Details
Originalsprache | Englisch |
---|---|
Seiten (von - bis) | 231-238 |
Seitenumfang | 8 |
Fachzeitschrift | Bioresource technology |
Jahrgang | 130 |
Publikationsstatus | Veröffentlicht - 20 Dez. 2012 |
Abstract
Little is known on basidiomycete sources of feruloyl esterases (FAEs), although many wood-rotting representatives of these fungi typically grow on feruloyl-rich substrates. A major reason is that the almost ubiquitous presence of laccases interferes with the detection of FAE activity. Laccases polymerize the liberated ferulic acid (FA). in situ, thus detracting the product of enzymatic hydrolysis from its detection. A rapid HPLC-UV method was developed to detect the loss of FA, but also to quantify the hydrolysis of FA esters. The method allows at the same time to evaluate the substrate specificity of a FAE. Forty one basidiomycetes were tested for their FAE activities, and 25 out of the set were positive. The basidiomycetes hydrolyzing cinnamates with the highest conversion rates were. Auricularia auricula-judae and. Marasmius scorodonius. Moreover, a new FAE inducer, the nonionic detergent Tween 80, was found. This is the first comprehensive study on basidiomycete sources of FAEs.
ASJC Scopus Sachgebiete
- Chemische Verfahrenstechnik (insg.)
- Bioengineering
- Umweltwissenschaften (insg.)
- Environmental engineering
- Energie (insg.)
- Erneuerbare Energien, Nachhaltigkeit und Umwelt
- Umweltwissenschaften (insg.)
- Abfallwirtschaft und -entsorgung
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in: Bioresource technology, Jahrgang 130, 20.12.2012, S. 231-238.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Detection of feruloyl- and cinnamoyl esterases from basidiomycetes in the presence of interfering laccase
AU - Haase-Aschoff, Paul
AU - Linke, Diana
AU - Berger, Ralf G.
N1 - Funding information: Support of the work by the BMBF cluster Biokatalyse2021 (P 37) and by L. Popper (Sternenzym Ahrensburg, Germany) is gratefully acknowledged.
PY - 2012/12/20
Y1 - 2012/12/20
N2 - Little is known on basidiomycete sources of feruloyl esterases (FAEs), although many wood-rotting representatives of these fungi typically grow on feruloyl-rich substrates. A major reason is that the almost ubiquitous presence of laccases interferes with the detection of FAE activity. Laccases polymerize the liberated ferulic acid (FA). in situ, thus detracting the product of enzymatic hydrolysis from its detection. A rapid HPLC-UV method was developed to detect the loss of FA, but also to quantify the hydrolysis of FA esters. The method allows at the same time to evaluate the substrate specificity of a FAE. Forty one basidiomycetes were tested for their FAE activities, and 25 out of the set were positive. The basidiomycetes hydrolyzing cinnamates with the highest conversion rates were. Auricularia auricula-judae and. Marasmius scorodonius. Moreover, a new FAE inducer, the nonionic detergent Tween 80, was found. This is the first comprehensive study on basidiomycete sources of FAEs.
AB - Little is known on basidiomycete sources of feruloyl esterases (FAEs), although many wood-rotting representatives of these fungi typically grow on feruloyl-rich substrates. A major reason is that the almost ubiquitous presence of laccases interferes with the detection of FAE activity. Laccases polymerize the liberated ferulic acid (FA). in situ, thus detracting the product of enzymatic hydrolysis from its detection. A rapid HPLC-UV method was developed to detect the loss of FA, but also to quantify the hydrolysis of FA esters. The method allows at the same time to evaluate the substrate specificity of a FAE. Forty one basidiomycetes were tested for their FAE activities, and 25 out of the set were positive. The basidiomycetes hydrolyzing cinnamates with the highest conversion rates were. Auricularia auricula-judae and. Marasmius scorodonius. Moreover, a new FAE inducer, the nonionic detergent Tween 80, was found. This is the first comprehensive study on basidiomycete sources of FAEs.
KW - Basidiomycete
KW - Biofuels
KW - Feruloyl esterase
KW - Fungi
KW - Laccase
UR - http://www.scopus.com/inward/record.url?scp=84872133087&partnerID=8YFLogxK
U2 - 10.1016/j.biortech.2012.12.039
DO - 10.1016/j.biortech.2012.12.039
M3 - Article
AN - SCOPUS:84872133087
VL - 130
SP - 231
EP - 238
JO - Bioresource technology
JF - Bioresource technology
SN - 0960-8524
ER -