期刊
CELLULOSE
卷 20, 期 4, 页码 1947-1955出版社
SPRINGER
DOI: 10.1007/s10570-013-9953-z
关键词
Xylanase; Purification; Enzyme activity; SDS-resistant; Extremophiles; Streptomonospora
资金
- National Basic Research Program of China [2010CB8 33801]
- Key Project of International Cooperation of Ministry of Science & Technology (MOST) [2013DFA 31980]
- National Natural Science Foundation of China [31270054]
- International Cooperation Research Program of Yunnan Province [2009AC017]
- Chinese Academy of Sciences
An extracellular xylanase from halophilic Streptomonospora sp. YIM 90494 was purified to homogeneity from a fermentation broth by ammonium sulphate precipitation, gel filtration chromatography and ion exchange chromatography. The purified xylanase appeared as a single protein band on SDS-PAGE with a molecular mass of approximately 50 kDa. The xylanase had maximum activity at pH 7.5 and 55 A degrees C. The enzyme was stable over a broad pH range (pH 4.0-10.0) and showed good thermal stability when being incubated at 60 A degrees C for 2 h. Kinetic experiments indicated that the enzyme had K (m) and V (max) values of 19.24 mg/mL and 6.1 mu mol/min/mg, respectively, using birch wood xylan as substrate. The inhibitory effects of various metal ions and chemical agents on the xylanase activity were investigated. It is greatly interesting to note that Ag+ ion and SDS, which strongly inhibited most xylanases reported previously increases the xylanase activity in this study. These characteristics suggest that the enzyme with new properties has considerable potential in industrial applications.
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