Purification and properties of a 1,3-β-glucanase from Penicillium oxalicum autolysates
- 1 December 1989
- journal article
- Published by Oxford University Press (OUP) in FEMS Microbiology Letters
- Vol. 65 (3) , 285-291
- https://doi.org/10.1016/0378-1097(89)90232-2
Abstract
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.Keywords
This publication has 0 references indexed in Scilit: