Microbiological Aspects of the Formation and Degradation of Cellulosic Fibers

Jurášek, L.; Colvin,; Dr, Whitaker

doi:10.1016/s0065-2164(08)70527-6

Cited by 11 publications

(2 citation statements)

References 92 publications

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“…Nakayama et al (25) indicated that partial proteolysis is a factor in the multiple endocellulase system from the same microorganism. Another factor producing electrophoretic heterogeneity could be the complexing of enzyme and polysaccharide, which was observed with a cellulase from Myrothecium verrucaria (14) and with the previously isolated xylanase from S. commune after mixing homogeneous xylanase and xylan (35). Our studies confirm that xylanase A strongly binds carbohydrate in a noncovalent manner.…”

Section: Discussionmentioning

confidence: 98%

Production, characterization, and partial amino acid sequence of xylanase A from Schizophyllum commune

Paice¹,

Jurášek²,

Carpenter³

et al. 1978

Appl Environ Microbiol

100

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Xylanase A, one of several extracellular xylanases produced by Schizophyllum commune strain Delmar when grown in submerged culture with spruce sawdust as carbon source, was purified 43-fold in 25% yield with respect to total xylanase activity. Although some polysaccharide was strongly bound to the purified enzyme, the complex could be dissociated by sodium dodecyl sulfate and appeared homogeneous on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The molecular weight of the protein, calculated from the electrophoretic mobility, was 33,000. The molecular activity of the purified xylanase A, determined with soluble larch xylan as substrate, was 1.4 x 105 min-', with xylobiose and xylose as the major products. The enzyme had a pH optimum of 5.0 and a temperature optimum of 550C in 10-min assays. The acid hydrolysate of xylanase A was rich in aspartic acid and aromatic amino acids. The sequence of 27 residues at the amino terminus showed no homology with known sequences of other proteins.

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