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Microbial Cellulases and Their Industrial Applications

DOI: 10.4061/2011/280696

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Microbial cellulases have shown their potential application in various industries including pulp and paper, textile, laundry, biofuel production, food and feed industry, brewing, and agriculture. Due to the complexity of enzyme system and immense industrial potential, cellulases have been a potential candidate for research by both the academic and industrial research groups. Nowadays, significant attentions have been devoted to the current knowledge of cellulase production and the challenges in cellulase research especially in the direction of improving the process economics of various industries. Scientific and technological developments and the future prospects for application of cellulases in different industries are discussed in this paper. 1. Introduction Biotechnological conversion of cellulosic biomass is potentially sustainable approach to develop novel bioprocesses and products. Microbial cellulases have become the focal biocatalysts due to their complex nature and wide spread industrial applications. Cellulases are composed of independently folding, structurally and functionally discrete units called domains or modules, making cellulases module [1]. Cellulases are inducible enzymes synthesized by a large diversity of microorganisms including both fungi and bacteria during their growth on cellulosic materials (Table 1) [2, 3]. These microorganisms can be aerobic, anaerobic, mesophilic or thermophilic. Among them, the genera of Clostridium, Cellulomonas, Thermomonospora, Trichoderma, and Aspergillus are the most extensively studied cellulase producer [4–7]. Table 1: Microorganisms having cellulolytic abilities. Structurally fungal cellulases are simpler as compared to bacterial cellulase systems, cellulosomes [8–10]. Fungal cellulases typically have two separate domains: a catalytic domain (CD) and a cellulose binding module (CBM), which is joined by a short polylinker region to the catalytic domain at the N-terminal. The CBM is comprised of approximately 35 amino acids, and the linker region is rich in serine and threonine. The main difference between cellulosomes and free cellulase enzyme is in the component of cellulosomes-cohesin containing scaffolding and dockerin containing enzyme. The free cellulase contains cellulose binding domains (CBMs), which are replaced by a dockerin in cellulosomal complex, and a single scaffolding-born CBM directs the entire cellulosomes complex to cellulosic biomass [11, 12]. Mechanistically, cellulase is a family of at least 3 groups of enzymes [10, 13–15], endo-(1,4)-β-D-glucanase (EC 3.2.1.4)

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