On the relationship between structure and catalytic effectiveness in solid surface-immobilized enzymes: Advances in methodology and the quest for a single-molecule perspective

Juan M. Bolivar, Bernd Nidetzky*

*Corresponding author for this work

Research output: Contribution to journalReview article

Abstract

The integration of enzymes with solid materials is important in many biotechnological applications, including the use of immobilized enzymes for biocatalytic synthesis. The development of functional enzyme-material composites is restrained by the lack of molecular-level insight into the behavior of enzymes in confined, surface-near environments. Here, we review recent advances in surface-sensitive spectroscopic techniques that push boundaries for the determination of enzyme structure and orientation at the solid-liquid interface. We discuss recent evidence from single-molecule studies showing that analyses sensitive to the temporal and spatial heterogeneities in immobilized enzymes can succeed in disentangling the effects of conformational stability and active-site accessibility on activity. Different immobilization methods involve distinct trade-off between these effects, thus emphasizing the need for a holistic (systems) view of immobilized enzymes for the rational development of practical biocatalysts.

Original languageEnglish
Article number140333
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1868
Issue number2
DOIs
Publication statusPublished - 1 Feb 2020

Keywords

  • Biocatalyst
  • Enzyme
  • Immobilization
  • Single-molecule analysis
  • Solid-liquid interface

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biophysics
  • Biochemistry
  • Molecular Biology

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