Chia Nan University of Pharmacy & Science Institutional Repository:Item 310902800/21877
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    標題: Isolation of Lysozyme by Anti-LS Immunoglobulin in Yolk Bound Immunoaffinity Chromatography
    作者: Yann-Ying Tu
    Chao-Cheng Chen
    貢獻者: 保健營養系
    日期: 2008-11
    上傳時間: 2009-10-30 16:09:44 (UTC+8)
    摘要: Immunoglobulin in yolk (Ig Y) specific against lysozyme (LS) was bound to Sepharose 4 Fast Flow gel to propare anti-LS Ig Y-immunoaffinity chromatographic column, to which diluted hen egg white and duck egg white were applied to determine and compare the changes in specific activity, recovery (%), and purification efficiency. It was observed that specific activity of isolated LS from hen egg white was about 44830 units/mg protein with a recovery of 94%, whereas that of isolated duck egg white was about 15460 units/mg protein with a recovery of only 12%. By repeated application of various amounts (0-5.75 mg LS/mL) of LS in commercial LS product or diluted hen egg white to anti-LS Ig Y-Sepharose 4 Fast Flow immunoaffinity chromatography, it was found that the binding capacity (qm) of this anti-LS Ig Y-immunoaffinity gel for commercial LS was 0.16 mg/mL wet gel, higher than that (0.11 mg/mL wet gel) of the immunoaffinity gel for diluted hen white. In contrast, the dissociation constant (Kd) of suck immunoaffinity gel for LS in diluted hen egg white was 3.72�10-8 M for commercial LS. It suggests a relatively weaker immunoaffinity between diluted hen egg white LS and anti-LS Ig Y-immunoaffinity gel.
    關聯: 台灣食品科技學會第38次年會,起迄日:2008/11/20~2008/11/21,地點:國立屏東科技大學
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