AI Article Synopsis
- Thermomyces lanuginosus is a high-temperature-loving fungus that produces important enzymes, especially thermostable chitinases, which haven't been fully studied yet.
- This research focuses on cloning and characterizing a specific gene for thermostable chitinase II, revealing it encodes a protein made up of 343 amino acids.
- The study indicates that chitinase II has a distinctive TIM-barrel structure, with a key amino acid (Glu176) vital for its activity, and confirmed the protein's stability through molecular dynamics simulations.
Article Abstract
Thermomyces lanuginosus is a thermophilic fungus that produces large number of industrially-significant enzymes owing to their inherent stability at high temperatures and wide range of pH optima, including thermostable chitinases that have not been fully characterized. Here, we report cloning, characterization and structure prediction of a gene encoding thermostable chitinase II. Sequence analysis revealed that chitinase II gene encodes a 343 amino acid protein of molecular weight 36.65kDa. Our study reports that chitinase II exhibits a well-defined TIM-barrel topology with an eight-stranded α/β domain. Structural analysis and molecular docking studies suggested that Glu176 is essential for enzyme activity. Folding studies of chitinase II using molecular dynamics simulations clearly demonstrated that the stability of the protein was evenly distributed at 350K.
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| http://dx.doi.org/10.1016/j.jtbi.2015.03.035 | DOI Listing |
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