Identification, Characterization, And Partial-Purification Of Glucoamylase From Aspergillus-Niger (Syn A-Ficuum) Nrrl-3135
Abbreviated Journal Title
AMINO-ACID-SEQUENCE; POLYACRYLAMIDE-GEL ELECTROPHORESIS; 2 FORMS; BIOCHEMICAL-CHARACTERIZATION; MUCOR-ROUXIANUS; RAW-STARCH; PULLULANASE; PHOSPHATASE; ISOZYMES; CLONING; Biochemistry & Molecular Biology
The crude extracellular extract of Aspergillus niger (syn A. ficuum) NRRL 3135 contains glucoamylase (exo-l,4-alpha-D-glucanohydrolase, EC 220.127.116.11). 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.
"Identification, Characterization, And Partial-Purification Of Glucoamylase From Aspergillus-Niger (Syn A-Ficuum) Nrrl-3135" (1995). Faculty Bibliography 1990s. 3020.