Purification and characterization of xylanases from Aspergillus giganteus.

Abstract:

:A strain of Aspergillus giganteus cultivated in a medium with xylan produced two xylanases (xylanase I and II) which were purified to homogeneity. Their molar mass, estimated by SDS-PAGE, were 21 and 24 kDa, respectively. Both enzymes are glycoproteins with 50 degrees C temperature optimum; optimum pH was 6.0-6.5 for xylanase I and 6.0 for xylanase II. At 50 degrees C xylanase I exhibited higher thermostability than xylanase II. Hg2+, Cu2+ and SDS were strong inhibitors, 1,4-dithiothreitol stimulated the reaction of both enzymes. Both xylanases are xylan-specific; kinetic parameters indicated higher efficiency in the hydrolysis of oat spelts xylan. In hydrolysis of this substrate, xylotriose, xylotetraose and larger xylooligosaccharides were released and hence the enzymes were classified as endoxylanases.

journal_title

Folia microbiologica

authors

Fialho MB,Carmona EC

doi

10.1007/BF02931639

keywords:

subject

Has Abstract

pub_date

2004-01-01 00:00:00

pages

13-8

issue

1

eissn

0015-5632

issn

1874-9356

journal_volume

49

pub_type

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