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Microbial cellulases that can be applied for lignocellulose saccharification have been extensively studied (Pavón-Orozco et al. 2012).
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The results of this study have provided novel thermostable archaeal cellulases that are stable up to at least 80 °C.
Table 2 shows a list of some industrially relevant thermostable cellulases that have been isolated and characterized.
F. succinogenes also appears to employ 'atypical' cellulases that may obviate the need for extensive CBMs [29].
Identified cellulolytic enzymes show low homology to cellulases from other organisms [29] and the F. succinogenes cellulases that have been cloned to date show poor performance on crystalline cellulose both alone and in combinations [29], [67].
Cellulases that are found in Nature vary considerably in their modular diversity and architecture.
Their substrate is cellobiose, which is soluble, unlike cellulases that degrade insoluble cellulose.
The short half-lives of T. reesei cellulases at temperatures above 50°C, together with very low expression levels of thermophilic cellulases (typically less than 100 mg/L, compared to over 150 gm/L for T. reesei cellulases) [ 6], motivates the development of thermostable T. reesei cellulases that can hydrolyze lignocellulose efficiently at temperatures beyond 50°C.
Among the cellulases that break down the polymeric cellulose are endoglucanases that act synergistically for subsequent hydrolytic reactions.
Besides Streptomyces, several other genera like Thermobifida and Micromonospora produce recombinant cellulases that can be commercially exploited [ 7].
These potential advantages motivate efforts to engineer T. reesei cellulases that can hydrolyze lignocellulose at temperatures ranging from 60 70°C.
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