Work

Analysis of β-glucosidase Mutant T352V

Year: 2025

Type: conference-paper

Abstract: This study looks at mutant T352V Β-glucosidase B (BglB). The mutant product was hypothesized to show reduced kinetic activity and thermostability compared to the wild-type. This was determined through modeling of the mutation using the FoldIt software. The protein was then purified and expressed through SDS-PAGE and Western Blotting. The results indicate that there was no production of a soluble protein. However, the Western Blot indicates the production of an insoluble protein. FoldIt modeling helps to explain the insoluble protein, as it indicates that the proximity of molecules without binding could cause aggregates to form inclusion bodies.

Source: Loyola eCommons (Loyola University of Chicago)

Authors: Ratz, John, Khan, Sufia

Language: English

Topic: Enzyme Production and Characterization

Subfield: Biotechnology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

OpenAlex ID: W6979926477

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