Purification and characterization of a xylanase from the thermophilic ascomycete Thelavia terrestris 255B.
Appl Biochem Biotechnol
; 34-35: 247-59, 1992.
Article
em En
| MEDLINE
| ID: mdl-1622204
ABSTRACT
Thielavia terrestris 255B, a thermophilic ascomycete, produced two major forms of xylanase with pIs of 4.6 (xylanase I) and 6.1 (xylanase II). The latter enzyme could be purified to greater than 99% homogeneity using anion-exchange chromatography and gel filtration. Xylanase II had a mol wt of 25.7 kDa (SDS-PAGE) and a pH and a temperature optimum of 3.6-4.0 and 60-65 degrees C, respectively. The ratio of the enzyme's activity against xylan and carboxymethylcellulose was 500-1000 to 1, indicating a possible application of this enzyme in biobleaching processes. The amino acid sequence of this protein is being determined, and initial data suggest that the enzyme belongs to a group of low-mol wt xylanases that have been isolated from both bacteria and fungi.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ascomicetos
/
Glicosídeo Hidrolases
Idioma:
En
Revista:
Appl Biochem Biotechnol
Ano de publicação:
1992
Tipo de documento:
Article
País de afiliação:
Canadá