Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Purification and characterization of an extracellular feruloyl esterase from the thermophilic anaerobe Clostridium stercorarium
Autore:
Donaghy, JA; Bronnenmeier, K; Soto-Kelly, PF; McKay, AM;
Indirizzi:
Dept Agr No Ireland, Food Sci Div Microbiol, Belfast BT9 5PX, Antrim, North Ireland Dept Agr No Ireland Belfast Antrim North Ireland BT9 5PX m, North Ireland Queens Univ Belfast, Dept Food Sci Microbiol, Belfast BT7 1NN, Antrim, North Ireland Queens Univ Belfast Belfast Antrim North Ireland BT7 1NN m, North Ireland Tech Univ Munich, Lehrstuhl Mikrobiol, D-8000 Munich, Germany Tech Univ Munich Munich Germany D-8000 Mikrobiol, D-8000 Munich, Germany
Titolo Testata:
JOURNAL OF APPLIED MICROBIOLOGY
fascicolo: 3, volume: 88, anno: 2000,
pagine: 458 - 466
SICI:
1364-5072(200003)88:3<458:PACOAE>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-WALL POLYSACCHARIDES; PARA-COUMAROYL ESTERASE; SUGAR-BEET PULP; ASPERGILLUS-NIGER; ACID ESTERASE; CELLULOLYTIC THERMOPHILE; FAE-III; STREPTOMYCES; DEGRADATION; BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Donaghy, JA Dept Agr No Ireland, Food Sci Div Microbiol, Newforge Lane, Belfast BT9 5PX, Antrim, North Ireland Dept Agr No Ireland Newforge Lane Belfast Antrim North Ireland BT9 5PX
Citazione:
J.A. Donaghy et al., "Purification and characterization of an extracellular feruloyl esterase from the thermophilic anaerobe Clostridium stercorarium", J APPL MICR, 88(3), 2000, pp. 458-466

Abstract

Feruloyl esterases act as accessory enzymes for the complete saccharification of plant cell wall hemicelluloses. Although many fungal feruloyl esterases have been purified and characterized, few bacterial phenolic acid esterases have been characterized. This study shows the extracellular productionof a feruloyl esterase by the thermophilic anaerobe Clostridium stercorarium when grown on birchwood xylan. The feruloyl esterase was purified 500-fold in successive steps involving ultrafiltration, preparative isoelectric focusing and column chromatography by anion exchange, gel filtration and hydrophobic interaction. The purified enzyme released ferulic, rho-coumaric, caffeic and sinapinic acid from the respective methyl esters. The purified enzyme also released ferulic acid from a de-starched wheat bran preparation. At pH 8.0 and 65 degrees C, the K-m and V-max values for the hydrolysis ofmethyl ferulate were 0.04 mmol l(-l) and 131 mu mol min(-1) mg(-1), respectively; the respective values for methyl coumarate were 0.86 mmol l(-l) and18 mu mol min(-1) mg(-1. ) The purified feruloyl esterase had an apparent mass of 33 kDa under denaturing conditions and showed optimum activity at pH8.0 and 65 degrees C. At a concentration of 5 mmol l(-l), the ions Ca2+, Cu2+, Co2+ and Mn2+ reduced the activity by 70-80%.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/11/20 alle ore 09:56:04