A marked decrease in hemoglobin extractability from washed and unwashed mince was observed at pH 6.0. This coincided with the binding of the hemoglobin to cod sarcoplasmic reticulum at...

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Veröffentlicht in:Food chemistry 2006-08, Vol.97 (4), p.567-576
Hauptverfasser: Thongraung, Chakree, Benjakul, Soottawat, Hultin, Herbert O.
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container_title Food chemistry
container_volume 97
creator Thongraung, Chakree
Benjakul, Soottawat
Hultin, Herbert O.
description The effect of pH, ADP and the soluble components of the muscle on the extractability of cod hemoglobin was studied. A marked decrease in hemoglobin extractability from washed and unwashed mince was observed at pH 6.0. This coincided with the binding of the hemoglobin to cod sarcoplasmic reticulum at pH 6.0. After 10 min of incubation at pH 6.0, most non-extractable hemoglobin could be extracted at pH 7.0 or higher. The soluble fraction of cod muscle increased hemoglobin extractability and decreased the hemoglobin bound to the sarcoplasmic reticulum. A decrease in hemoglobin extractability in unwashed mince with added ADP at pH 7.0 occurred with an increased amount of deoxyhemoglobin. The results suggested that medium pH and deoxygenation of hemoglobin were related to the decrease in hemoglobin extractability at pH 6.0.
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A marked decrease in hemoglobin extractability from washed and unwashed mince was observed at pH 6.0. This coincided with the binding of the hemoglobin to cod sarcoplasmic reticulum at pH 6.0. After 10 min of incubation at pH 6.0, most non-extractable hemoglobin could be extracted at pH 7.0 or higher. The soluble fraction of cod muscle increased hemoglobin extractability and decreased the hemoglobin bound to the sarcoplasmic reticulum. A decrease in hemoglobin extractability in unwashed mince with added ADP at pH 7.0 occurred with an increased amount of deoxyhemoglobin. 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A marked decrease in hemoglobin extractability from washed and unwashed mince was observed at pH 6.0. This coincided with the binding of the hemoglobin to cod sarcoplasmic reticulum at pH 6.0. After 10 min of incubation at pH 6.0, most non-extractable hemoglobin could be extracted at pH 7.0 or higher. The soluble fraction of cod muscle increased hemoglobin extractability and decreased the hemoglobin bound to the sarcoplasmic reticulum. A decrease in hemoglobin extractability in unwashed mince with added ADP at pH 7.0 occurred with an increased amount of deoxyhemoglobin. The results suggested that medium pH and deoxygenation of hemoglobin were related to the decrease in hemoglobin extractability at pH 6.0.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><doi>10.1016/j.foodchem.2005.05.006</doi><tpages>10</tpages></addata></record>
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subjects adenosine diphosphate
Binding of hemoglobin
binding properties
Biological and medical sciences
cod (fish)
color
Extractability of hemoglobin
extraction
Fish and seafood industries
Food industries
food processing
food quality
Fundamental and applied biological sciences. Psychology
Hemoglobin
Marine
minced fish
Sarcoplasmic reticulum
seafoods
surimi
water solubility
title Effect of pH, ADP and muscle soluble components on cod hemoglobin characteristics and extractability
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