Abstract
Thermophilic fungal cellulases are promising enzymes in protein engineering efforts aimed at optimizing industrial processes, such as biomass degradation and biofuel production. The cloning and expression in recent years of new cellulase genes from thermophilic fungi have led to a better understanding of cellulose degradation in these species. Moreover, crystal structures of thermophilic fungal cellulases are now available, providing insights into their function and stability. The present paper is focused on recent progress in cloning, expression, regulation, and structure of thermophilic fungal cellulases and the current research efforts to improve their properties for better use in biotechnological applications.
Highlights
Cellulose is one of the main components of plant cell wall material and is the most abundant and renewable nonfossil carbon source on Earth
This review aims at presenting up-to-date information on molecular, structural, genetic, and engineering aspects of thermophilic fungal cellulases and to highlight their potential in biotechnological applications
Purified thermophilic fungal cellulases have been characterized in terms of their molecular weight, optimal pH, optimal temperature, thermostability, and glycosylation
Summary
2. Cloning, Expression and Regulation of Cellulase Genes from Thermophilic Fungi. Potential regulatory element consensus sequences have been identified in the 5 upstream region of thermophilic fungal cellulase genes (6, 9, 13–15), and CREI genes from two thermophilic fungi (Talaromyces emersonii and Thermoascus aurantiacus) have been cloned (GenBank AF440004 and AY604200, resp.). It is, likely that cellulase gene regulation in thermophilic fungi may share certain similarities with T. reesei. Extensive glycosylation in recombinant enzymes could lead to reduced activity and increased non-productive binding on cellulose [29]
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