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A novel immobilized cellulase based on hydrogel microsphere was established to accommodate ionic liquid (IL)-involved in situ biomass saccharification. For immobilization, poly(N-isopropylacrylamide) (PNIPAM) was employed to immobilize cellulase, with immobilization yielded up to 95.6%. Besides, 1-ethyl-3-methyllimidazolium acetate ([EMIM]OAc) was found as an appropriate IL for in situ saccharification due to its relative enzymatic activity, which was as high as 167.5%. With utilization of immobilized cellulase in IL-pretreated in situ bagasse (BC) saccharification, relative enzymatic activity was 40.9%, which was higher than free cellulase under 5% (v/v) IL, and achieved 12.3%, which was found to be higher than free one in 25% (v/v) IL. Moreover, for estimating reusability, relative enzymatic activity on the 6th cycle retained over 85.2%. This novel immobilization system possessed a remarkable preservation to cellulase in hydrolysis contained interferences, e.g. IL, suggesting a noticeable practical potential in hydrolysis of cost-effective sustainable biomass materials.
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http://dx.doi.org/10.1016/j.biortech.2019.122146 | DOI Listing |
Int J Biol Macromol
September 2025
Protein Research Department, Genetic Engineering and Biotechnology Research Institute (GEBRI), City of Scientific Research and Technological Applications (SRTA-City), New Borg El-Arab, Alexandria, 21934, Egypt. Electronic address:
The growing demand for sustainable agriculture imposes innovative biocontrol strategies to mitigate phytopathogen threats while reducing dependence on chemical pesticides. This review explores the current knowledge on enzyme-based biocontrol, focusing on hydrolytic enzymes (e.g.
View Article and Find Full Text PDFBraz J Microbiol
August 2025
Department of Food Engineering and Technology, Tezpur University, Assam, 784028, India.
This study investigates the immobilization of crude cellulase from Aspergillus foetidus, produced through solid-state fermentation by different methods, including entrapment in agar cube, adsorption on agar xerogel, and adsorption on agar xerogel pretreated with glutaraldehyde. The immobilization efficiency achieved was 90.80%, 84.
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 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.
View Article and Find Full Text PDFThe successful application of enzymes in industries encounters challenges related to high costs, stability, and reuse. In this study, β-glucosidase (BGL) was immobilized via a covalent method after the synthesis of different generations (G) of polyamidoamine (PAMAM) dendrimers modified magnetic spent coffee grounds (SCGs). With the increase in PAMAM generation, BGL immobilization (163.
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