Abstract
BackgroundThe efficiency and cost of current lignocellulosic enzymes still limit the large-scale production of cellulosic ethanol in industry. Residual lignin after pretreatment severely depresses the activity of polysaccharide hydrolases and the h ydrolysis of holocellulose. If we include in hydrolase mixture construction the ligninase involved in lignin degradation, which mainly includes laccase, manganese peroxidases (MnP) and lignin peroxidase (LiP), it is feasible that this could greatly improve the fermentable sugars yield.ResultsThe psychrophilic lignocellulosic enzymes system of Cladosporium cladosporioides Ch2-2 including ligninase and polysaccharide hydrolases was suitable for selective delignification and efficient saccharification of biomass with wide thermal adaptability. The purified laccase was optimally active at 15°C and pH 3.5, exhibiting high thermostability over a broad range of temperatures (between 4 and 40°C). In addition, manganese-independent peroxidase (MIP), a special type of ligninase with the capacity to oxidize dimethyl phthalate (DMP) in the absence of H2O2 and Mn2+, was optimally active at 20°C and pH 2.5, exhibiting high thermostability over a broad range of temperatures (4 and 28°C), while depressed completely by Fe2+ and essentially unaffected by EDTA. Synergy between Ch2-2 crude enzymes and commercial xylanase obviously enhanced biomass hydrolysis, which could take the place of expensive commercial cellulase mixture. The maximum value of synergistic degree reached 4.7 at 28°C, resulting in 10.1 mg/mL reducing sugars.ConclusionsThe psychrophilic enzymes system of C. cladosporioides Ch2-2 with a different synergistic mechanism has huge potential for the enhancement of biomass hydrolysis at mesophilic and low temperatures. The application scope of the lignocellulosic enzyme cocktail could be greatly enlarged by optimizing the operation conditions specific to the characteristics of ligninase.
Highlights
The efficiency and cost of current lignocellulosic enzymes still limit the large-scale production of cellulosic ethanol in industry
From enzymatic characteristics of purified enzymes, we found that both laccase and manganese-independent peroxidase (MIP) from Ch2-2 exhibited substantially wide thermal adaptability in a mesophilic and psychrophilic environment, and MIP exhibited a special property that correlated with functional mechanism
The results indicate that crude enzymes mixture containing ligninase from C. cladosporioides Ch2-2 was able to enhance hydrolysis of other polysaccharide hydrolases significantly over a wide temperature range, which has a promising prospect for application in biomass degradation and high-value energy production at ambient temperature
Summary
The efficiency and cost of current lignocellulosic enzymes still limit the large-scale production of cellulosic ethanol in industry. Bagasse and Jerusalem artichoke stalks are both considered to be applicable for the large-scale biological production of cellulosic ethanol and other biobased chemicals. The low efficiency and high cost of existing enzymes converting lignocellulose to fermentable sugars still limit the large-scale industrialization of cellulosic ethanol at present. In this respect, the synergistic action of lignocellulosic enzymes has been recognized as a possible way to improve sugars yield at lower enzyme loadings [3]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
