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Formation of deglycosylated alpha-L-fucosidase by endo-beta-N-acetylglucosaminidase in Fusarium oxysporum

Two forms of alpha-L-fucosidase, deglycosylated and glycosylated, were found in the fucose-inducing culture broth of Fusarium oxysporum. Endo-beta-N-acetylglucosaminidase was also found in the same culture broth. The deglycosylated alpha-L-fucosidase was purified from the culture broth to homogeneit...

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Bibliographic Details
Published in:Applied and Environmental Microbiology 1990-04, Vol.56 (4), p.928-933
Main Authors: Tsuji, Y. (Institute of Soysauce, Tatsuno, Hyogo), Yamamoto, K, Tochikura, T
Format: Article
Language:English
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Summary:Two forms of alpha-L-fucosidase, deglycosylated and glycosylated, were found in the fucose-inducing culture broth of Fusarium oxysporum. Endo-beta-N-acetylglucosaminidase was also found in the same culture broth. The deglycosylated alpha-L-fucosidase was purified from the culture broth to homogeneity on polyacrylamide disc gel electrophoresis and analytical ultracentrifugation. Purified deglycosylated alpha-L-fucosidase was compared in chemical composition and immunological homology with glycosylated alpha-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 alpha-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 alpha-L-fucosidase is formed by the release of sugar chains from the glycosylated form by Fusarium endo-beta-N-acetylglucosaminidase. Furthermore, various enzymatic properties were compared: the two alpha-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
ISSN:0099-2240
1098-5336
DOI:10.1128/aem.56.4.928-933.1990