Raw starch adsorption-desorption purification of a thermostable beta-amylase from Clostridium thermosulfurogenes.
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.
Saha
B C
BC
Michigan Biotechnology Institute, Lansing, Michigan 48909.
Lecureux
L W
LW
Zeikus
J G
JG
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
D013213:Starch; D000681:Amylases; D001614:beta-Amylase