A Novel Peroxidase from Fresh Fruiting Bodies of the Mushroom Pleurotus pulmonarius

被引：2

作者：

Zou, Ya-Jie ^{[1
]}

Wang, He-Xiang ^{[2
]}

Zhang, Jin-Xia ^{[1
]}

机构：

[1] Chinese Acad Agr Sci, Inst Agr Resources & Reg Planning, Beijing, Peoples R China

[2] China Agr Univ, Coll Biol Sci, State Key Lab Agrobiotechnol, Beijing, Peoples R China

来源：

INTERNATIONAL JOURNAL OF PEPTIDE RESEARCH AND THERAPEUTICS | 2019年 / 25卷 / 04期

关键词：

Peroxidase; Mushroom; Pleurotus pulmonarius; Isolation; MANGANESE PEROXIDASE; REVERSE-TRANSCRIPTASE; VERSATILE PEROXIDASE; INHIBITORY-ACTIVITY; 1ST DEMONSTRATION; PURIFICATION; ISOENZYMES; POLYSACCHARIDE; DEGRADATION; SEQUENCE;

D O I：

10.1007/s10989-018-9784-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A novel peroxidase has been isolated from fresh fruiting bodies of the mushroom Pleurotus pulmonarius, with a purification protocol of ion exchange chromatography on DEAE-cellulose, affinity chromatography on ConA-Sepharose, ion exchange chromatography on CM-cellulose, and gel filtration by FPLC on Superdex 75. The peroxidase was unadsorbed on either DEAE-cellulose or ConA-Sepharose, but was adsorbed on CM-cellulose. It exhibited a molecular mass of 55 kDa in gel filtration and also in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, indicating that it is a monomeric protein. It possessed a distinctive N-terminal amino acid sequences from other isolated mushroom peroxidases. The optimal pH and temperature for the enzyme were 4.0 and 70 degrees C, respectively. All enzyme activity was destroyed after exposured in 100 degrees C for 10 min. The peroxidase did not exhibit HIV-1 reverse transcriptase inhibitory activity and antifungal activity. The stability against high temperature and extreme pH supported that the enzyme could be a potential peroxidase source for special industrial applications.

引用

页码：1389 / 1396

页数：8

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