2001
DOI: 10.1046/j.1472-765x.2001.00913.x
|View full text |Cite
|
Sign up to set email alerts
|

Kinetic differences of purified laccases from six Pleurotus ostreatus strains

Abstract: The different enzymatic properties of laccases from various P. ostreatus strains should be considered for a potential industrial or environmental application.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

6
57
0
6

Year Published

2008
2008
2024
2024

Publication Types

Select...
7
1

Relationship

0
8

Authors

Journals

citations
Cited by 118 publications
(75 citation statements)
references
References 27 publications
6
57
0
6
Order By: Relevance
“…The top PEG-rich phase which contained the partially purified enzyme (Lac ATPS) was then used for the oxidation experiments. Enzymatic activity and total protein was estimated at the end of the purification protocol, as described by Tinoco et al [19] and Bradford [20], respectively.…”
Section: Partial Purification Of Laccase From a Bisporus Using Aqueomentioning
confidence: 99%
“…The top PEG-rich phase which contained the partially purified enzyme (Lac ATPS) was then used for the oxidation experiments. Enzymatic activity and total protein was estimated at the end of the purification protocol, as described by Tinoco et al [19] and Bradford [20], respectively.…”
Section: Partial Purification Of Laccase From a Bisporus Using Aqueomentioning
confidence: 99%
“…Decolorization percentages were calculated by following the methodology reported by Morales et al, 2016. Laccase activity was determined following the protocol reported by Tinoco et al, 2001. Manganese peroxidase (MnP) activity was determined following the protocol reported by Quevedo-Hidalgo et al, 2015. …”
Section: Experimental Designmentioning
confidence: 99%
“…Both assays were performed at 120 rpm, and the evaluation time was 72 and 216 h for MG and CV respectively (this time was selected in function to the decoloration observed where the media was almost without dye in each case). Periodic sampling was performed to determine the percentage of decolorization, laccase activity (Tinoco et al, 2001), pH, and reducing sugars (Miller 1959). On the other hand, some production parameters (e.g.…”
Section: Removal Experimentsmentioning
confidence: 99%
“…One unit of laccase activity was defined as 1 µmol ABTS + formed per minute (Bourbonnais et al 1997, Tinoco et al 2001). …”
Section: Enzymatic Assaysmentioning
confidence: 99%