Abstract:
:Nine proteins with lignin peroxidase activity were separated from cultures of Phanerochaete chrysosporium INA-12 in glycerol as carbon source and non-nitrogen limited. Four lignin peroxidase isozymes (4, 5, 8, 9) were purified and characterized. Although differences in kinetic parameters could be shown, antibody reaction showed homology between isozymes. However, thermal stability studied, peptide mapping results, and N-terminal sequence analyses established a higher degree of homology between isozymes 4/5 and 8/9 types. Protein characterization and kinetic data indicate that lignin peroxidase isozymes 4, 5, 8, and 9 differ from described isozymes in strain BKM. The higher specific activity of lignin peroxidase isozymes in cultures with glycerol than in nitrogen-starved cultures accounts for the higher lignin peroxidase activity obtained in these conditions.
journal_name
Enzyme Microb Technoljournal_title
Enzyme and microbial technologyauthors
Odier E,Delattre Mdoi
10.1016/0141-0229(90)90056-vkeywords:
subject
Has Abstractpub_date
1990-06-01 00:00:00pages
447-52issue
6eissn
0141-0229issn
1879-0909pii
0141-0229(90)90056-Vjournal_volume
12pub_type
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journal_title:Enzyme and microbial technology
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更新日期:2019-06-01 00:00:00
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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journal_title:Enzyme and microbial technology
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