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. 1995 Dec;61(12):4468–4470. doi: 10.1128/aem.61.12.4468-4470.1995

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

A Blanco 1, T Vidal 1, J F Colom 1, F I Pastor 1
PMCID: PMC167756  PMID: 8534112

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.

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Selected References

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