CHARACTERIZATION OF AN ALKALINE ENDO-POLYGALACTURONASE (PGase LBW 5117) FROM ALKALIPHILIC BACILLUS HALODURANS LBW 5117 AND DEMONSTRATION OF ITS BIO-SCOURING POTENTIAL

IF 0.6 Q4 FOOD SCIENCE & TECHNOLOGY
K. R. Oluoch, E. Muge, Yvonne Wanjiku Mwangi, Francis Jakim Mulaa
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Abstract

The demand for pectinases in the global market has been on the rise in recent years due to their significant biotechnological uses. The present study involves the characterization of a crude alkaline pectinase from Bacillus halodurans LBW 5117 and the demonstration of its bioscouring potential. The enzyme was an endo polygalacturonase (PGase LBW 5117) that was brown and had a slight fermentation odor. It exhibited an activity of 0.21 U/ml and retained 67, 90.5, 95.2, and 95.2 % of this activity after 1 year of storage at -20, 4, 20, and 30 oC, respectively. Its operational pH and temperature ranged between 10.2 - 11.0 (optimum, 10.5) and 45 - 57 oC (optimum 50 oC), respectively. Metal ions e.g., K+, Ca2+, Mg2+, Fe3+, Cu2+, Na+, Mn2+, and Zn2+ either stimulated or did not significantly affect its activity at 1 mM. The enzyme retained only 15 % of its activity after 8 h of incubation at 50 oC, but this improved to 200 % in the presence of 1.5 mM Ca2+ and 0.05 mM Tween 20. The enzyme was cellulase-free and hydrolyzed pectin in an endo-manner. Moreover, when used under the established optimized operating conditions, it degraded and eliminated pectin (and other non-cellulosic hydrophobic impurities that adhere to it) from woven cotton (weight loss = 0.68 %) and produced a more hydrophilic fabric with improved wettability for water (drop test = 10 sec) and dye (capillary rise test = 28 mm after 30 min). This result shows that PGase LBW 5117 possesses good operational properties, potentially making it a good bioscouring agent. It is, however, recommended that the bioscouring process be optimized, and its effectiveness be compared with that of standard bio- and/or chemical-scouring process(es).
来自烷基嗜脂杆菌 LBW 5117 的烷基内多聚半乳糖醛酸内切酶(PGase LBW 5117)的鉴定及其生物清洗潜力的证明
近年来,由于果胶酶在生物技术方面的重要用途,全球市场对果胶酶的需求不断增加。本研究涉及卤化芽孢杆菌(Bacillus halodurans)LBW 5117 的一种粗制碱性果胶酶的表征及其生物酸化潜力的展示。该酶是一种内源性聚半乳糖醛酸酶(PGase LBW 5117),呈棕色,有轻微的发酵气味。它的活性为 0.21 U/ml,在-20、4、20 和 30 oC 温度下储存一年后,活性分别保持了 67%、90.5%、95.2%和 95.2%。其工作 pH 值和温度范围分别为 10.2 - 11.0(最佳值为 10.5)和 45 - 57 oC(最佳值为 50 oC)。金属离子(如 K+、Ca2+、Mg2+、Fe3+、Cu2+、Na+、Mn2+ 和 Zn2+)在 1 mM 的浓度下对其活性有刺激作用或无明显影响。在 50 oC 下培养 8 小时后,该酶仅保留了 15% 的活性,但在 1.5 mM Ca2+ 和 0.05 mM 吐温 20 的存在下,活性提高到了 200%。该酶不含纤维素酶,能以内切方式水解果胶。此外,在既定的优化操作条件下使用时,它能降解并消除棉织物中的果胶(以及附着在果胶上的其他非纤维素疏水杂质)(重量损失 = 0.68 %),并生产出亲水性更强的织物,提高了对水(水滴测试 = 10 秒)和染料(30 分钟后毛细管上升测试 = 28 毫米)的润湿性。这一结果表明,PGase LBW 5117 具有良好的操作性能,有可能成为一种良好的生物上光剂。不过,建议对生物上色工艺进行优化,并将其效果与标准生物和/或化学上色工艺进行比较。
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来源期刊
CiteScore
1.90
自引率
0.00%
发文量
156
审稿时长
8 weeks
期刊介绍: The Journal of Microbiology, Biotechnology and Food Sciences is an Open Access, peer-reviewed online scientific journal published by the Faculty of Biotechnology and Food Sciences (Slovak University of Agriculture in Nitra). The major focus of the journal is regular publishing of original scientific articles, short communications and reviews about animal, plant and environmental microbiology (including bacteria, fungi, yeasts, algae, protozoa and viruses), microbial, animal and plant biotechnology and physiology, microbial, plant and animal genetics, molecular biology, agriculture and food chemistry and biochemistry, food control, evaluation and processing in food science and environmental sciences.
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