Details
| Original language | English |
|---|---|
| Pages (from-to) | 348-357 |
| Number of pages | 10 |
| Journal | Fungal biology |
| Volume | 118 |
| Issue number | 3 |
| Publication status | Published - 6 Feb 2014 |
Abstract
An extracellular feruloyl esterase (PeFaeA) from the culture supernatant of Pleurotus eryngii was purified to homogeneity using cation exchange, hydrophobic interaction, and size exclusion chromatography. The length of the complete coding sequence of PeFaeA was determined to 1668 bp corresponding to a protein of 555 amino acids. The catalytic triad of Ser-Glu-His demonstrated the uniqueness of the enzyme compared to previously published FAEs. The purified PeFaeA was a monomer with an estimated molecular mass of 67kDa. Maximum feruloyl esterase (FAE) activity was observed at pH 5.0 and 50°C, respectively. Metal ions (5mM), except Hg2+, had no significant influence on the enzyme activity. Substrate specificity profiling characterized the enzyme as a type A FAE preferring bulky natural substrates, such as feruloylated saccharides, rather than small synthetic ones. Km and kcat of the purified enzyme for methyl ferulate were 0.15mM and 0.85s-1. In the presence of 3M NaCl activity of the enzyme increased by 28%. PeFaeA alone released only little ferulic acid from destarched wheat bran (DSWB), whereas after addition of Trichoderma viride xylanase the concentration increased more than 20 fold.
Keywords
- Basidiomycete, Ferulic acid esterase, Feruloyl saccharides, Fungi, Halotolerance
ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
- Ecology, Evolution, Behavior and Systematics
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
- Medicine(all)
- Infectious Diseases
Sustainable Development Goals
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In: Fungal biology, Vol. 118, No. 3, 06.02.2014, p. 348-357.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - A halotolerant type A feruloyl esterase from Pleurotus eryngii
AU - Nieter, Annabel
AU - Haase-Aschoff, Paul
AU - Linke, Diana
AU - Nimtz, Manfred
AU - Berger, Ralf G.
N1 - Copyright: Copyright 2020 Elsevier B.V., All rights reserved.
PY - 2014/2/6
Y1 - 2014/2/6
N2 - An extracellular feruloyl esterase (PeFaeA) from the culture supernatant of Pleurotus eryngii was purified to homogeneity using cation exchange, hydrophobic interaction, and size exclusion chromatography. The length of the complete coding sequence of PeFaeA was determined to 1668 bp corresponding to a protein of 555 amino acids. The catalytic triad of Ser-Glu-His demonstrated the uniqueness of the enzyme compared to previously published FAEs. The purified PeFaeA was a monomer with an estimated molecular mass of 67kDa. Maximum feruloyl esterase (FAE) activity was observed at pH 5.0 and 50°C, respectively. Metal ions (5mM), except Hg2+, had no significant influence on the enzyme activity. Substrate specificity profiling characterized the enzyme as a type A FAE preferring bulky natural substrates, such as feruloylated saccharides, rather than small synthetic ones. Km and kcat of the purified enzyme for methyl ferulate were 0.15mM and 0.85s-1. In the presence of 3M NaCl activity of the enzyme increased by 28%. PeFaeA alone released only little ferulic acid from destarched wheat bran (DSWB), whereas after addition of Trichoderma viride xylanase the concentration increased more than 20 fold.
AB - An extracellular feruloyl esterase (PeFaeA) from the culture supernatant of Pleurotus eryngii was purified to homogeneity using cation exchange, hydrophobic interaction, and size exclusion chromatography. The length of the complete coding sequence of PeFaeA was determined to 1668 bp corresponding to a protein of 555 amino acids. The catalytic triad of Ser-Glu-His demonstrated the uniqueness of the enzyme compared to previously published FAEs. The purified PeFaeA was a monomer with an estimated molecular mass of 67kDa. Maximum feruloyl esterase (FAE) activity was observed at pH 5.0 and 50°C, respectively. Metal ions (5mM), except Hg2+, had no significant influence on the enzyme activity. Substrate specificity profiling characterized the enzyme as a type A FAE preferring bulky natural substrates, such as feruloylated saccharides, rather than small synthetic ones. Km and kcat of the purified enzyme for methyl ferulate were 0.15mM and 0.85s-1. In the presence of 3M NaCl activity of the enzyme increased by 28%. PeFaeA alone released only little ferulic acid from destarched wheat bran (DSWB), whereas after addition of Trichoderma viride xylanase the concentration increased more than 20 fold.
KW - Basidiomycete
KW - Ferulic acid esterase
KW - Feruloyl saccharides
KW - Fungi
KW - Halotolerance
UR - http://www.scopus.com/inward/record.url?scp=84896734344&partnerID=8YFLogxK
U2 - 10.1016/j.funbio.2014.01.010
DO - 10.1016/j.funbio.2014.01.010
M3 - Article
C2 - 24607359
AN - SCOPUS:84896734344
VL - 118
SP - 348
EP - 357
JO - Fungal biology
JF - Fungal biology
SN - 1878-6146
IS - 3
ER -