Degradation of synthetic lignin by the protoplasts of Phanerochaete chrysosporium in the presence of lignin peroxidase or manganese peroxidase

S. Sayadi, E. Odier
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引用次数: 3

Abstract

Lignin was mineralized in the experiments in which 14 C-lignin was incubated with lignin peroxidase or manganese peroxidase in a tartrate buffer in the presence of cycloheximide-treated protoplasts obtained from the ligninolytic mycelia of Phanerochaete chrysosporium. The rate of lignin mineralization was dependent on the lignin peroxidase or manganese peroxidase concentration in the medium. In the experiments in which lignin was incubated with lignin peroxidase or manganese peroxidase, lignin was repolymerized irrespective of the presence of protoplasts mineralizing lignin, suggesting that an active degradation of lignin and repolymerization took place. Taking into account that lignin peroxidase and manganese peroxidase were the only extracellular enzymes in the experiments in which lignin was mineralized by the protoplasts, it is postulated that lignin peroxidase and/or manganese peroxidase can degrade lignin into small fragments which can then be further absorbed by the fungal cells and subsequently degraded to CO 2
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在木质素过氧化物酶或锰过氧化物酶存在下,黄孢原生质对合成木质素的降解
木质素矿化实验中,14c -木质素与木质素过氧化物酶或锰过氧化物酶在酒石酸缓冲液中孵育,存在环己亚胺处理的原生质体,原生质体来自黄孢原毛Phanerochaete chrysosporium的木质素降解菌丝体。木质素矿化率取决于培养基中木质素过氧化物酶或锰过氧化物酶的浓度。在木质素与木质素过氧化物酶或锰过氧化物酶的实验中,木质素被重新聚合,而不考虑原生质体矿化木质素的存在,这表明木质素的主动降解和再聚合发生了。考虑到木质素过氧化物酶和锰过氧化物酶是实验中唯一的木质素被原生质体矿化的细胞外酶,我们假设木质素过氧化物酶和/或锰过氧化物酶可以将木质素降解成小片段,然后这些小片段可以被真菌细胞进一步吸收并随后降解为二氧化碳
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