Salt-Switchable Artificial Cellulase Regulated by a DNA Aptamer

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

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


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
Issue number10
Publication statusPublished - Oct 10 2016

All Science Journal Classification (ASJC) codes

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry


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