In Vivo Enzyme Entrapment in a Protein Crystal | Zendy

Bradley S. Heater | Zendy; Zaofeng Yang | Zendy; Marianne M. Lee | Zendy; Michael K. Chan | Zendy

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In Vivo Enzyme Entrapment in a Protein Crystal

Author(s) -

Bradley S. Heater,

Zaofeng Yang,

Marianne M. Lee,

Michael K. Chan

Publication year - 2020

Publication title -

journal of the american chemical society

Language(s) - Uncategorized

Resource type - Journals

SCImago Journal Rank - 7.115

H-Index - 612

eISSN - 1520-5126

pISSN - 0002-7863

DOI - 10.1021/jacs.9b13462

Subject(s) - chemistry , thermostability , lipase , protein crystallization , biocatalysis , bacillus thuringiensis , enzyme , nanoporous , entrapment , immobilized enzyme , biochemistry , bacteria , catalysis , crystallization , organic chemistry , medicine , ionic liquid , surgery , biology , genetics

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.

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