Purification and characterization of two lignin peroxidase isozymes produced by Bjerkandera sp. strain BOS55

FEBS Letters

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