Min, K. Kim, Y.H. Kim, Ji ye Kim, Yunje Gong, Gyeong taek Um, Young soon 2024-01-19T13:02:30Z 2024-01-19T13:02:30Z 2022-01-10 2022-01 0960-8524 https://pubs.kist.re.kr/handle/201004/115899 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 MnII in acetate buffer evolves the MnIII-acetate complex functioning as a strong oxidant, and the non-specificity of MnIII-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. ？ 2021 Elsevier Ltd English Elsevier BV Effect of manganese peroxidase on the decomposition of cellulosic components: Direct cellulolytic activity and synergistic effect with cellulase Article 10.1016/j.biortech.2021.126138 1 Bioresource Technology, v.343 Bioresource Technology 343 N scie scopus 000719922100002 2-s2.0-85118502864 Agricultural Engineering Biotechnology & Applied Microbiology Energy & Fuels Agriculture Biotechnology & Applied Microbiology Energy & Fuels Article ENZYMATIC-HYDROLYSIS PHOSPHORIC ACID MN-PEROXIDASE DISSOLUTION INHIBITION CONVERSION CELLOBIOSE PATHWAYS ETHANOL BIOMASS Boosting cellulase activity Cellulose-decomposition Manganese peroxidase