Thermostable cellulases: Structure, catalytic mechanisms, directed evolution and industrial implementations

Fatima Akram, Ikram ul Haq, Amna Aqeel, Zeeshan Ahmed and Fatima Iftikhar Shah

Renewable and Sustainable Energy Reviews, 2021, vol. 151, issue C

Abstract: From an anthropocentric point of view, human culture has been intricately involved in harnessing the potential of lignocellulosic feedstock to bring the bio-competitive alternative of fossil-based fuel resources. In today's scenario, the impact of hyperthermophiles and their enzymes has been intensely investigated for implementation in various high-temperature biotechnological processes. Already characterized archaeal and eubacterial cellulolytic glycoside hydrolase have shown highly impressive catalytic structures and mechanisms. Several sequence and structural factors have simultaneously been proposed to contribute towards the augmented stability of thermophilic proteins. However, state-of-the-art technologies like the rational designing approach and mechanism of directed evolution have emerged as critical toolkits for broadened industrial applications of recombinant proteins. This manuscript discusses the cellulase engineering techniques to enhance the biological production and stability of thermostable cellulolytic enzymes.

Keywords: Cellulases; Cellulosome; Lignocellulosic biomass; Protein engineering; Thermozymes (search for similar items in EconPapers)
Date: 2021
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DOI: 10.1016/j.rser.2021.111597

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