Journal
PROCESS BIOCHEMISTRY
Volume 48, Issue 12, Pages 1872-1878Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.procbio.2013.09.016
Keywords
Fungi; Basidiomycete; Enzymatic hydrolysis; Benzoyl esterase; Cinnamoyl esterase; Feruloyl esterase
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Funding
- Federal Ministry of Education and Research cluster Biokatalyse [P 37]
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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. (C) 2013 Elsevier Ltd. All rights reserved.
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