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Expression and functional analysis of mouse chitinases without the ZZ domain of Staphylococcus aureus Protein A.
Int J Biol Macromol
January 2025
Division of Infectious Diseases and Immunology, Department of Microbiology, School of Medicine, Iwate Medical University, 1-1-1 Idaidori, Yahaba, Iwate 028-3694, Japan. Electronic address:
Chitinase plays a role in mammalian immune responses, particularly in the degradation of fungal cell walls. The aim of the present study was to express and characterize recombinant mouse chitotriosidase (Chit1) and acidic mammalian chitinase (AMCase) without the ZZ domain, a domain that may interfere with immunological analyses. We successfully expressed recombinant chitinases without the ZZ domain (Chit1-V5-His and AMCase-V5-His) as a soluble protein from an expression vector pET21a in the Escherichia coli Rosetta-gami B (DE3) strain.
View Article and Find Full Text PDFMolecular Dynamics Simulations Suggest That Side-Chain Motions of Charged Amino Acids Determine Long-Range Effects in Proteins: An Egg of Coulomb.
Int J Mol Sci
December 2024
Department of Biotechnology, Chemistry and Pharmacy, University of Siena, 53100 Siena, Italy.
Living systems cannot rely on random intermolecular approaches toward cell crowding, and hidden mechanisms must be present to favor only those molecular interactions required explicitly by the biological function. Electromagnetic messaging among proteins is proposed from the observation that charged amino acids located on the protein surface are mostly in adjacent sequence positions and/or in spatial proximity. Molecular dynamics (MD) simulations have been used to predict electric charge proximities arising from concerted motions of charged amino acid side chains in two protein model systems, human ubiquitin and the chitinolytic enzyme from .
View Article and Find Full Text PDFRecombinant expression and characterization of the family 5 cellulase from in BL21-CodonPlus (DE3)-RIPL.
Biochem Biophys Rep
March 2025
Institute of Biotechnology, Bioengineering and Food Systems, Advanced Engineering School, Far Eastern Federal University, Vladivostok, 690922, Russia.
B. velezensis RB. IBE29 is a chitinolytic bacterium originally isolated from agricultural soil of Vietnam.
View Article and Find Full Text PDFEnhanced chitinase production by Bacillus paralicheniformis GXMU-J23.1: Optimization, genomic insights, and chitin degradation mechanism.
Bioresour Technol
February 2025
Guangxi Key Laboratory for Polysaccharide Materials and Modifications, School of Marine Sciences and Biotechnology, Guangxi Minzu University, No. 158, Daxue Xi Road, Nanning 530008, PR China. Electronic address:
Article Synopsis
- Millions of tons of shrimp and crab waste generated each year contain chitin, which can be efficiently processed using a newly isolated strain of Bacillus paralicheniformis known as GXMU-J23.1.
- Genome sequencing of GXMU-J23.1 revealed various enzymes that break down chitin, including chitinase, which showed a significant increase in activity under optimal conditions.
- The isolated chitinase, Chi23, operates best at 50°C and pH 5.0, transforming chitin into simpler sugars and offering insights for future enzyme enhancements to improve chitin degradation processes.
Construction of Chitinase Complexes Using Self-Assembly Systems for Efficient Hydrolysis of Chitin.
ACS Synth Biol
December 2024
Laboratory of Applied Technology on Green-Eco-Healthy Animal Husbandry of Zhejiang Province, Zhejiang Provincial Engineering Research Center for Animal Health Diagnostics & Advanced Technology, Zhejiang International Science and Technology Cooperation Base for Veterinary Medicine and Health Management, China-Australia Joint Laboratory for Animal Health Big Data Analytics, College of Animal Science and Technology & College of Veterinary Medicine, Zhejiang A&F University, Hangzhou 311300, Zhejiang, China.
Chitin biomass is the second most abundant natural polysaccharide after cellulose on the earth, yet its recalcitrance to degrade and utilize severely limits its application. However, many microorganisms, such as , can secrete a range of free chitinases to degrade chitin, though their activity is typically insufficient to meet industrial demands. In this study, we employed self-assembly systems, named SpyTag/SpyCatcher and SnoopTag/SnoopCatcher, to modularize the molecular design of CHB, ChiB, ChiC, and CBP21 derived from ATCC14756, and we successfully constructed a variety of chitinase complexes.
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