Document Type

Article

Publication Date

4-30-1991

Journal or Book Title

ACS Symposium Series

Volume

460

First Page

417

Last Page

425

DOI

10.1021/bk-1991-0460.ch032

Abstract

An endo-(l→4)-β-D-xylanase from a cellulase-free Chainia strain was substantially purified and subjected to amino acid sequencing. The first forty N-terminal amino acid residues show high homology with endo-xylanases from Bacillus pumilus, B. subtilis, B. circulans, andSchizophylum commune, less homology with endo-xylanases from Aureobasidium sp. andPseudomonas fluorescens, and slight homology, but including a possible catalytic Asp residue, with catalytic domains of endo-xylanases from Clostridium thermocellum,Cryptococcus albidus, and an alkalophilic Bacillus and with a cellobiohydrolase fromCellulomonas fimi. The enzyme attacks substrates as small as xylotetraose and has xylosyltransferase activity. It is most active at pH 6 and 60°C and most stable between pHs 5 and 7.

Comments

Posted with permission from ACS Symposium Series, Vol. 460 (Washington, D.C.: American Chemical Society, 1991): 417–425, doi:10.1021/bk-1991-0460.ch032. Copyright 1991 American Chemical Society.

Copyright Owner

American Chemical Society

Language

en

File Format

application/pdf

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