CAJ | 학술논문

由大豆壳中分离出一种过氧化物酶-大豆种皮过氧化物酶(soybean hullperoxidase，SHP，EC 1.11.1.7)，经硫酸铵分级沉淀，DEAE-Sephdex A-50离子交换层析，Bio-Gel P-60凝胶过滤，DEAE-Sephadex A-25二次离子交换和Sephdex G-100凝胶过滤纯化了该酶.分子量为3.8×104u，薄层等电聚焦电泳测得SHP等电点为3.9.SHP的底物范围较宽，以H2O2为电子受体，可以氧化多种木素单体模型物，包括愈创木酚、2，3-二甲氧基酚、2，6-二甲氧基酚、3，4-二甲氧基酚、3，5-二甲氧基酚、1，2，4-三甲氧基苯、阿魏酸、咖啡酸、异丁子香酚和丁香醛联氮，提示该酶在木素的生物降解中有潜在的应用价值.
유대두각중분리출일충과양화물매-대두충피과양화물매(soybean hullperoxidase，SHP，EC 1.11.1.7)，경류산안분급침정，DEAE-Sephdex A-50리자교환층석，Bio-Gel P-60응효과려，DEAE-Sephadex A-25이차리자교환화Sephdex G-100응효과려순화료해매.분자량위3.8×104u，박층등전취초전영측득SHP등전점위3.9.SHP적저물범위교관，이H2O2위전자수체，가이양화다충목소단체모형물，포괄유창목분、2，3-이갑양기분、2，6-이갑양기분、3，4-이갑양기분、3，5-이갑양기분、1，2，4-삼갑양기분、아위산、가배산、이정자향분화정향철련담，제시해매재목소적생물강해중유잠재적응용개치.
Soybean hull peroxidase(EC 1.11.1.7),isolated from Glycine max, was purified to electrophoretic homogeneity by combined consecutive treatments consisting of ammonium sulfate fractionation, column chromatography by gradient elutions from DEAE-Sephadex A-50, gel filtration on Bio-Gel P-60, rechromatography on DEAESephadex A-25 and Sephadex G-100. The molecular weight of the enzyme,determined by SDS-PAGE, was 38000 and the isoelectric point was estimated to be around pH3.9 by IEF experiment. The enzyme possesses a wide substrate specificity along with a high potential and in the presence of hydrogen peroxide,can oxidize various lignin model compounds, including guaiacol, catechol, 2, 6-dimethoxyphenol, 2, 3-dimethoxyphenol, 3,4dimethoxyphenol, 3, 5-dimethoxyphenol, syringyl aldehyde, vanillylacetone, 1, 2, 4-trimethoxybenzene, ferulic acid,isoeugenol, caffeic acid and syringaldazine, etc. This indicates that the enzyme has potential value in lignin degradation.