Purification and properties of levanase from Rhodotorula sp.

被引：16

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

页码：55 / 61

页数：7

共 13 条

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