Abstract：
:A laccase from Pycnoporus sanguineus was purified by two steps using phenyl-Sepharose columm. A typical procedure provided 54.1-fold purification, with a yield of 8.37%, using syringaldazine as substrate. The molecular weight of the purified laccase was 69 and 68 kDa as estimated by 12% (w/v) SDS-PAGE gel and by gel filtration, respectively. The K (m) values for the substrates ABTS, syringaldazine, and guaiacol were 58, 8.3, and 370 muM, respectively. The enzyme's pH optimum for syringaldazine was 4.2 and optimal activity was 50 degrees C. The enzyme showed to be thermostable because when kept at 50 degrees C for 24 and 48 h it retained 93 and 76% activity. This laccase was inhibited by L: -cysteine, beta-mercaptoethanol, NaN(3), NaF, and HgCl(2).
journal_name
Appl Microbiol Biotechnoljournal_title
Applied microbiology and biotechnologyauthors
Garcia TA,Santiago MF,Ulhoa CJdoi
10.1007/s00253-006-0817-4subject
Has Abstractpub_date
2007-05-01 00:00:00pages
311-8issue
2eissn
0175-7598issn
1432-0614journal_volume
75pub_type
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