木质素对生物质酶解抑制的机制。
Mechanism of lignin inhibition of enzymatic biomass deconstruction.
作者信息
Vermaas Josh V, Petridis Loukas, Qi Xianghong, Schulz Roland, Lindner Benjamin, Smith Jeremy C
机构信息
UT/ORNL Center for Molecular Biophysics, Oak Ridge National Laboratory, 37831 Oak Ridge, TN USA ; Center for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, 61801 Urbana, IL USA.
UT/ORNL Center for Molecular Biophysics, Oak Ridge National Laboratory, 37831 Oak Ridge, TN USA.
出版信息
Biotechnol Biofuels. 2015 Dec 21;8:217. doi: 10.1186/s13068-015-0379-8. eCollection 2015.
BACKGROUND
The conversion of plant biomass to ethanol via enzymatic cellulose hydrolysis offers a potentially sustainable route to biofuel production. However, the inhibition of enzymatic activity in pretreated biomass by lignin severely limits the efficiency of this process.
RESULTS
By performing atomic-detail molecular dynamics simulation of a biomass model containing cellulose, lignin, and cellulases (TrCel7A), we elucidate detailed lignin inhibition mechanisms. We find that lignin binds preferentially both to the elements of cellulose to which the cellulases also preferentially bind (the hydrophobic faces) and also to the specific residues on the cellulose-binding module of the cellulase that are critical for cellulose binding of TrCel7A (Y466, Y492, and Y493).
CONCLUSIONS
Lignin thus binds exactly where for industrial purposes it is least desired, providing a simple explanation of why hydrolysis yields increase with lignin removal.
背景
通过酶促纤维素水解将植物生物质转化为乙醇为生物燃料生产提供了一条潜在的可持续途径。然而，木质素对预处理生物质中酶活性的抑制严重限制了该过程的效率。
结果
通过对包含纤维素、木质素和纤维素酶（TrCel7A）的生物质模型进行原子细节分子动力学模拟，我们阐明了详细的木质素抑制机制。我们发现木质素优先结合到纤维素酶也优先结合的纤维素元素上（疏水表面），并且还结合到纤维素酶的纤维素结合模块上对TrCel7A的纤维素结合至关重要的特定残基上（Y466、Y492和Y493）。
结论
因此，木质素恰好结合在工业上最不需要的位置，这为为什么水解产率随木质素去除而增加提供了一个简单的解释。
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