Wang Wei, Gao Peiji
The State Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, The People's Republic of China.
Biodegradation. 2002;13(6):383-94. doi: 10.1023/a:1022848414100.
A special low-molecular-weight peptide named Gt factor, was isolated and purified from the extracellular culture of brown-rot fungi Gloeophyllum trabeum via gel filtration chromatography and HPLC. It has been shown to reduce Fe3+ to Fe2+. Electron paramagnetic resonance (EPR) spectroscopy revealed Gt factor was able to drive H2O2 generation via a superoxide anion O2*- intermediate and mediate the formation of hydroxyl radical HO* in the presence of O2. All the results indicated that Gt factor could oxidize the cellulose, disrupt the inter- and intrahydrogen bonds in cellulose chains by a HO*-involved mechanism. This resulted in depolymerization of the cellulose, which made it accessible for further enzymatic hydrolysis.
一种名为Gt因子的特殊低分子量肽,通过凝胶过滤色谱法和高效液相色谱法从褐腐真菌密粘褶菌的细胞外培养物中分离纯化得到。研究表明,它能将Fe3+还原为Fe2+。电子顺磁共振(EPR)光谱显示,Gt因子能够通过超氧阴离子O2*-中间体驱动H2O2的产生,并在有O2存在的情况下介导羟基自由基HO的形成。所有结果表明,Gt因子可以氧化纤维素,通过一种涉及HO的机制破坏纤维素链中的分子间和分子内氢键。这导致纤维素解聚,使其易于进行进一步的酶促水解。