%0 Journal Article
%T Purification and characterization of laccase from Bjerkandera adusta WZFF.W-Y11<br>烟管菌漆酶的分离纯化及部分酶学性质研究
%A WANG Jian-Feng
%A WANG Zhang
%A RAO Jun
%A LI Jiang
%A BAI Tao
%A <br>王剑锋
%A 王璋
%A 饶军
%A 李江
%A 白涛
%J 菌物学报
%D 2008
%I 
%X 烟管菌Bjerkandera adusta WZFF.W-Y11漆酶粗酶液经过丙酮分级沉淀、DEAE-Cellulose离子交换层析、Sephadex G-100凝胶过滤,得到了三种电泳纯的漆酶同工酶,总酶活回收率达到65.5%,其中LacA平均纯化了29.2倍,LacB纯化了5.1倍,LacC纯化了18.5倍;三种同工酶的分子量分别为LacA:68.7kDa、LacB:80.2kDa、LacC:77.2kDa.LacA、LacC氧化愈创木酚的Km大于氧化ABTS的Km,最适作用温度在45-70℃,最适反应pH3.0-5.5,65℃时LacC比LacA稳定,LacC在pH3.5-6.0稳定,LacA在pH5.0-9.0稳定,Al3 对LacA、LacC的酶活有促进作用,Cl-、Fe3 、Hg2 抑制LacA、LacC的酶活,Cu2 抑制LacC的酶活,而对LacA的活性没有明显影响.
%K isoenzyme
%K acetone fractional precipitation
%K gel filtration chromatography
%K guaiacol<br>同工酶
%K 丙酮分级沉淀
%K 凝胶过滤
%K 愈创木酚
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=CA9F815FCB0F62294C4266BB6F902ACB&aid=4B40C2B5B804F46BAA55C5984B28F2B5&yid=67289AFF6305E306&vid=DB817633AA4F79B9&iid=0B39A22176CE99FB&sid=E42CAFB11D4BE21A&eid=51C74DF6A16DA45B&journal_id=1672-6472&journal_name=菌物学报&referenced_num=1&reference_num=18