红酵母属菌株中果聚糖酶的纯化及性质

Purification and properties of levanase from Rhodotorula sp.

作者信息

Chaudhary A, Gupta L K, Gupta J K, Banerjee U C

机构信息

Division of Environmental Sciences, IARI, New Delhi, India.

出版信息

J Biotechnol. 1996 Apr 18;46(1):55-61. doi: 10.1016/0168-1656(95)00183-2.

DOI:10.1016/0168-1656(95)00183-2

PMID:8672285

Abstract

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 molecular 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.

摘要

解聚酶是红酵母属的一种黏液溶解酶，通过硫酸铵沉淀、DEAE和凝胶过滤（Sephacryl S-200）色谱法纯化至约26倍。该酶的分子量为39 kDa。纯化后的解聚酶在pH 6.0和40℃时表现出最大活性。该酶在4℃以及pH 5.5至6.5时相当稳定。10 mM的Hg2+完全抑制解聚酶的活性，而相同浓度的2-巯基乙醇则使活性提高了2.93倍。除了果聚糖外，该酶对菊粉也表现出底物特异性。