Purification and characterization of a xylanase from the thermophilic ascomycete Thelavia terrestris 255B - PubMed (original) (raw)

. 1992 Spring:34-35:247-59.

doi: 10.1007/BF02920549.

Affiliations

• PMID: 1622204
• DOI: 10.1007/BF02920549

Purification and characterization of a xylanase from the thermophilic ascomycete Thelavia terrestris 255B

M Gilbert et al. Appl Biochem Biotechnol. 1992 Spring.

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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