2005
DOI: 10.5483/bmbrep.2005.38.1.017
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Endo-1,4-β-xylanase B from Aspergillus cf. niger BCC14405 Isolated in Thailand: Purification, Characterization and Gene Isolation

Abstract: During the screening of xylanolytic enzymes from locally isolated fungi, one strain BCC14405, exhibited high enzyme activity with thermostability. This fugal strain was identified as Aspergillus cf. niger based on its morphological characteristics and internal transcribed spacer (ITS) sequences. An enzyme with xylanolytic activity from BCC14405 was later purified and characterized. It was found to have a molecular mass of ca.

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Cited by 60 publications
(37 citation statements)
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“…These enzymes have applications in conversion of lignocellulosic substances to chemicals and fuels, animal feed digestion, food and textile industries, and as bleaching agents in the pulp and paper processing (KNOB et al, 2010;MOURE et al, 2006;POLIZELI et al, 2005). Filamentous fungi are widely used as enzyme producers and are generally considered as more potent xylanolytic enzymes producers than bacteria and yeast (KRISANA et al, 2005;POLIZELI et al, 2005).…”
Section: Introductionmentioning
confidence: 99%
“…These enzymes have applications in conversion of lignocellulosic substances to chemicals and fuels, animal feed digestion, food and textile industries, and as bleaching agents in the pulp and paper processing (KNOB et al, 2010;MOURE et al, 2006;POLIZELI et al, 2005). Filamentous fungi are widely used as enzyme producers and are generally considered as more potent xylanolytic enzymes producers than bacteria and yeast (KRISANA et al, 2005;POLIZELI et al, 2005).…”
Section: Introductionmentioning
confidence: 99%
“…The purification factor for xylanases from Aspergillus strains was relatively low as 1.3-4 8,14 and also in this study, middle high: 30-33 10,15,20 or very high: 77-93 11 . The purification yield of the xylanase from A. awamori VTCC-F312 was the highest (22%) among purification yield reported; low as 3.4-4.5% (xylanase II 8 , xylanase I 11, 14 ), middle high as 10.5-14.8% (xylanase II 11 , xylanase I 8, 15 ), and high as 20.7% 9 . The specific activity of the xylanase in this study (217 U/mg) was higher than that (124 U/mg) of the A. niger C3486 xylanase 15 , relatively high as that (289 U/mg) of the xylanase from A. ficuum AF-98 U2/1 (490 U/mg) 12 and A. cf.…”
Section: Purification Of a Awamori Vtcc-f312 Xylanasementioning
confidence: 99%
“…Xylanases from other Aspergillus strains were purified to homogeneity by using a similar purification scheme involving ammonium sulphate precipitation, gel filtration chromatography (Sephadex G-200, G-100, G-75), ion exchange chromatography (DEAESephadex A-50, DEAE Sepharose, Q-Sepharose), and affinity chromatography Phenyl Sepharose 6 Fast Flows, Sephacryl S-200 [8][9][10][11][12]15 . Xylanases have been purified to homogeneity with a molecular mass of 32-35 kDa from A. awamori 2B.361 U2/1 12 11 .…”
Section: Purification Of a Awamori Vtcc-f312 Xylanasementioning
confidence: 99%
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