2020
DOI: 10.6001/chemija.v31i3.4292
|View full text |Cite
|
Sign up to set email alerts
|

Biosynthesis, purification, characterization and immobilization of laccase from Lithothelium sp.

Abstract: Novel fungal laccase isoenzymes (namely L95-1 and L95-2) produced by the Ascomycete Lithothelium sp. isolated from the forest soil were purified. However, only one of them was characterized, because the other isoenzyme lost its activity during purification. Extracellular L95-1 laccase was purified 30-fold using ion-exchange and hydrophobic interaction chromatography, with an overall yield of 88%. The molecular mass of purified L95-1 was estimated to be 85 kDa by SDS-PAGE analysis. L95-1 laccase was stable at t… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1

Citation Types

0
1
0

Year Published

2021
2021
2021
2021

Publication Types

Select...
1

Relationship

1
0

Authors

Journals

citations
Cited by 1 publication
(1 citation statement)
references
References 31 publications
(36 reference statements)
0
1
0
Order By: Relevance
“…The kinetic curves were recorded at the wavelength corresponding to the maximum of absorbance. The catalytic constants were determined as described previously [ 57 ].…”
Section: Methodsmentioning
confidence: 99%
“…The kinetic curves were recorded at the wavelength corresponding to the maximum of absorbance. The catalytic constants were determined as described previously [ 57 ].…”
Section: Methodsmentioning
confidence: 99%