Purification and characterization of a low molecular weight xylanase from solid-state cultures of Aspergillus fumigatus fresenius
Rev. microbiol
;
30(2): 114-9, abr.-jun. 1999. tab, graf
Article
Dans Portugais, Anglais
| LILACS
| ID: lil-257205
RESUMO
A xylan-degrading enzyme (xylanase II) was purified to apparent homogeneity from solid-state cultures of Aspergillus fumigatus Fresenius. The molecular weight of xylanase II was found to be 19 and 8.5 kDa, as estimated by SDS-PAGE and gel filtration on FPLC, respectively. The purified enzyme was most active at 55 (degree)C and pH 5.5. It was specific to xylan. The apparent Km and Vmax values on soluble and indisoluble xylans from oat spelt and birchwood showed that xylanase II was most active on soluble birchwood xylan. Studies on hydrolysis products of various xylans and xylooligormers by xylanase II on HPLC showed that the enzyme released a range of products from xylobiose to xylohexaose, with a small amount of xylose from xylooligomers, and presented transferase activity.
Texte intégral:
Disponible
Indice:
LILAS (Amériques)
Sujet Principal:
Aspergillus fumigatus
/
Xylosidases
langue:
Anglais
/
Portugais
Texte intégral:
Rev. microbiol
Thème du journal:
Microbiologie
Année:
1999
Type:
Article
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