Tien M
Department of Molecular and Cell Biology, Pennsylvania State University, University Park.
Crit Rev Microbiol. 1987;15(2):141-68. doi: 10.3109/10408418709104456.
The wood-degrading fungus Phanerochaete chrysosporium Burds produces a family of enzymes which degrade lignin and lignin-like substrates. These ligninases exhibit a high degree of homology in being hemeprotein peroxidases, in Mr, in cross reactivity to polyclonal antibodies, in being glycosylated, and in catalytic properties. The predominant ligninase is able to generate cation radicals in its aromatic substrates. These radicals can undergo a variety of reactions thus explaining the nonspecific nature of the enzyme. A similar mechanism is suggested for the other isoenzymes. There are numerous potential applications for ligninases. These include: biopulping, waste treatment of byproduct lignins, detoxification of environmental pollutants, and modification of lignins to produce small molecular weight organics.
木材降解真菌黄孢原毛平革菌（Phanerochaete chrysosporium Burds）产生一系列可降解木质素和类木质素底物的酶。这些木质素酶在作为血红素蛋白过氧化物酶、分子量、与多克隆抗体的交叉反应性、糖基化以及催化特性方面表现出高度同源性。主要的木质素酶能够在其芳香族底物中产生阳离子自由基。这些自由基可发生多种反应，从而解释了该酶的非特异性本质。其他同工酶也被认为具有类似的机制。木质素酶有许多潜在应用。这些应用包括：生物制浆、副产物木质素的废物处理、环境污染物的解毒以及木质素改性以生产小分子有机物。
