Literature DB >> 16332903

Heterologous production of functional forms of Rhizopus oryzae lipase in Escherichia coli.

Mirella Di Lorenzo1, Aurelio Hidalgo, Michael Haas, Uwe T Bornscheuer.   

Abstract

To date, expression of the lipase from Rhizopus oryzae (ROL) in Escherichia coli always led to the formation of inclusion bodies and inactive protein. However, the production of active ROL and its precursor ProROL in soluble form was achieved when E. coli Origami(DE3) and pET-11d were used as expression systems.

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Year:  2005        PMID: 16332903      PMCID: PMC1317389          DOI: 10.1128/AEM.71.12.8974-8977.2005

Source DB:  PubMed          Journal:  Appl Environ Microbiol        ISSN: 0099-2240            Impact factor:   4.792


  17 in total

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9.  Expression of a Rhizopus oryzae lipase in Pichia pastoris under control of the nitrogen source-regulated formaldehyde dehydrogenase promoter.

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3.  Enhancement of the stability of a prolipase from Rhizopus oryzae toward aldehydes by saturation mutagenesis.

Authors:  Mirella Di Lorenzo; Aurelio Hidalgo; Rafael Molina; Juan A Hermoso; Domenico Pirozzi; Uwe T Bornscheuer
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6.  Gene Cloning, Heterologous Expression and Biochemical Characterization of A Novel Extracellular Lipase from Rhizopus Oryzae KU45.

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7.  Enhanced thermostability of a Rhizopus chinensis lipase by in vivo recombination in Pichia pastoris.

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8.  High-level expression of pro-form lipase from Rhizopus oryzae in Pichia pastoris and its purification and characterization.

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