Cloning and in silico study of an endoglucanase from a thermophilic bacterium isolated from a hydrothermal vent of West Kawio, Sangihe‐Talaud waters, North Sulawesi, Indonesia
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Edvan Arifsaputra Suherman(1*), Maelita Ramdani Moeis(2), Elvi Restiawaty(3)
(1) School of Life Sciences and Technology, Institut Teknologi Bandung, Jalan Ganesha 10, Bandung 40132, Indonesia
(2) School of Life Sciences and Technology, Institut Teknologi Bandung, Jalan Ganesha 10, Bandung 40132, Indonesia
(3) Department of Chemical Engineering, Institut Teknologi Bandung, Jalan Ganesha 10, Bandung 40132, Indonesia
(*) Corresponding Author
Abstract
Pro, and lower percentage of Gly compared to thermolabile endoglucanases from two Bacillus species. EgDSI2 harbored a catalytc domain belonging to glycosyl hydrolase family 9 (GH9) and a type 3 cellulose‐binding domain (CBM3). Propertes of endoglucanases with GH9‐CBM3 modular organizaton include actvity over a wide pH range, high optmum temperature, and thermostablity. Therefore, EgDSI2 has potental applicatons in the industries.
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