Expression of Microbispora bispora Bgl B ..Beta..-D-Glucosidase in Streptomyces lividans

    Research output: Chapter in Book/Report/Conference proceedingChapter


    Active, thermostable Microbispora bispora Bgl B Beta-D-glucosidase was expressed in Streptomyces lividans TK24 cells transformed with plasmid pIJ702 carrying the bg/B coding sequence under the control of Streptomyces longisporus STI-II trypsin inhibitor promoter. The recombinant enzyme, SlBgl B, has a molecular weight of 54 kDa, an isoelectric pH of 5.0, shows resistance to glucose inhibition,and is optimally active on omicron-nitrophenyl Beta-D-glucopyranoside at 57 degrees C. This recombinant Beta-D-glucosidase was more active on aryl-glycosides than on cellobiose. We also report a successful mutagenesis strategy used to achieve increased levels of SlBgl B expression in this host organism. Screening mutants created by low fidelity PCR using Taq polymerase in the presence ofmanganese ion revealed a series of up-regulated clones, one yielding 235 mg/L of SlBgl B.
    Original languageAmerican English
    Title of host publicationFuels and Chemicals from Biomass
    Subtitle of host publicationACS Symposium Series 666
    EditorsB. C. Saha, J. Woodward
    PagesCha 9: 154-171
    StatePublished - 1997

    Bibliographical note

    Developed from a symposium sponsored by the Division of Biochemical Technology at the 211th National Meeting of the American Chemical Society, 24-29 March, 1996, New Orleans, Louisiana.

    NREL Publication Number

    • NREL/CH-580-20775


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