A Search for Ligninolytic Peroxidases in the FungusPleurotus eryngii Involving α-Keto-γ-Thiomethylbutyric Acid and Lignin Model Dimers
A Search for Ligninolytic Peroxidases in the FungusPleurotus eryngii Involving α-Keto-γ-Thiomethylbutyric Acid and Lignin Model Dimers
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杏鲍菇真菌中涉及α-酮-γ-硫代甲基丁酸和木质素模型二聚体的木质素分解过氧化物酶的研究
DOI:
10.1128/aem.65.3.916-922.1999
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发表时间:
1999
影响因子:
4.4
通讯作者:
Angel T. Martı́nez
中科院分区:
文献类型:
--
作者:
L. Caramelo;M. Martínez;Angel T. Martı́nez
ABSTRACT Because there is some controversy concerning the ligninolytic enzymes produced by Pleurotus species, ethylene release from α-keto-γ-thiomethylbutyric acid (KTBA), as described previously for Phanerochaete chrysosporium lignin peroxidase (LiP), was used to assess the oxidative power ofPleurotus eryngii cultures and extracellular proteins. Lignin model dimers were used to confirm the ligninolytic capabilities of enzymes isolated from liquid and solid-state fermentation (SSF) cultures. Three proteins that oxidized KTBA in the presence of veratryl alcohol and H2O2 were identified (two proteins were found in liquid cultures, and one protein was found in SSF cultures). These proteins are versatile peroxidases that act on Mn2+, as well as on simple phenols and veratryl alcohol. The two peroxidases obtained from the liquid culture were able to degrade a nonphenolic β-O-4 dimer, yielding veratraldehyde, as well as a phenolic dimer which is not efficiently oxidized by P. chrysosporium peroxidases. The former reaction is characteristic of LiP. The third KTBA-oxidizing peroxidase oxidized only the phenolic dimer (in the presence of Mn2+). Finally, a fourth Mn2+-oxidizing peroxidase was identified in the SSF cultures on the basis of its ability to oxidize KTBA in the presence of Mn2+. This enzyme is related to the Mn-dependent peroxidase of P. chrysosporium because it did not exhibit activity with veratryl alcohol and Mn-independent activity with dimers. These results show that P. eryngii produces three types of peroxidases that have the ability to oxidize lignin but lacks a typical LiP. Similar enzymes (in terms of N-terminal sequence and catalytic properties) are produced by other Pleurotus species. Some structural aspects of P. eryngii peroxidases related to the catalytic properties are discussed.
DOI:
10.1073/pnas.90.4.1242
发表时间:
1993-02-15
影响因子:
11.1
作者:
KUAN, IC;TIEN, M
通讯作者:
TIEN, M
DOI:
--
发表时间:
1985
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Hammel,KE;Tien,M;Kalyanaraman,B;Kirk,TK
通讯作者:
Kirk,TK
影响因子:
2.9
作者:
Khindaria,A;Barr,DP;Aust,SD
通讯作者:
Aust,SD