Details
| Original language | English |
|---|---|
| Pages (from-to) | 7241-7251 |
| Number of pages | 11 |
| Journal | Applied Microbiology and Biotechnology |
| Volume | 97 |
| Issue number | 16 |
| Publication status | Published - 1 Dec 2012 |
Abstract
Investigating the secretion of esterases by the basidiomycetous fungus Pleurotus sapidus in a Tween 80-rich nutrient medium, an enzyme was discovered that hydrolyzed the ester bond of feruloylated saccharides. The enzyme was purified by ion exchange and size exclusion chromatography. Polyacrylamide gel electrophoresis analysis showed a monomeric protein of about 55 kDa. The complete coding sequence with an open reading frame of 1,665 bp encoded a protein (Est1) consisting of 554 amino acids. The enzyme showed no significant homology to any published feruloyl esterase sequences, but possessed putative conserved domains of the lipase/esterase superfamily. Substrate specificity studies classified the new enzyme as type-A feruloyl esterase, hydrolyzing methyl ferulate, methyl sinapate, and methyl p-coumarate but no methyl caffeate. The enzyme had a pH optimum of 6 and a temperature optimum at 50 C. Ferulic acid was efficiently released from ferulated saccharides, and the feruloyl esterase exhibited moderate stability in biphasic systems (50 % toluene or tert-butylmethyl ether).
Keywords
- Basidiomycete, Ferulated saccharides, Feruloyl esterase, Fungi, Pleurotus sapidus
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biotechnology
- Immunology and Microbiology(all)
- Applied Microbiology and Biotechnology
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In: Applied Microbiology and Biotechnology, Vol. 97, No. 16, 01.12.2012, p. 7241-7251.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - An esterase from the basidiomycete Pleurotus sapidus hydrolyzes feruloylated saccharides
AU - Linke, Diana
AU - Matthes, Rene
AU - Nimtz, Manfred
AU - Zorn, Holger
AU - Bunzel, Mirko
AU - Berger, Ralf G.
PY - 2012/12/1
Y1 - 2012/12/1
N2 - Investigating the secretion of esterases by the basidiomycetous fungus Pleurotus sapidus in a Tween 80-rich nutrient medium, an enzyme was discovered that hydrolyzed the ester bond of feruloylated saccharides. The enzyme was purified by ion exchange and size exclusion chromatography. Polyacrylamide gel electrophoresis analysis showed a monomeric protein of about 55 kDa. The complete coding sequence with an open reading frame of 1,665 bp encoded a protein (Est1) consisting of 554 amino acids. The enzyme showed no significant homology to any published feruloyl esterase sequences, but possessed putative conserved domains of the lipase/esterase superfamily. Substrate specificity studies classified the new enzyme as type-A feruloyl esterase, hydrolyzing methyl ferulate, methyl sinapate, and methyl p-coumarate but no methyl caffeate. The enzyme had a pH optimum of 6 and a temperature optimum at 50 C. Ferulic acid was efficiently released from ferulated saccharides, and the feruloyl esterase exhibited moderate stability in biphasic systems (50 % toluene or tert-butylmethyl ether).
AB - Investigating the secretion of esterases by the basidiomycetous fungus Pleurotus sapidus in a Tween 80-rich nutrient medium, an enzyme was discovered that hydrolyzed the ester bond of feruloylated saccharides. The enzyme was purified by ion exchange and size exclusion chromatography. Polyacrylamide gel electrophoresis analysis showed a monomeric protein of about 55 kDa. The complete coding sequence with an open reading frame of 1,665 bp encoded a protein (Est1) consisting of 554 amino acids. The enzyme showed no significant homology to any published feruloyl esterase sequences, but possessed putative conserved domains of the lipase/esterase superfamily. Substrate specificity studies classified the new enzyme as type-A feruloyl esterase, hydrolyzing methyl ferulate, methyl sinapate, and methyl p-coumarate but no methyl caffeate. The enzyme had a pH optimum of 6 and a temperature optimum at 50 C. Ferulic acid was efficiently released from ferulated saccharides, and the feruloyl esterase exhibited moderate stability in biphasic systems (50 % toluene or tert-butylmethyl ether).
KW - Basidiomycete
KW - Ferulated saccharides
KW - Feruloyl esterase
KW - Fungi
KW - Pleurotus sapidus
UR - http://www.scopus.com/inward/record.url?scp=84881224096&partnerID=8YFLogxK
U2 - 10.1007/s00253-012-4598-7
DO - 10.1007/s00253-012-4598-7
M3 - Article
C2 - 23203636
AN - SCOPUS:84881224096
VL - 97
SP - 7241
EP - 7251
JO - Applied Microbiology and Biotechnology
JF - Applied Microbiology and Biotechnology
SN - 0175-7598
IS - 16
ER -