2011
DOI: 10.1007/s13213-011-0212-y
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Abstract: In this research, the xylanase high-producing strain of BE-91 (Bacillus subtilis) was selected. The enzyme activity in the fermentation liquor of BE-91 at 8 h reached 408 U/mL, which was 3.4 times higher than that of strain ACCC 10243. The xylanase was purified from BE-91 fermentation liquor with the ultrafiltration and gel chromatography, and its enzyme activity was up to 28,454 U/mg. Its recovery was above 69%, and the purification multiple of the enzyme activity was up to 18 times. The molecular weight of t… Show more

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Cited by 6 publications
(3 citation statements)
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“…Many preliminary studies on ramie bio-degumming, including strain selection, [12][13][14] degumming processes optimization, [15][16][17][18][19] molecular biology studies, 20,21 have been done. Effective degumming strains, packaged degumming process, 22 and genes with potential uses (DQ364440, Liu et al) have been obtained.…”
mentioning
confidence: 99%
“…Many preliminary studies on ramie bio-degumming, including strain selection, [12][13][14] degumming processes optimization, [15][16][17][18][19] molecular biology studies, 20,21 have been done. Effective degumming strains, packaged degumming process, 22 and genes with potential uses (DQ364440, Liu et al) have been obtained.…”
mentioning
confidence: 99%
“…Duarte, Pellegrino, Portugal, Ponezi, and Franco (2000) reported high activity for four strains of B. pumilus, which demonstrated xylanolytic activity of 328, 131, 90 and 167 U mL -1 , respectively. In another study, Bacillus subtilis BE-91 (Liu et al, 2011) was shown to yield 408 U mL -1 , while Streptomyces species (Thomas, Sindhu, & Pandey, 2013b) yielded approximately 200 U mL -1 of xylanase. Since the isolate TC-DT13 was the best xylanase producer in the present screen, it was chosen for further study.…”
Section: Screening Of Xylanolitic Bacteriamentioning
confidence: 95%
“…Subsequently, the 5-50 kDa macromolecule fractions were collected as crude Pel4J4 for Sephadex G-100 gel chromatography. 19 The solution components collected at the double peak of Pel activity and protein content were subjected to 48 h dialysis at 4 C and then concentrated with polyethylene glycol 20,000. The purified Pel4J4 was tested by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE).…”
Section: Methodsmentioning
confidence: 99%