Effect of alkali lignins with different molecular weights from alkali pretreated rice straw hydrolyzate on enzymatic hydrolysis. (January 2016)

• Record Type: Journal Article
• Authors: Li, Yun; Qi, Benkun; Luo, Jianquan; Wan, Yinhua
• Is Part Of: Bioresource technology. Volume 200(2016)
• Page Start: 272
• Page End: 278
• Publication Date: 2016-01
• Subjects: Alkali lignin -- Ultrafiltration -- Molecular weight -- Enzymatic hydrolysis -- Enzyme distribution; Biomass -- Periodicals; Biomass energy -- Periodicals; Bioremediation -- Periodicals; Agricultural wastes -- Periodicals; Factory and trade waste -- Periodicals; Organic wastes -- Periodicals; Bioénergie -- Périodiques; Déchets agricoles -- Périodiques; Déchets industriels -- Périodiques; Déchets organiques -- Périodiques; Déchets (Combustible) -- Périodiques; 662.88
• DOI: 10.1016/j.biortech.2015.10.038
• Languages: English
• ISSNs: 0960-8524

Abstract

Highlights: Alkali lignin from rice straw enhanced the enzymatic hydrolysis and enzyme activity. Alkali lignin with highest molecular weight showed the maximal enhancement. Surface charge and hydrophobicity of alkali lignin were responsible for the effects. Abstract: This study investigated the effect of alkali lignins with different molecular weights on enzymatic hydrolysis of lignocellulose. Different alkali lignins fractions, which were obtained from cascade ultrafiltration, were added into the dilute acid pretreated (DAP) and alkali pretreated (AP) rice straws respectively during enzymatic hydrolysis. The results showed that the addition of alkali lignins enhanced the hydrolysis and the enhancement for hydrolysis increased with increasing molecular weights of alkali lignins, with maximum enhancement being 28.69% for DAP and 20.05% for AP, respectively. The enhancement was partly attributed to the improved cellulase activity, and filter paper activity increased by 18.03% when adding lignin with highest molecular weight. It was found that the enhancement of enzymatic hydrolysis was correlated with the adsorption affinity of cellulase on alkali lignins, and the difference in surface charge and hydrophobicity of alkali lignins were responsible for the difference in affinity between cellulase and lignins.