Artigo
Purification and characterization of xylanases from Aspergillus giganteus
Fecha
2004-04-20Registro en:
Folia Microbiologica, v. 49, n. 1, p. 13-18, 2004.
0015-5632
10.1007/BF02931639
WOS:000220630700003
2-s2.0-1842418765
4110421764783871
Autor
Universidade Estadual Paulista (Unesp)
Resumen
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°C temperature optimum; optimum pH was 6.0-6.5 for xylanase I and 6.0 for xylanase II. At 50°C xylanase I exhibited higher thermostability than xylanase II. Hg2+, Cu 2+ 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.
Materias
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