Heterologous Expression and Characterization of an Acidic GH11 Family Xylanase from <Emphasis Type="Italic">Hypocrea orientalis</Emphasis> |
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| Authors: | Hailong Li Hongli Wu Fengjiao Jiang Jinlian Wu Yong Xue Lihui Gan Jian Liu Minnan Long |
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| Institution: | 1.Guangzhou Institute of Energy Conversion,Chinese Academy of Sciences,Guangzhou,People’s Republic of China;2.College of Energy,Xiamen University,Xiamen,People’s Republic of China;3.CAS Key Laboratory of Renewable Energy,Guangzhou,People’s Republic of China;4.Guangdong Provincial Key Laboratory of New and Renewable Energy Research and Development,Guangzhou,People’s Republic of China |
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| Abstract: | A gene encoding glycoside hydrolase family 11 xylanase (HoXyn11B) from Hypocrea orientalis EU7–22 was expressed in Pichia pastoris with a high activity (413 IU/ml). HoXyn11B was partly N-glycosylated and appeared two protein bands (19–29 kDa) on SDS-PAGE. The recombinant enzyme exhibited optimal activity at pH 4.5 and 55 °C, and retained more than 90% of the original activity after incubation at 50 °C for 60 min. The determined apparent K m and V max values using beechwood xylan were 10.43 mg/ml and 3246.75 IU/mg, respectively. The modes of action of recombinant HoXyn11B on xylo-oligosaccharides (XOSs) and beechwood xylan were investigated by thin-layer chromatography (TLC), high-performance liquid chromatography (HPLC), and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS), which indicated that the modes of action of HoXyn11B are different from HoXyn11A since it is able to release a significant amount of xylose from various substrates. This study provides an opportunity to better understand the hydrolysis mechanisms of xylan by xylanases from Trichoderma. |
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