Application of the affinity binding of xylanases to oat-spelt xylan in the purification of endoxylanase CM-2 from Streptomyces chattanoogensis CECT 3336

被引:16
作者
López-Fernández, CL
Rodríguez, J
Ball, AS
Copa-Patiño, JL
Pérez-Leblic, MI
Arias, ME [1 ]
机构
[1] Univ Alcala de Henares, Dept Microbiol & Parasitol, Madrid 28871, Spain
[2] Univ Essex, Dept Biol Sci, Colchester CO4 3SQ, Essex, England
关键词
D O I
10.1007/s002530051291
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
The use of the insoluble polysaccharides Avicel and oat-spelt xylan for the binding and subsequent purification of active xylanases from Streptomyces chattanoogensis was investigated. Maximum recovery of xylanases was achieved with oat-spelt xylan, using NaCl (2 M) to remove active protein. The application of this technique to the purification of xylanases resulted in the purification of an endoxylanase (CM-2) with high specific activity (729.5 U mg(-1)). The properties of the purified enzyme, exhibiting activity and stability between 40 degrees C and 60 degrees C and between pH 5 and 8, suggest a potential role for both the enzyme and the rapid purification protocol in the removal of hemicelluloses from kraft pulp prior to bleaching.
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页码:284 / 287
页数:4
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