Biomolecular Engineering, Bioengineering, Biochemicals, Biofuels, and Food

Sensitivity analysis of a proposed model mechanism for newly created glucose-6-oxidases

  1. Tae Seok Moon†,§,
  2. David R. Nielsen‡,§,
  3. Kristala L. Jones Prather*

Article first published online: 14 SEP 2011

DOI: 10.1002/aic.12762

Issue

AIChE Journal

AIChE Journal

Volume 58, Issue 8, pages 2303–2308, August 2012

Additional Information

How to Cite

Moon, T. S., Nielsen, D. R. and Prather, K. L. J. (2012), Sensitivity analysis of a proposed model mechanism for newly created glucose-6-oxidases. AIChE J., 58: 2303–2308. doi: 10.1002/aic.12762

Author Information

  1. Dept. of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139

  1. †

    Dept. of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139

  2. ‡

    Dept. of Chemical Engineering, Arizona State University, Tempe, AZ

  1. §

    Tae Seok Moon and David Nielsen contributed equally to the work.

*Dept. of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA

  1. §

    Tae Seok Moon and David Nielsen contributed equally to the work.

Publication History

  1. Issue published online: 5 JUL 2012
  2. Article first published online: 14 SEP 2011
  3. Accepted manuscript online: 23 AUG 2011 04:41PM EST
  4. Manuscript Revised: 31 JUL 2011
  5. Manuscript Received: 19 APR 2011

Funded by

  • Synthetic Biology Engineering Research Center (SynBERC)
  • National Science Foundation. Grant Number: EEC-0540879

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Keywords:

  • glucose oxidase;
  • galactose oxidase;
  • lag time;
  • kinetic mechanism;
  • sensitivity analysis;
  • mutagenesis

Abstract

Parametric sensitivity analysis of a proposed model mechanism can serve as a valuable diagnostic for studying the fundamental characteristics of an enzymatic reaction. As the first step toward understanding the kinetics of a series of newly engineered glucose-6-oxidases, the activity of which has never been found in nature, we have proposed a mechanistic kinetic model and performed a parametric sensitivity analysis. The mechanism of our model consists of two enzyme conformations, namely “less active” and “more active,” and is shown to be consistent with experimental observations of prolonged periods of enzyme induction. The extended lag phase phenomenon was found to be well described mechanistically by a slow rate of interconversion between the two enzyme conformations (relative to the rate of product formation), and this prediction was further supported by our experimental results. The proposed enzymatic model will serve as a blueprint with which to better understand the mechanistic behavior of newly generated glucose-6-oxidases. © 2011 American Institute of Chemical Engineers AIChE J, 58: 2303–2308, 2012

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