FEBS Letters | |
Purification and characterization of two lignin peroxidase isozymes produced by Bjerkandera sp. strain BOS55 | |
Hartmans, Sybe1  ten Have, Rimko1  Teunissen, Pauline J.M1  Field, Jim A1  | |
[1] Division of Industrial Microbiology, Department of Food Technology and Nutrition, Wageningen Agricultural University, P.O. Box 8129, 6700 EV Wageningen, Netherlands | |
关键词: Bjerkandera sp. strain BOS55; Lignin peroxidase; Purification; N-terminal sequence; | |
DOI : 10.1016/S0014-5793(98)00044-1 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The white-rot fungus Bjerkandera sp. strain BOS55 excretes at least seven lignin peroxidase (LiP) isozymes. Two of these, LiP-2 and LiP-5 (molecular weight 40–42 kDa), were purified to homogeneity. Both isozymes had the same N-terminal amino acid sequence which showed strong homology with LiP isozymes produced by other white-rot fungi. The kinetics of both isozymes were similar. LiP-5 oxidized veratryl alcohol optimally only in the presence of H2O2 near pH 3.0 (16.7 U/mg) and LiP-2 did this below pH 2.5 (33.8 U/mg). Also at normal physiological pHs for fungal growth (pH 5.0–6.5) both isozymes were still active. Further characterization of LiP-2 and LiP-5 revealed that the K m for H2O2 strongly decreased with increasing pH. As a result of this the catalytic efficiency (TN/K m) calculated on the basis of the K m for H2O2 in the oxidation of veratryl alcohol was constant over wide pH range.
【 授权许可】
Unknown
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