In Vivo Enzyme Entrapment in a Protein Crystal
| Autor: | Marianne M. Lee, Bradley S. Heater, Michael K. Chan, Zaofeng Yang |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
chemistry.chemical_classification
biology Nanoporous Chemistry General Chemistry 010402 general chemistry biology.organism_classification 01 natural sciences Biochemistry Proteus mirabilis Catalysis 0104 chemical sciences Entrapment Colloid and Surface Chemistry Enzyme Biocatalysis Bacillus thuringiensis biology.protein Lipase Thermostability |
| Zdroj: | Journal of the American Chemical Society. 142:9879-9883 |
| ISSN: | 1520-5126 0002-7863 |
| Popis: | Cry3Aa is a protein that forms crystals naturally in the bacterium Bacillus thuringiensis. Here we report that coexpression of Cry3Aa and a Proteus mirabilis lipase without recombinant fusion results in the efficient passive entrapment of the lipase within the nanoporous channels of the resulting crystals. This Cry3Aa crystal-mediated entrapment provides multiple benefits to the lipase including a high enzyme loading, significantly improved thermostability, increased proteolytic resistance, and the ability to be utilized as a recyclable biodiesel catalyst. These characteristics, along with its greatly simplified method of isolation, highlight the potential of Cry3Aa crystal-mediated enzyme entrapment for use in biocatalysis and other biotechnological applications. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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