%0 Journal Article
%T PURIFICATION AND SOME PROPERTIES OF D-HYDANTOINASE PRODUCED BY PSEUDOMONAS 2262<br>假单胞杆菌D-海因酶的纯化及酶学性质
%A Shi Yawei
%A Li Hanqing
%A Yuan Jingming
%A <br>石亚伟
%A 李汉卿
%A 袁静明
%A 齐延红
%A 李晋川
%J 微生物学报
%D 2001
%I 
%X A D-hydantoinase produced by Pseudomonas 2262 was purified to electrophoretic homogeneity by the steps of thermal treatment, (NH4)2SO4 fractionation and column chromatography with Q-Sepharose fast flow, phenyl-Sepharose fast flow and Superose 12. Purification of about 60 fold was achieved with an overall yield of 16%. The relative molecular mass of the native enzyme is 109 kD and that of subunit is 53.7 kD by the analysis of Native and SDS-PAGE as well as gel filtration respectively. Some properties of the enzyme such as the sensitivity to thiol reagent and the effects of metal ions, for instance inhibited by Zn2+ and activited by Mn2+, Mg2+ are identical to dihydropyrimidinase. The optimum temperature and pH for enzymatic catalysis are 70 degrees C and 8.0 respectively. The enzyme activity is stable under 60 degrees C and in the pH range of 6-10. The N-terminal sequence for 10 amino acid residues is MDKLIKNGTI.
%K Pseudomonas 2262
%K Hydantoinase
%K Purification
%K Properties<br>假单胞杆菌2262
%K D－海因酶
%K 纯化
%K 性质
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=9825A6D437F899D4&yid=14E7EF987E4155E6&vid=2001E0D53B7B80EC&iid=94C357A881DFC066&sid=10A39635766FF5D0&eid=44E78A5D1B37D836&journal_id=0001-6209&journal_name=微生物学报&referenced_num=12&reference_num=11