Preprint Review Version 1 Preserved in Portico This version is not peer-reviewed

Heat Stability of Proteins and Its Exploitation for Purification of Heat-Stable Proteins

Version 1 : Received: 8 August 2020 / Approved: 9 August 2020 / Online: 9 August 2020 (22:00:46 CEST)

How to cite: Ahmad, M.; Tahir, A.; Salman Anjum, R. Heat Stability of Proteins and Its Exploitation for Purification of Heat-Stable Proteins. Preprints 2020, 2020080225 (doi: 10.20944/preprints202008.0225.v1). Ahmad, M.; Tahir, A.; Salman Anjum, R. Heat Stability of Proteins and Its Exploitation for Purification of Heat-Stable Proteins. Preprints 2020, 2020080225 (doi: 10.20944/preprints202008.0225.v1).

Abstract

Proteins possess complex three-dimensional structures, and these structures are stable only within specific ranges of temperature which mostly correspond to the temperature ranges of the host organisms. However, few exceptional proteins, called heat-stable proteins, are stable at temperatures that are substantially higher than those tolerated by the host organisms themselves. Most of the heat-stable proteins possess heat stability to perform their functions at high temperatures, but some of them are intrinsically heat-stable due to their structure. Heat-stable proteins are usually divided into three or four groups depending upon the intricacies of their structures and thermal behaviors. Their peculiar property, i.e. heat-stability, makes them very valuable in applications such as polymerase chain reaction, industrial processes requiring high temperature, and protein engineering. Heat-stability also makes it feasible to purify such proteins, from the rest of the heat-labile proteins, using a simple heat-treatment method. Moreover, heat treatment can be used as a combined cell-lysis and protein purification step which, as compared to conventional methods, can result in a higher yield of heat-stable proteins. Furthermore, some special heat-stable proteins, i.e. intrinsically disordered proteins (which include the proteins involved in important neurodegenerative diseases), need heat-treatment step, in some cases, as the only way for their successful purification and study. Hence, this paper provides a first-ever comprehensive review of all major aspects of heat-stable proteins, i.e., their structure, evolution, classification, significance, and heat-treatment mediated purification.

Subject Areas

Heat-stable proteins; Heat treatment; Hyperthermophilic proteins; Heat stability; Protein purification

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