Invertase from hyper producer strain of Aspergillus niger: physiochemical properties, thermodynamics and active site residues heat of ionization

Protein Pept Lett. 2009;16(9):1098-105. doi: 10.2174/092986609789055322. Epub 2009 Sep 1.

Abstract

Here we report for the first time heat of ionization of invertase (E.C.3.2.1.26) active site residues from hyper-producer strain of Aspergillus niger (34.1 U ml(-1)), along with its physiochemical properties, kinetics and thermodynamics of stability-function. The Invertase showed great potential for industry as being highly efficient (k(cat) = 24167 s(-1) at 65 degrees C, pH 5.0) and stable (half life= 12 h at 56 degrees C).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspergillus niger / enzymology*
  • Aspergillus niger / genetics
  • Catalytic Domain
  • Chemical Phenomena
  • Enzyme Stability
  • Kinetics
  • Temperature
  • Thermodynamics
  • beta-Fructofuranosidase / chemistry*
  • beta-Fructofuranosidase / genetics*
  • beta-Fructofuranosidase / isolation & purification
  • beta-Fructofuranosidase / metabolism

Substances

  • beta-Fructofuranosidase