Purification and properties of levanase from Rhodotorula sp.

被引：15
|
作者：
Chaudhary, A
Gupta, LK
Gupta, JK
Banerjee, UC
机构：
[1] INST MICROBIAL TECHNOL, CHANDIGARH 160014, INDIA
[2] INDIAN AGR RES INST, DIV ENVIRONM SCI, NEW DELHI 110012, INDIA
[3] PANJAB UNIV, DEPT MICROBIOL, CHANDIGARH 160014, INDIA
来源：
JOURNAL OF BIOTECHNOLOGY | 1996年 / 46卷 / 01期
关键词：
levanase; purification; chromatography; Rhodotorula sp;
D O I：
10.1016/0168-1656(95)00183-2
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
Levanase, a slime dissolving enzyme of Rhodotorula sp., was purified to approx. 26-fold by ammonium sulphate precipitation, DEAE and gel filtration (Sephacryl S-200) chromatography. The moleculer mass of the enzyme was 39 kDa. The purified levanase showed maximum activity at pH 6.0 and 40 degrees C. Enzyme was quite stable at 4 degrees C and at pH 5.5 to 6.5. Hg2+ at a level of 10 mM completely inhibited the levanase activity, while 2-mercaptoethanol at the same concentration showed a 2.93-times increase in activity. In addition to levan, the enzyme also showed substrate specificity towards inulin.
引用
收藏
页码：55 / 61
页数：7
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