Thermophilic Chitinases: Structural, Functional and Engineering Attributes for Industrial Applications
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Thermophilic Chitinases: Structural, Functional and Engineering Attributes for Industrial Applications Gincy M Mathew 1 & Aravind Madhavan 2 & K. B. Arun 2 & Raveendran Sindhu 1 & Parameswaran Binod 1 & Reeta Rani Singhania 3 & Rajeev K Sukumaran 1 & Ashok Pandey 4,5 Received: 18 April 2020 / Accepted: 12 August 2020/ # Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract
Chitin is the second most widely found natural polymer next to cellulose. Chitinases degrade the insoluble chitin to bioactive chitooligomers and monomers for various industrial applications. Based on their function, these enzymes act as biocontrol agents against pathogenic fungi and invasive pests compared with conventional chemical fungicides and insecticides. They have other functional roles in shellfish waste management, fungal protoplast generation, and Single-Cell Protein production. Among the chitinases, thermophilic and thermostable chitinases are gaining popularity in recent years, as they can withstand high temperatures and maintain the enzyme stability for longer periods. Not all chitinases are thermostable; hence, tailor-made thermophilic chitinases are designed to enhance their thermostability by direct evolution, genetic engineering involving mutagenesis, and proteomics approach. Although research has been done extensively on cloning and expression of thermophilic chitinase genes, there are only few papers discussing on the mechanism of chitin degradation using thermophiles. The current review discusses the sources of thermophilic chitinases, improvement of protein stability by gene manipulation, metagenomics approaches, chitin degradation mechanism in thermophiles, and their prospective applications for industrial, agricultural, and pharmaceutical purposes. Keywords Thermostability . Chitinases . Chitin . Applications . Extremozymes
Introduction Thermophilic extremozymes are gaining wide interest globally over chemical catalysts due to their high tolerance and catalytic action at elevated temperatures. Predominantly, industries use chemical solvents that decrease the viscosity and elevate the diffusion content and reaction rate
* Ashok Pandey [email protected]; [email protected] Extended author information available on the last page of the article
Applied Biochemistry and Biotechnology
at high temperatures [1, 2]. The intrinsic properties of thermophilic enzymes are ideal in catalyzing chemical reactions at high temperatures. For industrial purposes, high temperatures can enhance the solubility of hydrophobic compounds, prevent contamination of microbes, and aid in the biodegradation process by environmentally friendly approaches. The microbial physiology of the thermophilic microbes, the nature of their enzyme catalytic center, and evolutionary diversity are helpful in protein engineering for industrial applications. Thermophiles are adapted to thrive at high-temperature sites like volcanic and geothermal springs [3]. Scientists are interested in unveiling the mysteries involved in the
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