Details
| Original language | English |
|---|---|
| Pages (from-to) | 1872-1878 |
| Number of pages | 7 |
| Journal | Process biochemistry |
| Volume | 48 |
| Issue number | 12 |
| Publication status | Published - 18 Sept 2013 |
Abstract
Benzoic acid esterases and ferulic acid esterases (FAE) are enzymes with different profiles of substrate specificity. An extracellular esterase (EstBC) from culture supernatants of the edible basidiomycete fungus Auricularia auricula-judae was purified by anion exchange chromatography, followed by preparative isoelectric focusing and hydrophobic interaction chromatography. EstBC showed a molecular mass of 36 kDa and an isoelectric point of 3.2 along with broad pH and temperature windows similar to fungal FAEs. However, EstBC exhibited also characteristics of a benzoic acid esterase acting on both benzoates and cinnamates, and most efficiently on methyl and ethyl benzoate, methyl 3-hydroxybenzoate and methyl salicylate. Feruloyl saccharides as well as lipase substrates, such as long chain fatty acids esterified with glycerol, polyethoxylated sorbitan and p-nitrophenol were not hydrolyzed. Protein database analyses with tryptic peptides of EstBC solely yielded hits regarding hypothetical proteins belonging to the alpha/beta hydrolase family. The uncommon substrate specificity of EstBC concomitant with a lack of sequence homology to known enzymes suggests a new type of enzyme.
Keywords
- Basidiomycete, Benzoyl esterase, Cinnamoyl esterase, Enzymatic hydrolysis, Feruloyl esterase, Fungi
ASJC Scopus subject areas
- Chemical Engineering(all)
- Bioengineering
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Immunology and Microbiology(all)
- Applied Microbiology and Biotechnology
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In: Process biochemistry, Vol. 48, No. 12, 18.09.2013, p. 1872-1878.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - An enzyme from Auricularia auricula-judae combining both benzoyl and cinnamoyl esterase activity
AU - Haase-Aschoff, Paul
AU - Linke, Diana
AU - Nimtz, Manfred
AU - Popper, Lutz
AU - Berger, Ralf G.
N1 - Funding information: Support of the work by the Federal Ministry of Education and Research cluster Biokatalyse2021 (P 37) and M. Bunzel (KIT, Karlsruhe, Germany) is gratefully acknowledged.
PY - 2013/9/18
Y1 - 2013/9/18
N2 - Benzoic acid esterases and ferulic acid esterases (FAE) are enzymes with different profiles of substrate specificity. An extracellular esterase (EstBC) from culture supernatants of the edible basidiomycete fungus Auricularia auricula-judae was purified by anion exchange chromatography, followed by preparative isoelectric focusing and hydrophobic interaction chromatography. EstBC showed a molecular mass of 36 kDa and an isoelectric point of 3.2 along with broad pH and temperature windows similar to fungal FAEs. However, EstBC exhibited also characteristics of a benzoic acid esterase acting on both benzoates and cinnamates, and most efficiently on methyl and ethyl benzoate, methyl 3-hydroxybenzoate and methyl salicylate. Feruloyl saccharides as well as lipase substrates, such as long chain fatty acids esterified with glycerol, polyethoxylated sorbitan and p-nitrophenol were not hydrolyzed. Protein database analyses with tryptic peptides of EstBC solely yielded hits regarding hypothetical proteins belonging to the alpha/beta hydrolase family. The uncommon substrate specificity of EstBC concomitant with a lack of sequence homology to known enzymes suggests a new type of enzyme.
AB - Benzoic acid esterases and ferulic acid esterases (FAE) are enzymes with different profiles of substrate specificity. An extracellular esterase (EstBC) from culture supernatants of the edible basidiomycete fungus Auricularia auricula-judae was purified by anion exchange chromatography, followed by preparative isoelectric focusing and hydrophobic interaction chromatography. EstBC showed a molecular mass of 36 kDa and an isoelectric point of 3.2 along with broad pH and temperature windows similar to fungal FAEs. However, EstBC exhibited also characteristics of a benzoic acid esterase acting on both benzoates and cinnamates, and most efficiently on methyl and ethyl benzoate, methyl 3-hydroxybenzoate and methyl salicylate. Feruloyl saccharides as well as lipase substrates, such as long chain fatty acids esterified with glycerol, polyethoxylated sorbitan and p-nitrophenol were not hydrolyzed. Protein database analyses with tryptic peptides of EstBC solely yielded hits regarding hypothetical proteins belonging to the alpha/beta hydrolase family. The uncommon substrate specificity of EstBC concomitant with a lack of sequence homology to known enzymes suggests a new type of enzyme.
KW - Basidiomycete
KW - Benzoyl esterase
KW - Cinnamoyl esterase
KW - Enzymatic hydrolysis
KW - Feruloyl esterase
KW - Fungi
UR - http://www.scopus.com/inward/record.url?scp=84888199154&partnerID=8YFLogxK
U2 - 10.1016/j.procbio.2013.09.016
DO - 10.1016/j.procbio.2013.09.016
M3 - Article
AN - SCOPUS:84888199154
VL - 48
SP - 1872
EP - 1878
JO - Process biochemistry
JF - Process biochemistry
SN - 1359-5113
IS - 12
ER -