Lignocellulosic (LC) biomass is the most abundant renewable resource for mankind gravitating society towards sustainable solution for energy that can reduce the carbon footprint. The economic feasibility of 'biomass biorefinery' depends upon the efficiency cellulolytic enzymes which is the main crux. Its high production cost and low efficiencies are the major limitations, that need to be resolved. As the complexity of the genome increases, so does the complexity of the proteome, further facilitated by protein post-translational modifications (PTMs). Glycosylation is regarded the major PTMs and hardly any recent work is focused on importance of glycosylation in cellulase. By modifying protein side chains and glycans, superior cellulases with improved stability and efficiency can be obtained. Functional proteomics relies heavily on PTMs because they regulate activity, localization, and interactions with protein, lipid, nucleic acid, and cofactor molecules. O- and N- glycosylation in cellulases influences its characteristics adding positive attributes to the enzymes.
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http://dx.doi.org/10.1016/j.biortech.2023.128992 | DOI Listing |
Front Fungal Biol
December 2024
Water Systems and Biotechnology Institute, Faculty of Natural Sciences and Technology, Riga Technical University, Riga, Latvia.
The growing demand for novel enzyme producers to meet industrial and environmental needs has driven interest in lignocellulose-degrading fungi. In this study, lignocellulolytic enzyme production capabilities of environmental fungal isolates collected from boreal coniferous and nemoral summer green deciduous forests were investigated, using Congo Red, ABTS, and Azure B as indicators of cellulolytic and ligninolytic enzyme productions. Through qualitative and quantitative assays, the study aimed to identify promising species for lignocellulose-degrading enzyme secretion and assess their potential for biotechnological applications.
View Article and Find Full Text PDFBioresour Technol
December 2024
Key Laboratory of Shandong Microbial Engineering, School of Bioengineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan, Shandong 250353, People's Republic of China; Department of Chemical and Petroleum Engineering, University of Calgary, 2500 University Drive, NW, Calgary, Alberta, Canada. Electronic address:
Low-cost production of cellulases is a key factor in advancing the commercialization of lignocellulosic biorefinery. Thus far, Trichoderma reesei is the leading cellulase producer for biorefinery applications. Over 70 years of research, considerable advancements have been made in comprehending the mechanisms underlying cellulases biosynthesis and secretion in T.
View Article and Find Full Text PDFEnzyme Microb Technol
December 2024
Department of Biotechnology, Lorena School of Engineering, University of São Paulo, Lorena, SP, Brazil. Electronic address:
β-glucosidases (BGLs) are key enzymes in the depolymerization of cellulosic biomass, catalyzing the conversion of cello-oligosaccharides into glucose. This conversion is pivotal for enhancing the production of second-generation ethanol or other value-added products in biorefineries. However, the process is often cost-prohibitive due to the high enzyme loadings required.
View Article and Find Full Text PDFCurr Microbiol
December 2024
Instituto de Microbiologia Paulo de Góes, Universidade Federal do Rio de Janeiro, Av. Carlos Chagas Filho, 373, Cidade Universitária, Rio de Janeiro, RJ, 21941-902, Brazil.
Microb Biotechnol
December 2024
Ocean Genome Legacy Center, Northeastern University, Nahant, Massachusetts, USA.
Teredinibacter turnerae is a cultivable cellulolytic Gammaproteobacterium (Cellvibrionaceae) that commonly occurs as an intracellular endosymbiont in the gills of wood-eating bivalves of the family Teredinidae (shipworms). The genome of T. turnerae encodes a broad range of enzymes that deconstruct cellulose, hemicellulose and pectin and contribute to wood (lignocellulose) digestion in the shipworm gut.
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