Applied Microbiology and Biotechnology

, Volume 78, Issue 6, pp 927–938

Glucose oxidase: natural occurrence, function, properties and industrial applications

Mini-Review

DOI: 10.1007/s00253-008-1407-4

Cite this article as:
Wong, C.M., Wong, K.H. & Chen, X.D. Appl Microbiol Biotechnol (2008) 78: 927. doi:10.1007/s00253-008-1407-4

Abstract

Glucose oxidase (GOX) from Aspergillus niger is a well-characterised glycoprotein consisting of two identical 80-kDa subunits with two FAD co-enzymes bound. Both the DNA sequence and protein structure at 1.9 Ǻ have been determined and reported previously. GOX catalyses the oxidation of d-glucose (C6H12O6) to d-gluconolactone (C6H10O6) and hydrogen peroxide. GOX is produced naturally in some fungi and insects where its catalytic product, hydrogen peroxide, acts as an anti-bacterial and anti-fungal agent. GOX is Generally Regarded As Safe, and GOX from A. niger is the basis of many industrial applications. GOX-catalysed reaction removes oxygen and generates hydrogen peroxide, a trait utilised in food preservation. GOX has also been used in baking, dry egg powder production, wine production, gluconic acid production, etc. Its electrochemical activity makes it an important component in glucose sensors and potentially in fuel cell applications. This paper will give a brief background on the natural occurrence, functions as well as the properties of glucose oxidase. A good coverage on the diverse uses of glucose oxidase in the industry is presented with a brief outline on the working principles in the various settings. Furthermore, food grade GOX preparations are relatively affordable and widely available; the readers may be encouraged to explore other potential uses of GOX. One example is that GOX-catalysed reaction generates significant amount of heat (∼200 kJ/mol), and this property has been mostly neglected in the various applications described so far.

Keywords

Glucose oxidaseIndustrial applicationsAspergillus nigerFood processingAdditiveEnzymePropertiesOccurrenceFunctions

Copyright information

© Springer-Verlag 2008

Authors and Affiliations

  1. 1.Department of Chemical Engineering, Biotechnology & Food Engineering GroupMonash UniversityMelbourneAustralia
  2. 2.P.O. Box 109175, NewmarketAucklandNew Zealand