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Author
Padilla Meza, Osman
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Abstract
Beta-glucosidase (β − glucosidase) is an enzyme which is widely distributed in three-domain system in Biology (Bacteria, Archaea and Eukaryota) and moreover, it is well-studied to play fundamental roles in many biological functions in the different organisms. Due to this, the enzyme has been attractive to many researchers for its many biotechnological applications. In biofuel, food and beverages, laundry and detergents, paper and pulp, and textile industries.
Though the β − glucosidase’s enzymatic activity is a limiting factor to satisfy the demand for their different products in the industry. Many investigations use enzyme engineering tools to enhance different properties of the enzyme such as activity, affinity, selectivity and stability by two well-stablished procedures: rational design and directed evolution.
Knowing the different biological roles and biotechnological applications where β−glucosidase is involved, this master thesis focuses specially on beta-glucosidase 3 from Streptomyces sp., better known as Bgl3 protein. In previous studies, the Bgl3 enzyme has been classified into the family 1 glycosyl hydrolase and it has been studied their different catalytic properties. Furthermore, it was identified different catalytic residues through bioinformatic studies to find a possible enzyme candidate to accept septanoses (seven-atom ring sugars) as natural substrate through enzyme engineering.
For what in recent years, septanose carbohydrates are being studied their protein-carbohydrate interactions, their role in biological systems and for their possible therapeutic applications. However, one of the inconvenient to study seven-atom ring sugars, they have not been detected yet in natural biological systems. So that, septanoses are produced by different chemical methods.
Due to this, the Bgl3 enzyme, it has been mutated and studied by rational design, in order to obtain information about the different substrate-enzyme interactions and the differential behavior that would lie in the respective active sites of the different proteins. And finally, it is wanted to propose a new enzyme candidate that could be capable to accept septanose carbohydrate as substrate.
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