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    Please use this identifier to cite or link to this item: https://ir.fy.edu.tw:8080/ir/handle/987654321/2238


    Title: Studies on the physicochemical properties of milkfish myoglobin
    Authors: WEN-LEE CHEN;CHAU-JEN CHOW
    Contributors: 輔英科技大學 保健營養系
    Date: 2001-06-01
    Issue Date: 2010-09-26 14:12:20 (UTC+8)
    Abstract: Myoglobin (Mb) was isolated from the dark muscle of the milkfish (Chanos chanos) by Sephadex G-75 gel filtration chromatography. The molecular weight of milkfish Mb is 15, 900 Da. The tristimulus color values (L, a and b) of Mb solutions changed significantly depending upon the form of Mb. With the formation of metmyoglobin (metMb), the L value increased gradually with the increase in the percentage of metMb, while a values decreased and Mb aggregation gradually increased along with incubation time. The autoxidation of milkfish Mb proceeded as a first-order reaction, and the autoxidation rate constant increased with decreasing pH in a range of 5.5–7.0. The free energy for unfolding (Δ GD) of Mb at acidic pH was smaller than at neutral pH, with values of 5.8 kcal/mol at pH 6.63 and 6.0 kcal/mol at pH 7.05. A higher rate of autoxidation and lower values of free energy were observed at acidic pH than at neutral pH.
    Relation: Journal of Food Biochem25(2),157-174
    Appears in Collections:[保健營養系] 期刊論文

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