Beta
28965

Purification and studying some characters of laccase enzyme from irradiated Pleurotus ostreatus ATCC 56270

Article

Last updated: 23 Dec 2024

Subjects

-

Tags

-

Abstract

Purification of laccase enzyme by anion exchange chromatography using DEAE sepharose and sephacryl HR are successful in purifying laccase. The molecular weight of laccase was 75 KDa determined by SDS- PAGE. The optimum pH for activity was 5 and for stability was (6.5-7.5), the optimum temperature for activity was 35oC and stability of the enzyme was stable up to 55oC, the enzyme retained 100% of its activity after 20 minutes incubation, 85% of its activity after 1h incubation at the same temperature. The energy of activation (Eact) of the purified laccase between 20oC and 45oC at its optimum pH was 16.3 k Jmol-1. The apparent Km value of the enzyme for ABTS was estimated to be 1.4 mM under standard assay conditions, kcat value of ABTS was calculated to be 3450 min-1, Vmax is the maximum initial rate in the Michaelis- Menten equation (1.2 µmol L-1 min -1).Microencapsulation of laccase was exhibited that free laccase (35U/ml) has higher activity than encapsulated laccase (24.3 U/ml).

DOI

10.21608/ajnsa.2019.3804.1090

Keywords

: Laccase, Pleurotus ostreatus, Purification, properties, Microencapsulation

Authors

First Name

ola

Last Name

haggar

MiddleName

ahmad

Affiliation

microbiology, Faculity of science El-azher university

Email

olaseif20@yahoo.com

City

cairo

Orcid

-

Volume

52

Article Issue

2

Related Issue

4364

Issue Date

2019-04-01

Receive Date

2018-05-11

Publish Date

2019-04-01

Page Start

94

Page End

102

Print ISSN

1110-0451

Online ISSN

2090-4258

Link

https://ajnsa.journals.ekb.eg/article_28965.html

Detail API

https://ajnsa.journals.ekb.eg/service?article_code=28965

Order

13

Type

Original Article

Type Code

455

Publication Type

Journal

Publication Title

Arab Journal of Nuclear Sciences and Applications

Publication Link

https://ajnsa.journals.ekb.eg/

MainTitle

Purification and studying some characters of laccase enzyme from irradiated Pleurotus ostreatus ATCC 56270

Details

Type

Article

Created At

22 Jan 2023