Purification and characteristics of a low-molecular-weight peptide possessing oxidative capacity for phenol from Phanerochaete chrysosporium |
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Authors: | HU Ming ZHANG Weican LU Xuemei GAO Peiji |
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Institution: | State Key Laboratory of Microbial Technology, Shandong University, Jinan 250100, China |
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Abstract: | A new low-molecular-weight peptide with phenol oxidase activity, named Pc factor, was isolated and purified from liquid culture
of a white-rot basidiomycete Phanerochaete chrysosporium. Its molecular weight was about 600 Da estimated by gel-filtration. Three amino acids Glu, Gly and Val were detected in hydrolysate.
Absorption peaks corresponding to amino acids and peptide were observed by UV and IR spectra analysis. And the signal of Cα
of amino acid was also detected by 13C-NMR method. Pc factor had high thermostability and remained active in weakly alkalescent pH range. It could chelate Fe3+ and reduce it to Fe2+, but no hydroxyl radical HO˙ could be detected during the reaction process. It could oxidize phenolic lignin-model compounds
such as 2,6-dimethoxyphenol (2,6-DMP), 2,2′-azinobis (3-ethylbenzathiazoline-6-sulfinic acid) (ABTS) and syringaldazine in
the absence of Mn2+ and H2O2. These characteristics differed greatly from those of manganese peroxidases. The oxidative catalysis of Pc factor can be
enhanced by certain metal ions such as Cu2+ and Mn2+ etc., and O2 molecule was necessary for this reaction. In summary, Pc factor may function as an electron carrier in this novel oxidation-reduction
system. |
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Keywords: | Phanerochaete chrysosporium Pc factor purification phenol oxidase activity lignin |
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