Characterization of a novel manganese peroxidase from white-rot fungus Echinodontium taxodii 2538, and its use for the degradation of lignin-related compounds
Characterization of a novel manganese peroxidase from white-rot fungus Echinodontium taxodii 2538, and its use for the degradation of lignin-related compounds
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DOI：
10.1016/j.procbio.2016.01.007
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发表时间：
2016-11-01
影响因子：
4.4
通讯作者：
Zhang, Xiaoyu
中科院分区：
文献类型：
--
作者：
Kong, Wen;Chen, Hong;Zhang, Xiaoyu
本研究分离并鉴定了一种新的锰过氧化物酶（MnP）。一株新的选择性白腐真菌Echinodontium taxodii 2538（E. taxodiii 2538）在毛竹天然木质纤维素培养基上生长。纯化的MNP分子量为53.4 kDa，在十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS-PAGE）上显示单一条带，其N-端氨基酸序列为GTFPSNGVVVP。该酶在pH3.5和55 ℃下均表现出最大酶活，在较宽的pH（2.0-6.0）和温度（45 ℃以下）范围内培养24 h后仍能保持较高的酶活。动力学参数表明，MnP对MnSO 4的亲和力最高（K-m值为0.35 μ M）在所有的基板。研究了MnP对不同类型木质素模型化合物的降解。结果表明，MnP对木质素酚基和非酚基单元均有氧化作用。此外，MnP与漆酶（Lac）结合后，MnP的酶活明显高于漆酶。taxodii 2538对木质素的降解效率更高。总之，本研究为木质素的高效改性提供了一种潜在的酶和一条有前途的途径。(C)2016爱思唯尔有限公司版权所有。
A novel manganese peroxidase (MnP) was isolated and characterized in this study. The MnP was produced by a new selective linguini-degrading white-rot fungus Echinodontium taxodii 2538 (E. taxodii 2538) on natural lignocellulose medium of moso bamboo. The purified MnP had an estimated molecular mass of 53.4 kDa, showing a single band on sodium dodecyl sulfate poly acrylamide gel electrophoresis (SDS-PAGE), and composed of an amino acid sequence of GTFPSNGVVVP at N-terminal. The enzyme showed maximum activity when incubated at pH 3.5 or 55 degrees C and could maintain a high enzymatic activity after 24h incubation under a broad range of pH (2.0-6.0) and temperature (below 45 degrees C). The kinetic parameters revealed that the MnP had the highest affinity toward MnSO4 (K-m values was 0.35 mu M) among all the substrates. Degradation of different types of lignin model compounds by MnP was investigated. It revealed that the MnP could oxidize both phenolic and nonphenolic lignin units. In addition, the MnP combined with laccase (Lac) from E. taxodii 2538 could degrade lignin more efficiently. In summary, this study provided a potential enzyme and a promising path for more efficient lignin modification. (C) 2016 Elsevier Ltd. All rights reserved.