Immobilization Increases the Stability and Reusability of Pigeon Pea NADP+ Linked Glucose-6-Phosphate Dehydrogenase

Protein J. 2017 Feb;36(1):49-55. doi: 10.1007/s10930-017-9702-5.

Abstract

Immobilization of enzymes is valuably important as it improves the stability and hence increases the reusability of enzymes. The present investigation is an attempt for immobilization of purified glucose-6-phosphate dehydrogenase from pigeon pea on different matrix. Maximum immobilization was achieved when alginate was used as immobilization matrix. As compared to soluble enzyme the alginate immobilized enzyme exhibited enhanced optimum pH and temperature. The alginate immobilized enzyme displayed more than 80% activity up to 7 continuous reactions and more than 50% activity up to 11 continuous reactions.

Keywords: Alginate; Enzyme; Glucose-6-phosphate dehydrogenase; Immobilization; Reusability.

MeSH terms

  • Alginates / chemistry*
  • Cajanus / enzymology*
  • Enzyme Stability
  • Enzymes, Immobilized / chemistry*
  • Glucosephosphate Dehydrogenase / chemistry*
  • Glucuronic Acid / chemistry
  • Hexuronic Acids / chemistry
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • NAD / chemistry*

Substances

  • Alginates
  • Enzymes, Immobilized
  • Hexuronic Acids
  • NAD
  • Glucuronic Acid
  • Glucosephosphate Dehydrogenase