Biomass-binding peptides designed by molecular evolution for efficient degradation of cellulose in biomass by cellulase

Abstract

Molecular evolution was used to generate capping molecules that selectively bound to the noncellulose components in cellulosic biomass and facilitated access of cellulolytic enzymes to the substrate components. The peptides, which were selected by means of a phage-display method, strongly promoted the enzymatic degradation of cellulose components in the biomass.Scheme 1 Phage-displayed peptide library method used in this study. † Electronic supplementary information (ESI) available: Experimental procedures, adsorption isotherms against cellulose (Fig. S1), and peptide properties for identified biomass-binding peptides (Table S1). See

Toward a fundamental understanding of cellulase‐lignin interactions in the whole slurry enzymatic saccharification process

“…Enhancement of enzymatic digestion of plant biomass by three non‐glycoside hydrolase proteins were reported by Su et al These hydrolases are all small proteins heterologously produced in E. coli ., which indicates a promising direction for rational design of lignin‐blocking polypeptides. Nakazawa et al . designed and in vivo synthesized a series of capping peptides molecules by molecular evolution.…”

“…These artificial peptides showed higher affinity to the lignin‐rich biomass than to the native biomass or pure cellulose. The preferred peptide (SSLQAHKPHHLR) promoted the production of reducing sugars from acid pre‐treated grass by 90% which significantly surpassed that with addition of BSA as control . Another group identified the lignin‐binding peptides processing characteristic sequences of HFPSP based on the phage display technique .…”

Robust Surface Plasmon Resonance Chips for Repetitive and Accurate Analysis of Lignin–Peptide Interactions

“…17 On the other hand, the coexistence of lignin with cellulose and hemicelluloses is known to limit this conversion process severely by adsorbing or trapping the cellulase enzymes. 17−19 Considerable efforts have thus far been paid to study the interactions of lignin with proteins or peptides by highly sensitive SPR 20,21 and quartz crystal microbalance 22−24 sensor techniques in addition to conventional less sensitive methods, such as enzymatic reactions, 25−27 adsorption isotherms, 28−30 and potentiometric titrations. 31 However, lignins have usually been attached to sensor chips via physical adsorption; 32 consequently, undesired detachment of lignin from the sensor chip surface has impeded accurate analysis.…”

“…Lignin, cellulose, and hemicelluloses are primary components of lignocellulosic biomass and have gained considerable attention for their efficient and practical use as a renewable energy source and sustainable chemical feedstock. , In particular, enzymatic conversion of cellulose and hemicelluloses to ethanol has been recognized as a crucial technology to produce liquid fuels (bioethanol) free from the excessive use of fossil resources . On the other hand, the coexistence of lignin with cellulose and hemicelluloses is known to limit this conversion process severely by adsorbing or trapping the cellulase enzymes. − Considerable efforts have thus far been paid to study the interactions of lignin with proteins or peptides by highly sensitive SPR , and quartz crystal microbalance − sensor techniques in addition to conventional less sensitive methods, such as enzymatic reactions, − adsorption isotherms, − and potentiometric titrations . However, lignins have usually been attached to sensor chips via physical adsorption; consequently, undesired detachment of lignin from the sensor chip surface has impeded accurate analysis.…”

Design of Compact Biomimetic Cellulose Binding Peptides as Carriers for Cellulose Catalytic Degradation

“…To the best of our knowledge, this work represents the first successful rational design of a peptide-based carbohydrate binding mimetic. Few cellulose binding peptides were identified by phase display technologies. − …”