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The cost of enzymolysis is a major bottleneck for the industrialisation of lignocellulosic enzymatic hydrolysis technology, and recycling cellulase can reduce this cost. Herein, a sulfobetaine prepolymer (CPS) with terminal chlorine was grafted onto enzymatic hydrolysis residual lignin (EHL) from corncob to construct thermosensitive lignin-based "molecular glues" (lignin-based sulfobetaine polymers, L-CPS) that were used to recover and recycle cellulase. L-CPS (1.0 g/L) was added to the corncob residue (CCR) enzymolysis system (50 °C, pH 4.5). After hydrolysis, L-CPS co-precipitated with cellulase through hydrophobic binding when cooling to 25 °C. This co-precipitation decreased the amount of cellulase by 40 %. In summary, a thermally responsive lignin-based molecular glue was constructed for green recycling of cellulase, providing a new approach to decreasing the cost of lignocellulosic enzymolysis and high value utilisation of industrial lignin.
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http://dx.doi.org/10.1016/j.ijbiomac.2024.135474 | DOI Listing |
Int J Biol Macromol
September 2025
College of Textile Science and Engineering (International Institute of Silk), Zhejiang Sci-Tech University, Hangzhou 310018, China.
Recycling cellulase by using pH-responsive additives is an effective strategy for reducing the cost of lignocellulosic enzymatic hydrolysis. Traditional pH-responsive additives have limitations, including an insensitive pH response or weak binding to enzyme proteins, which restrict their industrial applications. The strong binding property of lignin to enzyme proteins was used to construct a series of ultra-high pH-responsive lignin-modified copolymers containing amide and carboxylic acid groups (L-CPM), which were obtained by using lignin cross-link pH-sensitive prepolymers containing amide and carboxylic acid groups (CPM).
View Article and Find Full Text PDFJ Biotechnol
July 2025
School of Chemistry and Chemical Engineering, Jiangsu University, Zhenjiang 212013, China. Electronic address:
In the field of biocatalysis, enzymes play a crucial role. However, they are faced with many challenges in practical applications, such as poor operational stability, high production costs and difficulties in recycling. Therefore, the efficient separation, purification and immobilization of enzymes are key to realize their industrial application.
View Article and Find Full Text PDFCurr Microbiol
July 2025
State Key Laboratory of Green Papermaking and Resource Recycling, School of bioengineering, Shandong Provincial Key Laboratory of Microbial Engineering, Qilu University of Technology, Shandong Academy of Sciences, Jinan, 250353, P. R. China.
Penicillium oxalicum is a filamentous fungus widely recognized for its robust production of cellulases. It features complex pathways that govern the triggered expression of these enzymes. Signal transduction serves a critical function in the effective management of cellulase induction and expression.
View Article and Find Full Text PDFSci Rep
July 2025
Department of Food Science, Faculty of Food and Consumer Sciences, Ladoke Akintola University of Technology, P.M.B. 4000, Ogbomoso, Oyo State, Nigeria.
Waste management and effluent treatment in bio-procedures are essential for maintaining a clean environment and enhancing the value of cassava waste. The study analysed effluents for biochemical oxygen demand (BOD) content and cyanide concentration (HCN), using activated charcoal, sand, and gravel as filter media. It also evaluated the enzymatic production of starch from cassava peels and fermentation with Aspergillus niger for citric acid production.
View Article and Find Full Text PDFJ Am Chem Soc
July 2025
Department of Chemical Sciences, Indian Institute of Science Education and Research, Mohanpur, Kolkata 741246, India.
Enzymes are powerful biocatalysts but suffer from a loss of activity under harsh conditions. In this study, we developed a one-pot aqueous synthesis of enzyme-encapsulated covalent organic frameworks (COFs) to enhance both the stability and reusability of enzymes and provided a detailed analysis of enzyme-COF interactions. We successfully encapsulated β-glucosidase (BGL), alkaline phosphatase (ALP), and eight other enzymes and proteins within the TpAzo COF.
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