链霉菌SO1菌株几丁质酶的纯化及性质  

PURIFICATION AND PROPERTIES OF CHITINASE FROM STREPTOMYCES SP.S01

作　　者：杨文博[1] 冯波[1] 佟树敏[1] 

机构地区：[1]南开大学微生物学系,天津300071

出　　处：《微生物学通报》1997年第2期84-88,共5页Microbiology China

摘　　要：由链霉菌（Streptomycessp.）SO1菌株产生的几丁质酶（Citinase）经硫酸铵盐析、OEAE纤维素柱层析、SephadexG－100柱层桥分离纯化后，得到SDS－PAGE均一样品。用SDS－PAG测得纯化后的几丁质酶分子量为41Ku，用PAGEIEF测得等电点PI为5.4。酶反应的最适pH值为6．0，最适温度为50℃，在pH5．0～9．0、温度30～50℃时酶活性比较稳定。在相当于0.1mol／LNaCl的离子强度下酶活性最高。金属离子中的Mg2+、Ca2+、Mn2+对酶有较强的激活作用，而Fe3+、Hg2+则有强烈的抑制作用。SO1菌几丁质酶对胶体几丁质的Km及Vmax分别为0.91mg·ml-1和262.13μmol·min-1·mg-1。T c chitinase produced by Strptodyces sp.S01bwas purified to SDS-PAGE homogeneity by （NE4）SO4 precipitation, DEAE-cellulose column chromatography, and Sephadex G-100 colunm gel filtration. Molecular wdight and pI value of the chitinase wrre 41ku and 5.4When they were determined by the methods of SDS-PAGES-PAG PAGEIEF.nThe optimum pH and tempererature were 6.0 and 50℃.The enzyme activity was stable in the pH rang of 5.0 ～ 9.0 and tempereture range of 30～50℃. The highest enzyme activity could be obtained in the ionic Strength tha corresponded to 0.1mol ／L NaCl solution.The edzyme was enhaned by Mg2+, Ca2+, Mn2+, and was Strongly iultibital by Fe3+,Hg2+. When colloidal chihn was ued as substrate, the michaelis constant (Km) and Maximum velicity (Vmax) of chitinase from SO1 strain Were 0.91mg' ml-1 and 262.13 umol min-1 mg-1respectively.

关 键 词：几丁质酶 链霉菌S01菌株 纯化 性质 

分 类 号：Q939.130.6[生物学—微生物学]