Understanding the Inhibition Mechanism of Lignin Adsorption to Cellulase in Terms of Changes in Composition and Conformation of Free Enzymes

被引:3
作者
Cui, Can [1 ]
Yan, Cancan [1 ]
Wang, Ailin [1 ]
Chen, Cui
Chen, Dan [2 ]
Liu, Shiwei [1 ]
Li, Lu [1 ]
Wu, Qiong [1 ]
Liu, Yue [1 ]
Liu, Yuxiang [1 ]
Nie, Genkuo [1 ]
Jiang, Xiaoqing [1 ]
Nie, Shuangxi [3 ]
Yao, Shuangquan [3 ]
Yu, Hailong [1 ,3 ]
机构
[1] Qingdao Univ Sci & Technol, Coll Chem Engn, State Key Lab Base Ecochem Engn, 53 Zhengzhou Rd, Qingdao 266042, Peoples R China
[2] Qingdao High Tech Ind Promot Ctr, Qingdao 266540, Peoples R China
[3] Guangxi Univ, Coll Light Ind & Food Engn, Guangxi Key Lab Clean Pulp & Papermaking & Pollut, 100 Daxue Rd, Nanning 530004, Peoples R China
基金
中国国家自然科学基金;
关键词
cellulase; corn stover; lignin adsorption; secondary structure; tryptophan residues; BINDING; HYDROLYSIS;
D O I
10.3390/su15076057
中图分类号
X [环境科学、安全科学];
学科分类号
08 ; 0830 ;
摘要
The adsorption of lignin to cellulase is the major obstacle in the sugar-platform conversion of lignocellulosic bioresources. In this study, the adsorption behavior of untreated and pretreated lignin samples from corn stover to cellulase was investigated, in particular the effects of lignin adsorption on the composition and spatial conformation of free enzymes were explored. The results showed that pretreatments decreased the hydrophobic groups contents of lignin, i.e., aromatic ring, ether and carbonyl, as well as the content of ionizable group, i.e., carboxyl, which reduced its hydrophobicity and negative charge density, thus weakening the adsorption ability of lignin to cellulase. The lignin samples mainly adsorbed the CBHII component of cellulase to inhibit the synergistic effect of free enzymes. Lignin adsorption altered the spatial position of tryptophan residues in free enzymes, exposing them to the protein surface. In addition, the secondary structure of free enzymes was altered, with a decrease in the alpha-helix content and an increase in the random coil content, thus loosening the spatial conformation of free enzymes. The change degree in the spatial structure of free enzymes correlated with the adsorption capacity of the lignin, i.e., lignin with low adsorption capacity caused the least damage to free enzyme, with NaOH pretreated lignin being the best. It appears that appropriate pretreatment and chemical modification of enzymes to resist lignin adsorption is a promising long-term pathway to overcome the lignin inhibition during sugar-platform conversion of lignocellulosic bioresources.
引用
收藏
页数:12
相关论文
共 27 条
[1]   Exploring the Mechanism of Fluorescence Quenching in Proteins Induced by Tetracycline [J].
Anand, Uttam ;
Jash, Chandrima ;
Boddepalli, Ravi Kiran ;
Shrivastava, Aseem ;
Mukherjee, Saptarshi .
JOURNAL OF PHYSICAL CHEMISTRY B, 2011, 115 (19) :6312-6320
[2]   Agricultural waste biorefinery development towards circular bioeconomy [J].
Awasthi, Mukesh Kumar ;
Sindhu, Raveendran ;
Sirohi, Ranjna ;
Kumar, Vinod ;
Ahluwalia, Vivek ;
Binod, Parameswaran ;
Juneja, Ankita ;
Kumar, Deepak ;
Yan, Binghua ;
Sarsaiya, Surendra ;
Zhang, Zengqiang ;
Pandey, Ashok ;
Taherzadeh, Mohammad J. .
RENEWABLE & SUSTAINABLE ENERGY REVIEWS, 2022, 158
[3]   Improving Enzymatic Saccharification and Ethanol Production from Hardwood by Deacetylation and Steam Pretreatment: Insight into Mitigating Lignin Inhibition [J].
Chu, Qiulu ;
Wang, Rui ;
Tong, Wenyao ;
Jin, Yongcan ;
Hu, Jinguang ;
Song, Kai .
ACS SUSTAINABLE CHEMISTRY & ENGINEERING, 2020, 8 (49) :17967-17978
[4]   Lignin-derived inhibition of monocomponent cellulases and a xylanase in the hydrolysis of lignocellulosics [J].
Kellock, Miriam ;
Rahikainen, Jenni ;
Marjamaa, Kaisa ;
Kruus, Kristiina .
BIORESOURCE TECHNOLOGY, 2017, 232 :183-191
[5]   Soluble inhibitors/deactivators of cellulase enzymes from lignocellulosic biomass [J].
Kim, Youngmi ;
Ximenes, Eduardo ;
Mosier, Nathan S. ;
Ladisch, Michael R. .
ENZYME AND MICROBIAL TECHNOLOGY, 2011, 48 (4-5) :408-415
[6]   The Effect of Isolated Lignins, Obtained From a Range of Pretreated Lignocellulosic Substrates, on Enzymatic Hydrolysis [J].
Nakagame, Seiji ;
Chandra, Richard P. ;
Saddler, Jack N. .
BIOTECHNOLOGY AND BIOENGINEERING, 2010, 105 (05) :871-879
[7]   The Tryptophan Residue at the Active Site Tunnel Entrance of Trichoderma reesei Cellobiohydrolase Cel7A Is Important for Initiation of Degradation of Crystalline Cellulose [J].
Nakamura, Akihiko ;
Tsukada, Takeshi ;
Auer, Sanna ;
Furuta, Tadaomi ;
Wada, Masahisa ;
Koivula, Anu ;
Igarashi, Kiyohiko ;
Samejima, Masahiro .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2013, 288 (19) :13503-13510
[8]   Contribution of hydrogen bonds to protein stability [J].
Pace, C. Nick ;
Fu, Hailong ;
Fryar, Katrina Lee ;
Landua, John ;
Trevino, Saul R. ;
Schell, David ;
Thurlkill, Richard L. ;
Imura, Satoshi ;
Scholtz, J. Martin ;
Gajiwala, Ketan ;
Sevcik, Jozef ;
Urbanikova, Lubica ;
Myers, Jeffery K. ;
Takano, Kazufumi ;
Hebert, Eric J. ;
Shirley, Bret A. ;
Grimsley, Gerald R. .
PROTEIN SCIENCE, 2014, 23 (05) :652-661
[9]   Changes of the surface structure of corn stalk in the cooking process with active oxygen and MgO-based solid alkali as a pretreatment of its biomass conversion [J].
Pang, Chunsheng ;
Xie, Tujun ;
Lin, Lu ;
Zhuang, Junping ;
Liu, Ying ;
Shi, Jianbin ;
Yang, Qiulin .
BIORESOURCE TECHNOLOGY, 2012, 103 (01) :432-439
[10]   Multiple Functions of Aromatic-Carbohydrate Interactions in a Processive Cellulase Examined with Molecular Simulation [J].
Payne, Christina M. ;
Bomble, Yannicki ;
Taylor, Courtney B. ;
McCabe, Clare ;
Himmel, Michael E. ;
Crowley, Michael F. ;
Beckham, Gregg T. .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2011, 286 (47) :41028-41035