What is it about?
As a result of the recent advances and successes in the molecular modification of aspartic proteases, the goal of this review is to present an overview of engineered microbial aspartic proteases (EMAPs) including those that have been heterologously expressed and/or mutated as potential alternative for industries based on structural/molecular characterizations to increase productivity. However, there is no goal of exhausting the subject; rather, it is hoped to pique the scientific community’s interest in this technology, which is equally appealing to the industrial sector.
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Why is it important?
Molecular tools, functional genomics, and genome editing technologies coupled with other biotechnological approaches have aided in improving the potential of industrially important microbial proteases by addressing some of their major limitations, such as: low catalytic efficiency, low conversion rates, low thermostability, and less enzyme yield. However, the native folding within their full domain is dependent on a surrounding structure which challenges their functionality in substrate conversion, mainly due to their mutual interactions in the context of complex systems. Hence, manipulating their structure and controlling their expression systems could potentially produce enzymes with high selectivity and catalytic functions.
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This page is a summary of: Molecular modification and biotechnological applications of microbial aspartic proteases, Critical Reviews in Biotechnology, February 2023, Taylor & Francis, DOI: 10.1080/07388551.2023.2171850.
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