Detection and partial characterization of oxalate decarboxylase from Agaricus bisporus

Citation
M. Kathiara et al., Detection and partial characterization of oxalate decarboxylase from Agaricus bisporus, MYCOL RES, 104, 2000, pp. 345-350
Citations number
30
Categorie Soggetti
Plant Sciences
Journal title
MYCOLOGICAL RESEARCH
ISSN journal
09537562 → ACNP
Volume
104
Year of publication
2000
Part
3
Pages
345 - 350
Database
ISI
SICI code
0953-7562(200003)104:<345:DAPCOO>2.0.ZU;2-Q
Abstract
Oxalate decarboxylase activity was present in liquid culture medium and myc elium of Agaricus bisporus. Enzyme activity in the mycelium peaked at two-w eekly intervals after primary growth phase and into secondary metabolism wi th activity peaks in the medium occurring 7 d later than in the mycelium. T he enzyme was partially purified and had two isozymes with pls 3.0 and 3.4. Characterization of the protein by SDS-PAGE and Western blotting against a polyclonal antibody raised to oxalate decarboxylase from Collybia velutipe s showed a major protein band of 64 kDa. Oxalate decarboxylase was also det ected in the fruit body up to the cup stage of development. The pH optimum for the enzyme was 3.6 and temperature optimum was 35 degrees C.