title: Raw starch adsorption-desorption purification of a thermostable beta-amylase from Clostridium thermosulfurogenes.
abstract: The beta-amylase from Clostridium thermosulfurogenes was readily adsorbed onto raw starch. The adsorbed beta-amylase was eluted from raw starch by using boiled soluble starch solution as an elutant. The soluble starch treated beta-amylase could not adsorb onto raw starch which indicates that the soluble and insoluble substrate binding sites of the beta-amylase may be the same. The beta-amylase was purified to homogeneity by raw starch adsorption-desorption techniques and octyl-Sepharose chromatography. It had a specific activity of 4188 units/mg protein. The insoluble substrate adsorption-desorption technique may be used for the purification of other enzymes.
authors: Michigan Biotechnology Institute, Lansing, Michigan 48909.
authors: B C
authors: BC
authors: Saha
authors: L W
authors: LW
authors: Lecureux
authors: J G
authors: JG
authors: Zeikus
mesh_terms: D000327:Adsorption; D000681:Amylases / Q000302:isolation & purification*; D002850:Chromatography, Gel / Q000379:methods; D003013:Clostridium / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006358:Hot Temperature; D008970:Molecular Weight; D013213:Starch; D001614:beta-Amylase / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D013213:Starch; D000681:Amylases; D001614:beta-Amylase