Herein, it was unearthed that manganese peroxidase (MnP) from Phanerochaete chrysosporium, a lignin-degrading enzyme, is capable of not only directly decomposing cellulosic components but also boosting cellulase activity. MnP decomposes various cellulosic substrates (carboxymethyl cellulose, cellobiose [CMC], and Avicel®) and produces reducing sugars rather than oxidized sugars such as lactone and ketoaldolase. MnP with Mn^II in acetate buffer evolves the Mn^III-acetate complex functioning as a strong oxidant, and the non-specificity of Mn^III-acetate enables cellulose-decomposition. The catalytic mechanism was proposed by analyzing catalytic products derived from MnP-treated cellopentaose. Notably, MnP also boosts cellulase activity on CMC and Avicel®, even considering the cellulolytic activity of MnP itself. To the best of the authors’ knowledge, this is the first report demonstrating a previously unknown fungal MnP activity in cellulose-decomposition in addition to a known delignification activity. Consequently, the results provide a promising insight for further investigation of the versatility of lignin-degrading biocatalysts.

在此，从金黄原毛菌中发现的锰过氧化物酶 (MnP) 是一种木质素降解酶，不仅能够直接分解纤维素成分，而且能够提高纤维素酶的活性。MnP 分解各种纤维素底物（羧甲基纤维素、纤维二糖 [CMC] 和 Avicel®）并产生还原糖而不是氧化糖，例如内酯和酮醛缩酶。MnP 与 Mn ^II在乙酸盐缓冲液中形成 Mn ^{III -乙酸盐络合物，起强氧化剂的作用，而 Mn III}的非特异性-醋酸盐使纤维素分解。通过分析来自 MnP 处理的纤维五糖的催化产物，提出了催化机制。值得注意的是，即使考虑到 MnP 本身的纤维素分解活性，MnP 也能提高 CMC 和 Avicel® 上的纤维素酶活性。据作者所知，这是第一份报告，除了已知的脱木质素活性外，还证明了以前未知的真菌 MnP 在纤维素分解中的活性。因此，该结果为进一步研究木质素降解生物催化剂的多功能性提供了有希望的见解。