里氏木霉β-木糖苷酶的分离纯化、酶学性质及水解机理研究

doi:10.3969/j.issn.1673-5854.2013.01.004

›› 2013, Vol. 47 ›› Issue (1): 27-32.doi: 10.3969/j.issn.1673-5854.2013.01.004

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Purification, Characterization and Hydrolysis Mechanism of β-Xylosidase from Trichoderma reesei

JIANG Xiao-hua, ZHU Jun-jun, YU Shi-yuan, YONG Qiang

College of Chemical Engineering, Nanjing Forestry University, Nanjing 210037, China

Received:2012-11-23 Revised:1900-01-01 Online:2013-01-30 Published:2013-01-30

Abstract

Abstract: Using ammonium sulfate precipitation, ultrafiltration desalination, ion-exchange and gel filtration column chromatography, a β-xylosidase with molecular weight of 110.8 ku and specific activity of 61.99 IU/mg was purified to homogeneity from culture xylanase solution of Trichoderma reesei Rut C-30. Results of enzymatic properties showed that the optimal reaction condition of the enzyme was: pH value of 3.5; reaction temperature of 60 ℃. The enzyme was stable below 60 ℃ and pH value ranges from 3.0 to 8.0. It had a K_m value of 0.29 μmol/mL and V_max value of 169.99 IU/mg by using p-nitrophenyl-β-D-xylopyranoside as the substrate. Results of enzymatic hydrolysis mechanism indicated that β-xylosidase released xylose from non-reducing ends of xylooligosaccharides by cutting off β-1,4-glycosidic bond. The optimum substrate of β-xylosidase was short-chain xylooligosaccharides. With chain length of xylooligosaccharides increased, the enzyme hydrolysis efficiency decreased gradually and xylan was hardly to be degraded.

Key words: Trichoderma reesei, β-xylosidase, purification, enzymatic hydrolysis

CLC Number:

TQ35

JIANG Xiao-hua;ZHU Jun-jun;YU Shi-yuan;YONG Qiang. Purification, Characterization and Hydrolysis Mechanism of β-Xylosidase from Trichoderma reesei[J]. , 2013, 47(1): 27-32.

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Purification, Characterization and Hydrolysis Mechanism of β-Xylosidase from Trichoderma reesei

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