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Thermophilic Chitinases: Structural, Functional and Engineering Attributes for Industrial Applications
Gincy M Mathew1, Aravind Madhavan2, K B Arun2
1Microbial Processes and Technology Division, CSIR-National Institute for Interdisciplinary Science and Technology, Trivandrum, 695 019, India.
Applied Biochemistry and Biotechnology
|August 23, 2020
Summary
Thermophilic chitinases offer enhanced stability for industrial applications. Research focuses on improving these enzymes through genetic engineering and exploring their mechanisms for biocontrol and waste management.
Area of Science:
- Biochemistry
- Enzymology
- Biotechnology
Background:
- Chitin, a prevalent biopolymer, requires degradation by chitinases for diverse applications.
- Chitinases serve as biocontrol agents and are crucial in waste management and protein production.
- Thermophilic chitinases exhibit superior stability at high temperatures, making them industrially valuable.
Purpose of the Study:
- To review sources and applications of thermophilic chitinases.
- To discuss methods for enhancing chitinase thermostability.
- To explore the chitin degradation mechanism in thermophiles.
Main Methods:
- Literature review of thermophilic chitinases.
- Analysis of protein engineering techniques for thermostability (direct evolution, mutagenesis, proteomics).
- Examination of metagenomics approaches for enzyme discovery.
Main Results:
- Thermophilic chitinases are sourced from various extremophiles.
- Genetic engineering and directed evolution significantly enhance enzyme stability.
- Metagenomics offers a powerful tool for discovering novel thermophilic chitinases.
Conclusions:
- Tailor-made thermophilic chitinases are essential for advanced industrial processes.
- Further research into degradation mechanisms will unlock new applications.
- These enzymes hold significant promise for agriculture, industry, and pharmaceuticals.
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