Multiple display of catalytic modules on a protein scaffold: Nano-fabrication of enzyme particles

Arnon Heyman, Yoav Barak, Jonathan Caspi, David B. Wilson, Arie Altman, Edward A. Bayer, Oded Shoseyov*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

Self assembly is a prerequisite for fabricating nanoscale structures. Here we present a new fusion protein based on the stress-responsive homo-oligomeric protein, SP1. This ring-shaped protein is a highly stable homododecamer, which can be potentially utilized to self-assemble different modules and enzymes in a predicted and oriented manner. For that purpose, a cohesin module (a component of the bacterial cellulosome) was selected, its gene fused in-frame to SP1, and the fusion protein was expressed in Escherichia coli. The cohesin module, specialized to incorporate different enzymes through specific recognition of a dockerin modular counterpart, is used to display new moieties on the SP1 scaffold. The SP1 scaffold displayed 12 active cohesin modules and specific binding to a dockerin-fused cellulase enzyme from Thermobifida fusca. Moreover, we found a significant increase in specific activity of the scaffold-displayed enzymes.

Original languageAmerican English
Pages (from-to)433-439
Number of pages7
JournalJournal of Biotechnology
Volume131
Issue number4
DOIs
StatePublished - 30 Sep 2007

Bibliographical note

Funding Information:
This research was supported in part by a grant from the United States–Israel Binational Science Foundation (BSF), Jerusalem, Israel.

Keywords

  • Cohesin-dockerin recognition
  • Nano-bioreactor
  • Nano-fabrication
  • SP1
  • Scaffold
  • Self assembly

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