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In recent years, biofuel or biogas have become the primary source of bio-energy, providing an alternative to conventionally used energy that can meet the growing energy demand for people all over the world while reducing greenhouse gas emissions. Enzyme hydrolysis in bioethanol production is a critical step in obtaining sugars fermented during the final fermentation process. More efficient enzymes are being researched to provide a more cost-effective technique during enzymatic hydrolysis. The exploitation of microbial catabolic biochemical reactions to produce electric energy can be used for complex renewable biomasses and organic wastes in microbial fuel cells. In hydrolysis methods, a variety of diverse enzyme strategies are used to promote efficient bioethanol production from various lignocellulosic biomasses like agricultural wastes, wood feedstocks, and sea algae. This paper investigates the most recent enzyme hydrolysis pathways, microbial fermentation, microbial fuel cells, and anaerobic digestion in the manufacture of bioethanol/bioenergy from lignocellulose biomass.
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http://dx.doi.org/10.1016/j.biortech.2023.128679 | DOI Listing |
Microbiol Spectr
September 2025
Division of Infectious Diseases, Department of Medicine, University of Texas at Tyler School of Medicine, Tyler, Texas, USA.
Despite the long therapy duration, the treatment outcomes for lung disease (MAB-LD) are very poor. β-Lactams are among the recommended drugs for the treatment of MAB-LD; however, they are prone to hydrolysis by MAB β-lactamase enzymes. Therefore, β-lactamase inhibitors have been developed to overcome this problem.
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September 2025
State Key Laboratory of Chemical Resource Engineering, Beijing University of Chemical Technology, Beijing, 100029, China.
Modifying cells to achieve desired functions has attracted extensive attention in bioengineering and bio-manufacturing. Approaches based on cell-surface engineering have the potential to endow cells with multiple functions and also create a protective shell around them. However, such shells are generally irreversible and lack functionality, leading to various drawbacks associated with irreversible dynamics.
View Article and Find Full Text PDFACS Catal
August 2025
Department of Chemistry, University of Southern California, Los Angeles, California 90089, United States.
Chlorinated hydrocarbons are widely used as solvents and synthetic intermediates, but their chemical persistence can cause hazardous environmental accumulation. Haloalkane dehalogenase from (DhlA) is a bacterial enzyme that naturally converts toxic chloroalkanes into less harmful alcohols. Using a multiscale approach based on the empirical valence bond method, we investigate the catalytic mechanism of 1,2-dichloroethane dehalogenation within DhlA and its mutants.
View Article and Find Full Text PDFBackgroundRAY1216 is an alpha-ketoamide-based peptide inhibitor of severe acute respiratory syndrome coronavirus type 2 (SARS-CoV-2) major protease (M). This study evaluated the absorption, distribution, metabolism and excretion of [C]-labelled RAY1216 by oral administration.Research design and methodsThis phase Ι study was designed to assess the pharmacokinetics, mass balance and metabolic pathways in 6 healthy Chinese adult men after a single fasting oral administration of 240 mL (containing 400 mg/100 μCi) [C] RAY1216.
View Article and Find Full Text PDFInt J Biol Macromol
September 2025
Department of Pharmaceutical Engineering, School of Engineering, China Pharmaceutical University, Nanjing, 211198, China; Engineering Research Center for Smart Pharmaceutical Manufacturing Technologies, Ministry of Education, China Pharmaceutical University, Nanjing, 211198, China. Electronic addres
1,3-Dioleoyl-2-palmitoylglycerol (OPO) is crucial for infant nutrition; however, conventional immobilized lipase requires high-purity enzymes, which increases costs and limits industrial scalability. Herein, Rhizomucor miehei lipase (RML) was immobilized on surface-modified magnetic nanoparticles using cross-linked enzyme aggregates (CLEAs) technology to produce FeO@SiO@TPOAC@RML CLEAs. This approach combines the separation and immobilization of enzymes, allowing for the use of lower-purity lipase, which enhances its suitability for industrial-scale processes.
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