Purification and properties of a 1,3-beta-glucanase from Penicillium oxalicum autolysates.
High 1,3-beta-glucanase activity was detected during autolysis in a culture medium containing Penicillium oxalicum. It was due to the combined action of four enzymes. The purification process for the major enzyme produced a homogeneous band in the SDS polyacrylamide gel that corresponded to a molecular weight of 79,400 daltons. The enzyme pI was 6.3 and it was only active against 1,3-beta-glucans, with a S0.5 of 0.23 mg ml-1 against laminarin. The enzymatic optima were found at pH 4 and 55 degrees C, and instability was evident when pH and temperature were altered. The enzyme was not active against oxidated laminarin and was barely inhibited by glucono-D-lactone. Hg2+, Ag+ and Fe2+ were effective inhibitors. The enzyme was adsorbed by concanavalin-A-sepharose.
Copa-Patiño
J L
JL
Departamento de Microbiología y Parasitologia, Universidad Alcalá de Henares, Madrid, Spain.
Reyes
F
F
Pérez-Leblic
M I
MI
D002850:Chromatography, Gel; D004693:Glucan Endo-1,3-beta-D-Glucosidase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010407:Penicillium / Q000201:enzymology*; D013696:Temperature
D006026:Glycoside Hydrolases; D004693:Glucan Endo-1,3-beta-D-Glucosidase