Purification and biochemical characterization of two extracellular peroxidases from Phanerochaete chrysosporium responsible for lignin biodegradation

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• 作者：Guang-Ming Zeng ; Mei-Hua Zhao ; Dan-Lian Huang ; Cui Lai ; Chao Huang ; Zhen Wei ; Piao Xu ; Ning-Jie Li ; Chen Zhang ; Fang-Ling Li ; Min Cheng
• 关键词：Purification ; Enzymes ; Phanerochaete chrysosporium ; Characterization ; Lignin ; Biodegradation
• 刊名：International Biodeterioration and Biodegradation
• 出版年：November, 2013
• 年：2013
• 卷：85
• 期：Complete
• 页码：166-172
• 全文大小：825 K

文摘

Two extracellular peroxidases from Phanerochaete chrysosporium, namely a lignin peroxidase (LiP) and manganese peroxidase (MnP), were purified simultaneously by applying successively, ultrafiltration, ion-exchange and gel filtration chromatography. LiP and MnP have a molecular mass of 36 and 45聽kDa, respectively. The optimal pHs for LiP and MnP activities were 3.0 and 4.5, respectively. Both peroxidases showed maximal activity at 30聽掳C and moderate thermostability. MnP activity was strongly inhibited by Fe²⁺, Zn²⁺, Mg²⁺ and Hg²⁺, and enhanced by Mn²⁺, Ca²⁺ and Cu²⁺. LiP activity was enhanced by Ca²⁺, Na⁺ and Co²⁺ and it was inhibited in the presence of K⁺, Hg⁺, Fe²⁺, Mg²⁺ and high concentrations of Cu²⁺ and Zn²⁺. The K_m and V_max for LiP toward veratryl alcohol as a substrate were 0.10聽mM and 15.2聽U聽mg^鈭?, respectively and for MnP toward Mn²⁺, they were respectively 0.03聽mM and 25.5聽U聽mg^鈭?. The two peroxidases were also able to break down rice lignin in a small-scale solid state treatment system. Data suggest these two peroxidases may be considered as potential candidates for the development of enzyme-based technologies for lignin degradation.