title: Proteases of Maitake (Grifola frondosa) responsible for breakdown of wheat flour dough and their reaction with gluten proteins.
abstract: Two proteases capable of decreasing dough strength when added to wheat flour were purified from Maitake and these were both thought to be peptidyl-Lys metalloendopeptidase. The major purified protease SP-3-A hydrolyzed high-molecular-weight glutenin subunits preferably to the other glutenin subunits. SP-3-A cleaved peptide bonds adjacent to the N-terminal of lysine in the high-molecular-weight glutenin subunit.
authors.affiliation: Department of Japanese Studies, Faculty of Intercultural Studies, Gakushuin Women's College, Tokyo, Japan. makoto.abe@gakushuin.ac.jp
authors.forename: Makoto
authors.initials: M
authors.lastname: Abe
authors.forename: Masaharu
authors.initials: M
authors.lastname: Seguchi
mesh_terms: D000363:Agaricales / Q000201:enzymology*; D000595:Amino Acid Sequence; D001665:Binding Sites; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism*; D005433:Flour; D005983:Glutens / Q000737:chemistry / Q000378:metabolism*; D006868:Hydrolysis; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000235:genetics / Q000378:metabolism; D014908:Triticum / Q000737:chemistry*
chemical_list: D010446:Peptide Fragments; D005983:Glutens; D010450:Endopeptidases