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

Can Cui, Cancan Yan, Ailin Wang, Cui Chen, Dan Chen, Shiwei Liu, Lu Li, Qiong Wu, Yue Liu, Yuxiang Liu, Genkuo Nie, Xiaoqing Jiang, Shuangxi Nie, Shuangquan Yao and Hailong Yu ()
Additional contact information
Can Cui: State Key Laboratory Base of Eco-Chemical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, 53# Zhengzhou Road, Qingdao 266042, China
Cancan Yan: State Key Laboratory Base of Eco-Chemical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, 53# Zhengzhou Road, Qingdao 266042, China
Ailin Wang: State Key Laboratory Base of Eco-Chemical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, 53# Zhengzhou Road, Qingdao 266042, China
Cui Chen: State Key Laboratory Base of Eco-Chemical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, 53# Zhengzhou Road, Qingdao 266042, China
Dan Chen: Qingdao High-Tech Industry Promotion Center, Qingdao 266540, China
Shiwei Liu: State Key Laboratory Base of Eco-Chemical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, 53# Zhengzhou Road, Qingdao 266042, China
Lu Li: State Key Laboratory Base of Eco-Chemical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, 53# Zhengzhou Road, Qingdao 266042, China
Qiong Wu: State Key Laboratory Base of Eco-Chemical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, 53# Zhengzhou Road, Qingdao 266042, China
Yue Liu: State Key Laboratory Base of Eco-Chemical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, 53# Zhengzhou Road, Qingdao 266042, China
Yuxiang Liu: State Key Laboratory Base of Eco-Chemical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, 53# Zhengzhou Road, Qingdao 266042, China
Genkuo Nie: State Key Laboratory Base of Eco-Chemical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, 53# Zhengzhou Road, Qingdao 266042, China
Xiaoqing Jiang: State Key Laboratory Base of Eco-Chemical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, 53# Zhengzhou Road, Qingdao 266042, China
Shuangxi Nie: Guangxi Key Laboratory of Clean Pulp and Papermaking and Pollution Control, College of Light Industry and Food Engineering, Guangxi University, 100# Daxue Road, Nanning 530004, China
Shuangquan Yao: Guangxi Key Laboratory of Clean Pulp and Papermaking and Pollution Control, College of Light Industry and Food Engineering, Guangxi University, 100# Daxue Road, Nanning 530004, China
Hailong Yu: State Key Laboratory Base of Eco-Chemical Engineering, College of Chemical Engineering, Qingdao University of Science and Technology, 53# Zhengzhou Road, Qingdao 266042, China

Sustainability, 2023, vol. 15, issue 7, 1-12

Abstract: 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.

Keywords: cellulase; corn stover; lignin adsorption; secondary structure; tryptophan residues (search for similar items in EconPapers)
JEL-codes: O13 Q Q0 Q2 Q3 Q5 Q56 (search for similar items in EconPapers)
Date: 2023
References: View references in EconPapers View complete reference list from CitEc
Citations: View citations in EconPapers (2)

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