Interplays of enzyme, substrate, and surfactant on hydrolysis of native lignocellulosic biomass
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Publication Details
Author list: Lee S., Akeprathumchai S., Bundidamorn D., Salaipeth L., Poomputsa K., Ratanakhanokchai K., Chang K.-L., Phitsuwan P.
Publisher: Taylor and Francis Group
Publication year: 2021
Volume number: 12
Issue number: 1
Start page: 5110
End page: 5124
Number of pages: 15
ISSN: 1949-1018
eISSN: 1949-1026
Languages: English-Great Britain (EN-GB)
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Abstract
Tracking enzyme, substrate, and surfactant interactions to reach maximum reducing sugar production during enzymatic hydrolysis of plant biomass may provide a better understanding of factors that limit the lignocellulosic material degradation in native rice straw. In this study, enzymes (Cellic Ctec2 cellulase and Cellic Htec2 xylanase) and Triton X-100 (surfactant) were used as biocatalysts for cellulose and xylan degradation and as a lignin blocking agent, respectively. The response surface model (R 2 = 0.99 and R 2-adj = 0.97) indicated that Cellic Ctec2 cellulase (p < 0.0001) had significant impacts on reducing sugar production, whereas Cellic Htec2 xylanase and Triton X-100 had insignificant impacts on sugar yield. Although FTIR analysis suggested binding of Triton X-100 to lignin surfaces, the morphological observation by SEM revealed similar surface features (i.e., smooth surfaces with some pores) of rice straw irrespective of Triton X-100. The reducing sugar yields from substrate hydrolysis with or without the surfactant were comparable, suggesting similar exposure of polysaccharides accessible to the enzymes. The model analysis and chemical and structural evidence suggest that there would be no positive effects on enzymatic hydrolysis by blocking lignins with Triton X-100 if high lignin coverage exists in the substrate due to the limited availability of hydrolyzable polysaccharides. © 2021 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.
Keywords
lignocellulosic material, Nonionic surfactant, nonproductive binding