Two forms of α-L-fucosidase, deglycosylated and glycosylated, were found in the fucose-inducing culture broth of Fusarium oxysporum. Endo-β-N-acetylglucosaminidase was also found in the same culture broth. The deglycosylated α-L-fucosidase was purified from the culture broth to homogeneity on polyacrylamide disc gel electrophoresis and analytical ultracentrifugation. Purified deglycosylated α-L-fucosidase was compared in chemical composition and immunological homology with glycosylated α-L-fucosidase which had been reported previously (K. Yamamoto, Y. Tsuji, H. Kumagai, and T. Tochikura, Agric. Biol. Chem. 50:1689, 1986). Both enzymes had nearly the same amino acid compositions and were immunologically identical. Glycosylated α-L-fucosidase had mannose, galactose, and N-acetylglucosamine residues. In contrast, the deglycosylated enzyme had only N-acetylglucosamine residues. These results suggest that the deglycosylated α-L-fucosidase is formed by the release of sugar chains from the glycosylated form by Fusarium endo-β-N-acetylglucosaminidase. Furthermore, various enzymatic properties were compared: the two α-L-fucosidases were found to exhibit similar catalytic activities and thermal stability profiles. The deglycosylated enzyme, however, was slightly unstable in the acidic pH range compared with the glycosylated enzyme.
CITATION STYLE
Tsuji, Y., Yamamoto, K., & Tochikura, T. (1990). Formation of deglycosylated α-L-fucosidase by endo-β-N-acetylglucosaminidase in Fusarium oxysporum. Applied and Environmental Microbiology, 56(4), 928–933. https://doi.org/10.1128/aem.56.4.928-933.1990
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