Oxidation with galactose oxidase: multifunctional enzymatic catalysis

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Abstract

Galactose oxidase (EC 1.1.3.9) is a single copper metalloenzyme, having a molecular weight of 65–68 kDa. Galactose oxidase catalyzes the oxidation of primary alcohols to corresponding aldehydes with strict regioselectivity, and the selectivity is high for the galactose C-6 primary hydroxyl group. The oxidation of alcohols to carbonyl compounds is one of the most important reactions in synthetic chemistry, thus enzymatic biocatalysis requiring only molecular oxygen as an oxidant is a valuable alternative to chemical reagents.

We review here the various mono-, oligo- and polysaccharide derivatives that have been synthesized by galactose oxidase-catalyzed reactions, and the several either qualitative or quantitative analytical techniques utilized to follow of the reaction, determine the conversion, and identify the products. The optimal reaction conditions, the formation of side products, and the oxidation of substrates other than carbohydrates are discussed. Finally, we summarize engineering efforts of galactose oxidase that have improved recombinant enzyme expression and yield, or altered substrate specificity.
Original languageEnglish
JournalJournal of Molecular Catalysis B: Enzymatic
Volume120
Pages (from-to)47-59
Number of pages13
ISSN1381-1177
DOIs
Publication statusPublished - 2015
MoE publication typeA1 Journal article-refereed

Fields of Science

  • 220 Industrial biotechnology
  • 116 Chemical sciences

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