Gelatin and Starch: What Better Stabilizes the Enzyme Activity?

Dokl Biol Sci. 2020 Mar;491(1):43-46. doi: 10.1134/S0012496620020039. Epub 2020 Jun 1.

Abstract

The regularities of the functioning of a number of enzymes in a viscous environment created by natural polymers, starch and gelatin are examined. Based on the analysis of kinetic curves of thermal inactivation, mechanisms of thermal inactivation of enzymes in a viscous microenvironment are proposed. Using the example of butyrylcholinesterase, NAD(P)H:FMN oxidoreductase, and coupled system of the luminous bacteria (NAD(P)H:FMN oxidoreductase + luciferase), the conditions, under which starch and gelatin have a stabilizing effect on enzyme activity during storage and exposure to various physical and chemical environmental factors, were found. A significant increase in the stabilizing effect is achieved by eliminating water during drying the enzyme preparations immobilized in starch and gelatin polymer gels.

Keywords: NAD(P)H:FMN oxidoreductase; butyrylcholinesterase; enzyme stabilization; gelatin; luciferase; starch; thermal inactivation of enzymes.

MeSH terms

  • Butyrylcholinesterase / chemistry
  • Butyrylcholinesterase / metabolism
  • Enzyme Stability
  • Enzymes / chemistry*
  • Enzymes / metabolism
  • FMN Reductase / chemistry
  • FMN Reductase / metabolism
  • Gelatin / chemistry*
  • Gels / chemistry
  • Kinetics
  • Luciferases / chemistry
  • Luciferases / metabolism
  • NAD / chemistry
  • NAD / metabolism
  • Starch / chemistry*

Substances

  • Enzymes
  • Gels
  • NAD
  • Gelatin
  • Starch
  • Luciferases
  • FMN Reductase
  • Butyrylcholinesterase