Comparison of glycosylation patterns of phytase from Aspergillus niger(A. Ficuum) NRRL 3135 and recombinant phytase

    Authors

    T. Panchal;R. J. Wodzinski

    Comments

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    Abbreviated Journal Title

    Prep. Biochem. Biotechnol.

    Keywords

    GLYCOPROTEIN; Biochemical Research Methods; Biochemistry & Molecular Biology; Biotechnology & Applied Microbiology

    Abstract

    The glycosylation patterns of phytase (E C 3.1.3.8) from Aspergillus niger NRRL 3135 with recombinant phytase from A. niger van Tieghem were compared. The following characteristics were studied: size of the whole molecule, type of linkage (N-linked or O-linked oligosaccharide), profile (number of different types of oligosaccharides present), monosaccharide composition, their order, and configuration. The molecular weights of both glycoproteins, after deglycosylation, was approximately 55 kDa as determined by SDS-PAGE. Both glycoproteins were about 35.29% glycosylated (calculations were made on the basis of 85 kDa molecular weight before deglycosylation). Only N-linked oligosaccharides were present. When N-linked oligosaccharides were released and labeled, the same profile was obtained for both glycoproteins. Mannose residues were detected after digestion by combinations of various exoglycosidases. N-acetylneuraminic acid, galactose, and N-acetylglucosamine residues were not detected. Released mannose residues were (alpha 1-2,3,6) linked. The trisaccharide core structure was nonfucosylated for all the oligosaccharides released from both glycoproteins. The only major difference found between the two glycoproteins was the migration pattern of oligosaccharide bands on gel after digestion with alpha-mannosidases. The structure of N-linked oligosaccharides ranged from (Man)(5)(GlcNAc)(2) to (Man)(10) (GlcNAc)(2).

    Journal Title

    Preparative Biochemistry & Biotechnology

    Volume

    28

    Issue/Number

    3

    Publication Date

    1-1-1998

    Document Type

    Article

    Language

    English

    First Page

    201

    Last Page

    217

    WOS Identifier

    WOS:000075731900001

    ISSN

    1082-6068

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