title: Production and purification of a granular-starch-binding domain of glucoamylase 1 from Aspergillus niger.
abstract: A domain of glucoamylase 1 from Aspergillus niger which binds to granular starch was produced by proteolytic digestion and purified to apparent homogeneity by extraction with corn starch followed by anion-exchange chromatography and gel filtration. The peptide has a molecular weight of 25,100, contains approximately 38% carbohydrate (w/w) and corresponds to residues 471-616 at the C-terminus of glucoamylase 1. The peptide bound to granular corn starch maximally at 1.08 nmol/mg starch. It inhibited the hydrolysis of granular starch by glucoamylase 1 but had no effect on the hydrolysis of starch in solution.
authors.affiliation: AFRC Institute of Food Research, Norwich, Norfolk, UK.
authors.forename: N J
authors.initials: NJ
authors.lastname: Belshaw
authors.forename: G
authors.initials: G
authors.lastname: Williamson
mesh_terms: D000596:Amino Acids / Q000032:analysis; D001234:Aspergillus niger / Q000201:enzymology*; D001665:Binding Sites; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D005087:Glucan 1,4-alpha-Glucosidase / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D013213:Starch / Q000378:metabolism
chemical_list: D000596:Amino Acids; D013213:Starch; D005087:Glucan 1,4-alpha-Glucosidase