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    A structure-activity understanding of the interaction between lignin and various cellulase domains

    Year: 2022

    Journal: Bioresour. Technol., Volume 351, MAY

    Authors: Zhao, Xiaoxue; Huang, Caoxing; Lin, Wenqian; Bian, Bin; Lai, Chenhuan; Ling, Zhe; Yong, Qiang

    Organizations: National Natural Science Foundation of China [31870569]; Priority Academic Program Development of Jiangsu Higher Education Institution (PAPD); Natural Science Foundation of Jiangsu Province for Youth [BK20200797]; National First-class Disciplines (PNFD)

    Keywords: Lignin; Endo-Cellulase; Carbohydrate-Binding Module; Interaction Mechanism; Fluorescence spectroscopy

    To elucidate the structure-activity relationship between lignin and various cellulase domains, four lignin fractions with specific structures and molecular weight were prepared from bamboo kraft lignin (BKL) and used to investigate the adsorption mechanism between different cellulase domains by fluorescence spectroscopy and SDS-PAGE. Endo-cellulase 6B exhibited a higher affinity to BKL fractions than the carbohydrate-binding module (CBM4A) of cellulase, which is positively correlated to molecular weight. The thermodynamic mechanism showed that the adsorption between BKL fractions and endo-cellulase 6B was dominated by van der Waals and electrostatic forces, while hydrophobic force is the driver for BKL fractions to adsorb CBM4A. Structure-activity relationship between lignin fractions and cellulase domain revealed that thermodynamics and interaction forces were more easily affected by the structure of BKL, including S/G ratio, molecular weight and hydrophobicity. The aforementioned results demonstrated that lignin's structure plays a critical role in its adsorption with various cellulase domains.
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