1977
DOI: 10.1271/nogeikagaku1924.51.7_429
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Abstract: Xylanase from Streptomyces sp. E-86 was purified by a procedure including DEAE-sephadex¥cellulose treatment, QAE-sephadex column chromatography and gel filtration on a Biogel P-150 column. The purified enzyme was homogeneous on both Disc-electrophoretical and ultracentrifugal analyses.

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Cited by 35 publications
(10 citation statements)
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“…Xylanases of Streptomyces sp. E_86 13 ) and Aspergillus niger 7) were not inhibited by PCMB. On the other hand, the activity of P. insularus enzyme was greatly elevated by the addition of CaC1 2 and NaCI, but NaN0 3 had no effect on the enzyme activity.…”
Section: Discussionmentioning
confidence: 89%
“…Xylanases of Streptomyces sp. E_86 13 ) and Aspergillus niger 7) were not inhibited by PCMB. On the other hand, the activity of P. insularus enzyme was greatly elevated by the addition of CaC1 2 and NaCI, but NaN0 3 had no effect on the enzyme activity.…”
Section: Discussionmentioning
confidence: 89%
“…X-I, X-II-A, and X-II-B had wider ranges of pH stability than those of known xylanases (pH 3.9 ± 1.2 "-I 8.0 ± 1.5). 3,24,[26][27][28][29][30][31][32] There was a strong similarity between X-II-A and X-II-B in chemical, physico-chemical, and enzymatic characters with a single exception of the isoelectric point. X-I was different from X-II-A and X-II-B in many respects, molecular weight, isoelectric point, and pH stability.…”
Section: Discussionmentioning
confidence: 99%
“…3) In previous papers, 4 -7) we reported the structures of xylans in corncobs,4,S) rice-straw, 6) and cotton-seed cake,7) and the specificity of Streptomyces olivaceoviridis E-86 {J-xylanase 8 ) toward the xylans. We found in the paper that the specificity of Streptomyces xylanase toward arabinose stubs differed considerably from that toward 4-0-methyl-glucuronic acid and glucuronic acid stubs.…”
mentioning
confidence: 98%