Catalytic Properties and Partial Amino Acid Sequence of an Actinomycete Endo-(1→4)-β-D-Xylanase from Chainia SpeciesACS Symposium Series
AbstractAn 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.
Copyright OwnerAmerican Chemical Society
Citation InformationKulbhushan B. Bastawde, Louisa B. Tabatabai, Michael M. Meagher, Mandayam C. Srinivasan, et al.. "Catalytic Properties and Partial Amino Acid Sequence of an Actinomycete Endo-(1→4)-β-D-Xylanase from Chainia Species" ACS Symposium Series Vol. 460 (1991) p. 417 - 425
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