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首页> 外文期刊>Biotechnology Progress >Fast flow rate processes for purification of alkaline xylanase isoforms from Bacillus pumilus AJK and their biochemical characterization for industrial application purposes
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Fast flow rate processes for purification of alkaline xylanase isoforms from Bacillus pumilus AJK and their biochemical characterization for industrial application purposes

机译：快速流速工艺，用于纯化芽孢杆菌AJK碱性木聚糖酶同种型的方法及其生化特性，用于工业应用目的

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摘要

This study shows the presence of five isozymic forms of alkaline xylanase from Bacillus pumilus using fast flow rate microfiltration, ultrafiltration, Q-sepharose, and phenyl sepharose chromatographic techniques. Polyacrylamide gel electrophoresis, high-performance liquid chromatography, and zymographic studies also revealed the purity of five isoforms of alkaline xylanases. Isoforms-X-I, X-III, and X-V exhibited optimum activity at pH 8.5, whereas X-II, X-IV showed maximum activity at pH 9. All isoforms were optimally active at temperature 55 degrees C. Isoforms were found to be stable at pH 7-11, showed 92-100% residual activity after 3 hr, treatment time for most industrial applications. The isoforms retained nearly 80-86% residual activity after incubating at 45 degrees C for 3 hr. Molecular weights of xylanase I-V, were 13.1, 15.3, 18.4, 20.1, and 21.0 kDa, respectively. Mg2+ ions were found to be potent activator for all isozymic forms. The Km and Vmax values of X-I, X-II, X-III, X-IV, and X-V were 6.71, 6.66, 7.14, 5.88, 6.25 mg/ml and 2,000, 1,695, 1,666.66, 1,428.57, and 1,408.45 IU/mg protein, respectively. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis revealed the monomeric nature of all isoforms. The low-molecular masses, significantly enhanced activity in the presence of industrially suitable-low cost activator, better stability of all isoforms at pH 7-11 and at higher temperature, also presence of multiple forms of alkaline xylanase, makes this enzyme suitable for textile-paper industries. This is also the first report mentioning the purification of five isozymic forms of alkaline xylanase using fast flow rate techniques.
机译：该研究表明，使用快速流速微滤，超滤，Q-Sepharose和苯琼脂糖色谱技术，来自芽孢杆菌的芽孢杆菌的碱性木聚糖酶的五种同工酶形式的存在。聚丙烯酰胺凝胶电泳，高性能液相色谱和泽胺图谱还揭示了碱性木聚糖酶的五种同种型的纯度。同种型Xi，X-III和XV在pH 8.5上表现出最佳活性，而X-II，X-IV在pH 9时显示出最大活性。所有同种型在温度下最佳活性活性活性55℃。发现同种型在PH 7-11，显示3小时后的残余活性92-100％，大多数工业应用的治疗时间。在45℃下孵育3小时后，同种型在45℃下保留了近80-86％的残余活性。木聚糖酶I-V的分子量分别为13.1,15.3,18.4,20.1和21.0kDa。发现Mg2 +离子是所有同工形式的有效活化剂。 XI，X-II，X-III，X-IV和XV的KM和VMAX值为6.71,6.6,7.14,5.88,6.25mg / ml和2,000,1,695,1,666.66,1,428.57和1,408.45 Iu / mg蛋白， 分别。十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳分析显示所有同种型的单体性质。低分子质量，在工业上合适的低成本活化剂存在下显着增强，所有同种型的稳定性更好，在较高温度下，也存在多种形式的碱性木聚糖酶，使得该酶适用于纺织品纸行业。这也是使用快速流速技术提出五种同工碱形式的碱性木聚糖酶的第一个报告。

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