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

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...

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Bibliographic Details
Published in:International journal of peptide research and therapeutics 2019-12, Vol.25 (4), p.1389-1396
Main Authors: Zou, Ya-Jie, Wang, He-Xiang, Zhang, Jin-Xia
Format: Article
Language:English
Subjects:
Affinity chromatography
Animal Anatomy
Antifungal activity
Biochemistry
Biomedical and Life Sciences
Cellulose
Chromatography
Enzymatic activity
Enzymes
Filtration
Fruit bodies
Gel electrophoresis
High temperature
Histology
HIV
Human immunodeficiency virus
Industrial applications
Ion exchange
Life Sciences
Liquid chromatography
Molecular Medicine
Morphology
Peroxidase
pH effects
Pharmaceutical Sciences/Technology
Pharmacology/Toxicology
Pleurotus pulmonarius
Polymer Sciences
RNA-directed DNA polymerase
Sodium
Sodium lauryl sulfate
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Summary: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 °C, respectively. All enzyme activity was destroyed after exposured in 100 °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.
ISSN:1573-3149
1573-3904
DOI:10.1007/s10989-018-9784-8