Identification, Characterization, And Partial-Purification Of Glucoamylase From Aspergillus-Niger (Syn A-Ficuum) Nrrl-3135

    Authors

    A. S. Vandersall; R. G. Cameron; C. J. Nairn; G. Yelenosky;R. J. Wodzinski

    Comments

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    Abbreviated Journal Title

    Prep. Biochem.

    Keywords

    AMINO-ACID-SEQUENCE; POLYACRYLAMIDE-GEL ELECTROPHORESIS; 2 FORMS; BIOCHEMICAL-CHARACTERIZATION; MUCOR-ROUXIANUS; RAW-STARCH; PULLULANASE; PHOSPHATASE; ISOZYMES; CLONING; Biochemistry & Molecular Biology

    Abstract

    The crude extracellular extract of Aspergillus niger (syn A. ficuum) NRRL 3135 contains glucoamylase (exo-l,4-alpha-D-glucanohydrolase, EC 3.2.1.2). The enzyme, a glycoprotein, was purified 7-fold by ion-exchange chromatography, chromatofocusing, and conconavalin A affinity chromatography. The molecular weight of the enzyme was estimated to be 90 kDa by SDS-PAGE and gel permeation chromatography. The pi of the enzyme was 3.4. The temperature optimum of the enzyme was 60 degrees C and the pH optimum was 5.0. The V-max values for soluble starch, maltose, maltotriose, maltotetraose, maltopentaose, and isomaltose were 55.2, 11.7, 32.3, 47.8, 59.2, 12.5 nKat glucose/sec, respectively and the K-m values for the same substrates were 0.09%, 0.67 mM, 0.76 mM, 0.76 mM, 0.68 mM, and 122.01 mM, respectively.

    Journal Title

    Preparative Biochemistry

    Volume

    25

    Issue/Number

    1-2

    Publication Date

    1-1-1995

    Document Type

    Article

    Language

    English

    First Page

    29

    Last Page

    55

    WOS Identifier

    WOS:A1995QW28100004

    ISSN

    0032-7484

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