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Title: Purification and characterization of metmyoglobin reductase from ordinary muscle of blue-fin tuna
Authors: Ching-Yung Pong;Tze-Kuei Chiou;Fang-Pei Nieh;Shann-Tzong Jiang
Contributors: 國立臺灣海洋大學:食品科學系
Keywords: metmyoglobin reductase;property;purification;tuna
Date: 2000-06
Issue Date: 2016-01-14T07:11:29Z
Publisher: Fisheries Science
Abstract: Abstract:Metmyoglobin (Met-Mb) reductase from blue-fin tuna ordinary muscle was purified to electrophoretical homogeneity by ammonium sulfate fractionation, ion exchange and organomercurial agarose affinity chromatography. The molecular weight estimated by SDS-PAGE was 100 kDa. The optimal pH and temperature for the reduction of met-Mb were 7.3 and 25°C, respectively. This enzyme was very stable at pH 7.0–7.3 and 4°C–15°C. The purified enzyme was strongly activated by K+, moderately activated by Na+ and Mn2+, but not affected by Ni2+. It was moderately inhibited by Li+, NH4+, Mg2+, and Co2+. The Vmax for the reduction of met-Mb and NADH were 0.32 and 0.43 mM/min/mg, while Km were 2.3 × 10−5 and 24.4 × 10−5 M, respectively.
Relation: 66(3)
Appears in Collections:[Department of Food Science] Periodical Articles

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