Functional expression and characterization of two laccases from the brown rot Fomitopsis pinicola
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F21%3A00548116" target="_blank" >RIV/61388971:_____/21:00548116 - isvavai.cz</a>
Alternative codes found
RIV/00216224:14740/21:00124503
Result on the web
<a href="https://www.sciencedirect.com/science/article/pii/S0141022921000594?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0141022921000594?via%3Dihub</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.enzmictec.2021.109801" target="_blank" >10.1016/j.enzmictec.2021.109801</a>
Alternative languages
Result language
angličtina
Original language name
Functional expression and characterization of two laccases from the brown rot Fomitopsis pinicola
Original language description
Laccase is predominantly found in lignin degrading filamentous white rot fungi, where it is involved in the oxidative degradation of this recalcitrant heteropolymer. In brown rot fungi it is much less prevalent: laccases from only a few brown rots have been detected and only two have been characterized. This study tries to understand the role of this ligninolytic enzyme in brown rots by investigating the catalytic properties of laccases secreted by Fomitopsis pinicola FP58527 SS1. When grown on either poplar or spruce wood blocks, several laccases were detected in the secretome. Two of them (FpLcc1 and FpLcc2) were heterologously produced using Trichoderma reesei QM9414 Delta xyr1 as expression host and purified to homogeneity by consecutive steps of hydrophobic interaction, anion exchange and size exclusion chromatography. With the substrates 2,2-azino-bis(3ethylthiazoline-6-sulfonate) (ABTS), 2,6-dimethoxyphenol (2,6-DMP) and guaiacol both laccases showed similar, low pH-optima below 3 for ABTS and 2,6-DMP and at pH 3.5 for guaiacol which is at the acidic end of laccases isolated from white rot fungi. The determined KM values were low while kcat values measured at acidic conditions were comparable to those reported for other laccases from white rot fungi. While both enzymes showed a moderate decrease in activity in the presence of oxalic and citric acid FpLcc2 was activated by acetic acid up to 3.7 times. This activation effect is much more pronounced at pH 5.0 compared to pH 3.0 and could already be observed at a concentration of 1 mM acetic acid.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Enzyme and Microbial Technology
ISSN
0141-0229
e-ISSN
1879-0909
Volume of the periodical
148
Issue of the periodical within the volume
AUG 2021
Country of publishing house
US - UNITED STATES
Number of pages
12
Pages from-to
109801
UT code for WoS article
000663552500001
EID of the result in the Scopus database
2-s2.0-85105692675