Purification and properties of an acetylxylan esterase from Fibrobacter succinogenes S85
| Autor: | C R MacKenzie, Cecil W. Forsberg, K P McDermid |
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| Rok vydání: | 1990 |
| Předmět: |
Rumen
Naphthols Applied Microbiology and Biotechnology Esterase Bacteria Anaerobic chemistry.chemical_compound Hydrolysis Animals Hemicellulose Isoelectric Point Cellulose Acetylxylan esterase Chromatography Fibrobacter succinogenes Ecology Temperature Acetylesterase Hydrogen-Ion Concentration Chromatography Ion Exchange Molecular Weight Isoelectric point chemistry Biochemistry Electrophoresis Polyacrylamide Gel Xylans Isoelectric Focusing Research Article Food Science Biotechnology |
| Zdroj: | Applied and Environmental Microbiology. 56:3805-3810 |
| ISSN: | 1098-5336 0099-2240 |
| DOI: | 10.1128/aem.56.12.3805-3810.1990 |
| Popis: | An acetylxylan esterase (EC 3.1.1.6) was purified to apparent homogeneity from the nonsedimentable extracellular culture fluid of Fibrobacter succinogenes S85 grown on cellulose. This enzyme had an apparent molecular mass of 55 kDa and an isoelectric point of 4.0. The temperature and pH optima were 45 degrees C and 7.0, respectively. The apparent Km and Vmax were 2.7 mM and 9,100 U/mg, respectively, for the hydrolysis of alpha-naphthyl acetate. The enzyme cleaved acetyl residues from birchwood acetylxylan but did not hydrolyze carboxymethylcellulose, larchwood xylan, ferulic acid-arabinose-xylose polymer, p-nitrophenyl-alpha-L-arab-inofuranoside, or longer-chain naphthyl fatty acid esters. The esterase enzyme may play a role in enhancing hemicellulose degradation by F. succinogenes, thereby allowing it greater access to cellulose present in forage cell walls. |
| Databáze: | OpenAIRE |
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