Properties of Streptomyces sp. endo-β-xylanases in relation to their applicability in kraft pulp bleaching

A screening of a collection of Streptomyces sp. strains has shown that Streptomyces achromogenes 5028 (S1), Streptomyces longisporus ruber 4–167 (S2) and Streptomyces sp. 8812 (S3) degraded efficiently beechwood xylan. The -xylanase activities present in the culture filtrate of the strains were purified to electrophoretic homogeneity and found to be typical non-debranching endo--xylanases (1,4--D-xylan xylanohydrolases: E.C. 3.2.1.8) with respective molecular weights of 25,000 (S1), 45,000 (S2) and 22,000 (S3). The enzymes were characterized with respect to their temperature–pH relationship and kinetic profile. Immunological experiments suggested that the enzyme produced by S1 belonged to family 11 of glycanases and the S3 enzyme to family 10. The three xylanases adsorbed onto crystalline cellulose but were catalytically inert towards this material, indicating a possible application of these enzymes in biobleaching processes. With respect to its effect on and brightness values in a DEDED bleaching sequence, the xylanase produced by the S1 strain appeared as comparable to a Trichoderma longibrachiatum commercial enzyme preparation (Novozym 431). Streptomyces sp. xylanases may find applications in elemental-chlorine-free bleaching procedures.     

A bifunctional beta-xylosidase-xylose isomerase from Streptomyces sp. EC 10

beta-Xylosidase (1,4-beta-D-xylan xylohydrolase EC 3.2.1.37) and xylose isomerase (D-xylose ketol-isomerase EC 5.3.1.5) produced by Streptomyces sp. strain EC 10, were cell-bound enzymes induced by xylan, straw, and xylose. Enzyme production was subjected to a form of carbon catabolite repression by glycerol. beta-Xylosidase and xylose isomerase copurified strictly, and the preparation was found homogeneous by gel electrophoresis after successive chromatography on DEAE-Sephacel and gel filtration on Biogel A. Streptomyces sp. produced apparently a bifunctional beta-xylosidase-xylose isomerase enzyme. The molecular weight of the enzyme was measured to be 163,000 by gel filtration and 42,000 by SDS-PAGE, indicating that the enzyme behaved as a tetramer of identical subunits. The Streptomyces sp. beta-xylosidase was a typical glycosidase acting as an exoenzyme on xylooligosaccharides, and working optimally at pH 7.5 and 45 degrees C. The xylose isomerase optimal temperature was 70 degrees C and maximal activity was observed in a broad range pH (5-8). Enhanced saccharification of arabinoxylan caused by the addition of the enzyme to endoxylanase suggested a cooperative enzyme action. The first 35 amino acids of the N-terminal sequence of the enzyme showed strong analogies with N-terminal sequences of xylose isomerase produced by other microorganisms but not with other published N-terminal sequences of beta-xylosidases.