Cellobiohydrolases are enzymes that cleave off cellobiose units from cellulose chains in a processive manner. Melanocarpus albomyces Cel7B is a thermostable single-module cellobiohydrolase that has relatively low activity on small soluble substrates at room temperature. It belongs to glycoside hydrolase family 7, which includes endo-beta-1,4-glucanases and cellobiohydrolases. Cel7B was crystallized using the hanging-drop vapour-diffusion method and streak-seeding. The crystals belonged to space group P2(1), with unit-cell parameters a = 50.9, b = 94.5, c = 189.8 A, beta = 90.0 degrees and four monomers in the asymmetric unit. Analysis of the intensity statistics showed that the crystals were pseudo-merohedrally twinned, with a twinning fraction of 0.37. X-ray diffraction data were collected at 1.6 A resolution using synchrotron radiation.
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http://dx.doi.org/10.1107/S1744309107034458 | DOI Listing |
Environ Sci Pollut Res Int
December 2024
Faculty of Fundamental Sciences, Van Lang University, Ho Chi Minh City, Vietnam.
Polyethylene (PE), widely utilized in everyday life, is notorious for its protracted degradation period, extending over decades, presenting an environmental hazard. Recently, there has been growing interest in utilizing microorganisms to aid in PE decomposition. Molecular docking and molecular dynamics simulations are valuable tools for understanding specific mechanisms and conducting initial screenings to support experimental research in this context.
View Article and Find Full Text PDFJ Phys Chem B
September 2024
Chongqing Key Laboratory of Theoretical and Computational Chemistry, School of Chemistry and Chemical Engineering, Chongqing University, Chongqing 401331, P. R. China.
Laccases play a vital role in the degradation of toxic phenolic and aromatic amine compounds, generating considerable attention in ecological pollution remediation. However, the distinct mechanism of the laccase-catalyzed oxidation of phenols and arylamines remains unclear. Here, we examined the catalytic oxidation mechanisms of phenols and arylamines by (TvL) and (MaL) laccases using molecular docking, quantum mechanics (QM), and QM/molecular mechanics (QM/MM) calculations.
View Article and Find Full Text PDFJ Adv Vet Anim Res
March 2022
Department of Biochemistry and Microbiology, North South University, Dhaka, Bangladesh.
Objectives: The research aims to analyze the catabolic strength of different hydrolytic enzymes in assessing the biological conversion potential of lignocellulose parts of agricultural biomass wastes into functional edible sugars and biofuels.
Materials And Methods: The enzymes' hydrolytic properties-versatile peroxidase, manganese peroxidase, and lignin peroxidase were used to identify their complexing strength with the lignin substrate, whereas endoglucanase cel12A, acidocaldarius cellulase, and Melanocarpus albomyces endoglucanase were tested on the cellulose gel substrate. Because the biodegradation properties are heavily influenced by the "enzyme-substrate complexing energy level," proper molecular optimization and energy minimization of the enzymes and substrates were carried out, as well as the identification of the enzyme's active sites prior to complexing.
Cryobiology
August 2021
Kutahya Health Sciences University, Training and Research Center, 43100, Kutahya, Turkey. Electronic address:
Thermophilic fungi have several biotechnological and industrial applications such as thermostable enzyme production, biodegradation, and tobacco processing, etc. Thermophilic fungi cannot survive at temperatures below 20 °C. Owing to their inability to grow at low temperatures, they are not stable, so stocking is very difficult.
View Article and Find Full Text PDFChembiochem
June 2019
DWI Leibniz Institute for Interactive Materials, Forckenbeckstrasse 50, 52056, Aachen, Germany.
To date, commercial laccase preparations are used in the food, textile, and paper and pulp industries (mild pH). Laccases are attractive in the synthesis of dye molecules or oxidative lignin treatment, which take place at high pH (≥8.0).
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