Characterization of a Galactose Oxidase from Fusarium odoratissimum and Its Application in the Modification of Agarose.

ABSTRACT: A galactose oxidase gene, gao-5f, was cloned from Fusarium odoratissimum and successfully expressed in E. coli. The galactose oxidase GAO-5F belongs to the AA5 family and consists of 681 amino acids, with an estimated molecular weight of 72 kDa. GAO-5F exhibited maximum activity at 40 °C and pH 7.0 and showed no change in activity after 24 h incubation at 30 °C. Moreover, GAO-5F exhibited 40% of its maximum activity after 24 h incubation at 50 °C and 60% after 40 h incubation at pH 7.0. The measured thermostability of GAO-5F is superior to galactose oxidase's reported thermostability. The enzyme exhibited strict substrate specificity toward D-galactose and oligosaccharides/polysaccharides containing D-galactose. Further analysis demonstrated that GAO-5F specifically ox

SUBMITTER: Cao N 

PROVIDER: S-EPMC9914589 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature