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机构地区:[1]中国科学院微生物研究所
出 处:《微生物学报》1993年第6期427-433,共7页Acta Microbiologica Sinica
摘 要:从海枣曲霉麦麸培养物抽提液中,通过聚乙二醇6000-磷酸钾缓冲液双水相分离,相继用Sephadex G-100凝胶过滤、DEAE-Sephadex A-50离子交换柱层析、羟基磷石吸附层析、DEAE-Sephadex A-50离子交换层析、SE-Sephadex C-50离子交换层析以及最适温度为65℃,在pH3.5-6.5之间稳定,酶保温30分钟时的半失活温度(t1/2)为68℃。A β-Xylosidase has been purified to PAGE homogeneity from the wheat branculture of Aspergillus phoenicis.by PEG 6000-phosphate buffer aqueous twophaseseparation and successive chromatography on Sephadex G-100,DEAE-Sephadex A-50,hydroxyapatite,DEAE-Sephadex A-50,SE-Sephadex C-50 and Sephadex G-50columns.The enzyme showed optimum activity at pH 3.5 and 65(?),it was stable in thepH range 3.5—6.5.The molecular weight of the enzyme was 95000 as determined bySDS-PAGE and concentration gradient-PAGE.The isoelectric point was estimated to bepI 4.4.The enzyme showed the highest activity toward pNP-β-Xyloside.The K_m andthe V_(max) values were 0.63mmol/L,and 410μmol·min^(-1)·mg^(-1),respectively.Theenzyme was strongly inhibited by Hg^(2+),Ag^+ and D-Xylose.The K_1 for D-Xylose wasabout 7.5 mmol/L,as determined by Lineweaver-Burk plot and Dixon plot.
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