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Purification and properties of xylanase A from alkali-tolerant Bacillus sp. strain BP-23.

By A Blanco, T Vidal, J F Colom and F I Pastor

Abstract

Xylanase A from the recently isolated Bacillus sp. strain BP-23 was purified to homogeneity. The enzyme shows a molecular mass of 32 kDa and an isoelectric point of 9.3. Optimum temperature and pH for xylanase activity were 50 degrees C and 5.5 respectively. Xylanase A was completely inhibited by N-bromosuccinimide. The main products of birchwood xylan hydrolysis were xylotetraose and xylobiose. The enzyme was shown to facilitate chemical bleaching of pulp, generating savings of 38% in terms of chlorine dioxide consumption. The amino-terminal sequence of xylanase A has a conserved sequence of five amino acids found in xylanases from family F

Topics: Research Article
Year: 1995
OAI identifier: oai:pubmedcentral.nih.gov:167756
Provided by: PubMed Central
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