Abstract

BackgroundLignin is known to hinder efficient enzymatic conversion of lignocellulose in biorefining processes. In particular, nonproductive adsorption of cellulases onto lignin is considered a key mechanism to explain how lignin retards enzymatic cellulose conversion in extended reactions.ResultsLignin-rich residues (LRRs) were prepared via extensive enzymatic cellulose degradation of corn stover (Zea mays subsp. mays L.), Miscanthus × giganteus stalks (MS) and wheat straw (Triticum aestivum L.) (WS) samples that each had been hydrothermally pretreated at three severity factors (log R0) of 3.65, 3.83 and 3.97. The LRRs had different residual carbohydrate levels—the highest in MS; the lowest in WS. The residual carbohydrate was not traceable at the surface of the LRRs particles by ATR-FTIR analysis. The chemical properties of the lignin in the LRRs varied across the three types of biomass, but monolignols composition was not affected by the severity factor. When pure cellulose was added to a mixture of LRRs and a commercial cellulolytic enzyme preparation, the rate and extent of glucose release were unaffected by the presence of LRRs regardless of biomass type and severity factor, despite adsorption of the enzymes to the LRRs. Since the surface of the LRRs particles were covered by lignin, the data suggest that the retardation of enzymatic cellulose degradation during extended reaction on lignocellulosic substrates is due to physical blockage of the access of enzymes to the cellulose caused by the gradual accumulation of lignin at the surface of the biomass particles rather than by nonproductive enzyme adsorption.ConclusionsThe study suggests that lignin from hydrothermally pretreated grass biomass retards enzymatic cellulose degradation by acting as a physical barrier blocking the access of enzymes to cellulose rather than by inducing retardation through nonproductive adsorption of enzymes.

Highlights

  • Lignin is known to hinder efficient enzymatic conversion of lignocellulose in biorefining processes

  • The adsorption reduced the free activity in the supernatant, the performance of the enzymes was not affected by the presence of lignin-rich residues (LRRs)

  • We suggest that the lignin surface coverage, plausibly due to its inherent physicochemical and structural properties, determines the degree of retardation of enzymatic cellulose degradation in lignocellulosic biomass feedstocks

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Summary

Introduction

Lignin is known to hinder efficient enzymatic conversion of lignocellulose in biorefining processes. Nonproductive adsorption of cellulases onto lignin is considered a key mechanism to explain how lignin retards enzymatic cellulose conversion in extended reactions. Hydrothermal pretreatment (HTP) and other types of physicochemical pretreatment methods are used to overcome the recalcitrance of the lignocellulosic biomass feedstocks to allow efficient enzymatic and biological processing [1, 2]. The presence of lignin in hydrothermally pretreated lignocellulosic biomass has been considered as an important limiting factor in the enzymatic hydrolysis of cellulose [4, 5]. Nonproductive adsorption of cellulases to lignin has been considered as a key factor that limits the enzymatic conversion of pretreated biomass [4, 6, 9]

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