Comparison of nonproductive adsorption of cellulase onto lignin isolated from pretreated lignocellulose
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ORIGINAL RESEARCH
Comparison of nonproductive adsorption of cellulase onto lignin isolated from pretreated lignocellulose Mingfu Li . Liu Yi . Luo Bin . Qingtong Zhang . Junlong Song . Hongrui Jiang . Changzhou Chen . Shuangfei Wang . Douyong Min
Received: 26 February 2020 / Accepted: 16 July 2020 Ó Springer Nature B.V. 2020
Abstract Lignin, as a main factor inhibiting the enzymatic hydrolysis of lignocellulose, was investigated by comparing lignin isolated from untreated and pretreated lignocellulose to elucidate the differences in the enzyme adsorption ability. The nonproductive adsorption of cellulase on lignin was investigated by using a quartz crystal microbalance with dissipation. The results indicated that more cellulase adsorbed on the lignin isolated from autohydrolysis and green liquor-pretreated lignocellulose than on protolignin. Higher temperature and enzyme concentration increased the initial adsorption rate and the amount of enzyme adsorbed on lignin. A dynamic equation for enzyme adsorption on lignin was established. The adsorption of enzymes on lignin increased as the content of phenolic hydroxyl groups, and b-b and b-5 linkages in the lignin increased, attributed to enhanced
M. Li L. Yi L. Bin Q. Zhang H. Jiang C. Chen S. Wang D. Min (&) College of Light Industry and Food Engineering, Guangxi University, Nanning 530004, China e-mail: [email protected] M. Li L. Yi L. Bin Q. Zhang C. Chen S. Wang D. Min Guangxi Key Laboratory of Clean Pulp & Papermaking and Pollution Control, Guangxi University, Nanning 530004, China J. Song College of Light Industry and Food Engineering, Nanjing Forest University, Nanjing 210037, China
hydrogen bonding and hydrophobic interaction. Consequently, inhibition of the enzymatic hydrolysis of cellulose was promoted by a higher phenolic hydroxyl group, b-b, and b-5 content. The adsorption of the enzyme components on lignin followed the order: bglucosidase [ xylanase [ endo-glucanase [ cellobiohydrolase, as revealed by polyacrylamide gel electrophoresis analysis. Electrostatic interaction increased the adsorption of b-glucosidase and xylanase on lignin, while synergistic hydrophobic interaction and hydrogen bonding increased the adsorption of endo-glucanase and cellobiohydrolase on lignin. The results indicate that the adsorption of enzymes on lignin is affected by the structure of lignin and the composition of the enzymes. The findings of the current study provide fundamental knowledge for improving the enzymatic conversion of lignocellulose. Keywords Lignin Cellulase Adsorption Interaction QCM-D
Introduction Lignocellulosic biomass, a renewable biomaterial resource, has attracted interest from many researchers in various countries because of its wide distribution, abundance, and highly reproducible structure (Canilha et al. 2012). The main components of lignocellulose
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Cellulose
include cellulose, hemicellulose, and lignin which are used for producing ethanol, biodiesel, chem
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