Background: Efficient hydrolysis of lignocellulosic materials to sugars for conversion to biofuels and chemicals is a key step in biorefinery. Designing an active saccharifying enzyme system with synergy among their components is considered a promising approach.
Results: In this study, a lignocellulose-degrading enzyme system of Chaetomium globosum BCC5776 (CG-Cel) was characterized for its activity and proteomic profiles, and synergism with accessory enzymes. The highest cellulase productivity of 0.40 FPU/mL was found for CG-Cel under the optimized submerged fermentation conditions on 1% (w/v) EPFB (empty palm fruit bunch), 2% microcrystalline cellulose (Avicel®) and 1% soybean meal (SBM) at 30 °C, pH 5.8 for 6 d. CG-Cel worked optimally at 50-60 °C in an acidic pH range. Proteomics analysis by LC/MS/MS revealed a complex enzyme system composed of core cellulases and accessory hydrolytic/non-hydrolytic enzymes attacking plant biopolymers. A synergistic enzyme system comprising the CG-Cel, a β-glucosidase (Novozyme® 188) and a hemicellulase Accellerase® XY was optimized on saccharification of alkaline-pretreated rice straw by a mixture design approach. Applying a full cubic model, the optimal ratio of ternary enzyme mixture containing CG-Cel: Novozyme® 188: Accellerase® XY of 44.4:20.6:35.0 showed synergistic enhancement on reducing sugar yield with a glucose releasing efficiency of 256.4 mg/FPU, equivalent to a 2.9 times compared with that from CG-Cel alone.
Conclusions: The work showed an approach for developing an active synergistic enzyme system based on the newly characterized C. globosum for lignocellulose saccharification and modification in bio-industries.
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http://dx.doi.org/10.1186/s12896-016-0312-7 | DOI Listing |
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Department of Life Sciences and Medicine (DLSM), University of Luxembourg, Belvaux, Luxembourg.
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Energy Systems Engineering Department, Engineering Faculty, Adana Alparslan Türkeş Science and Technology University, 01250, Adana, Türkiye.
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Adsorption and biodegradation are two important means to remove the pollutants from the environment, but how to combine them and improve the catalytic performance and stability of free enzyme are facing great challenges. Herein, lipase from Candida rugosa (CRL) was immobilized into bimetallic ZnCo-MOF by biomineralization, which not only significantly improved the catalytic activity and stability of CRL but also endowed it with excellent reusability. Furthermore, CRL@ZnCo-MOF established a synergetic system of combined adsorption and enzymatic degradation for the sustainable removal of dibutyl phthalate (DBP) in actual water environment.
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