Salt-Switchable Artificial Cellulase Regulated by a DNA Aptamer

Mari Takahara, Geisa Aparecida Lopes Gonçalves Budinova, Hikaru Nakazawa, Yutaro Mori, Mitsuo Umetsu, Noriho Kamiya

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Abstract

A novel artificial cellulase was developed by conjugating a DNA aptamer to an endoglucanase catalytic domain, thereby substituting the natural carbohydrate-binding module. Circular dichroism spectroscopy and adsorption isotherm showed the binding motif of cellulose-binding DNA aptamer (CelApt) was G-quadruplex and stem-loop structures stabilized in the presence of salts, and CelApt binding preferred the amorphous region of the solid cellulose. By introducing the revealed salt-switchable cellulose-binding nature of CelApt into a catalytic domain of a cellulase, we created CelApt-catalytic domain conjugate possessing both controllable adsorption on the solid substrates and equal enzymatic activity to the wild-type cellulase. Thus potential use of a responsive DNA aptamer for biocatalysis at a solid surface was demonstrated.

Original languageEnglish
Pages (from-to)3356-3362
Number of pages7
JournalBiomacromolecules
Volume17
Issue number10
DOIs
Publication statusPublished - Oct 10 2016

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All Science Journal Classification (ASJC) codes

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

Cite this

Takahara, M., Budinova, G. A. L. G., Nakazawa, H., Mori, Y., Umetsu, M., & Kamiya, N. (2016). Salt-Switchable Artificial Cellulase Regulated by a DNA Aptamer. Biomacromolecules, 17(10), 3356-3362. https://doi.org/10.1021/acs.biomac.6b01141