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首页> 外文期刊>Bioprocess and Biosystems Engineering >Immobilization of an alkaline endopolygalacturonase purified from Bacillus paralicheniformis exhibits bioscouring of cotton fabrics
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Immobilization of an alkaline endopolygalacturonase purified from Bacillus paralicheniformis exhibits bioscouring of cotton fabrics

机译：从副粘芽孢杆菌纯化的碱性内聚半乳糖醛酸酶的固定化表现出棉织物的生物煮练

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Pectin degrading enzyme has been increasing interest in an industrial application as biocatalysts, such as juice, textile, and wine industry. Bacillus paralicheniformis CBS3, isolated from popular traditional Korean food (kimchi), produced a novel extracellular thermostable alkaline endopolygalacturonase (BPN3). In this study, BPN3 was purified to 22.04-fold with a recovery yield of 18.93% and specific activity of 2216.41 U/mg by gel filtration and anion exchange column chromatography. The molecular mass of BPN3 was approximately 53 kDa as analyzed by SDS-PAGE and pectic zymography. The N-terminal sequence of BPN3 was AIPVILAX. BPN3 was stable over a broad pH range (8.14-11.47), was thermally stable at 50-60 degrees C, and functioned optimally in pH 9.1 at 60 degrees C. BPN3 had K-m and V-max values of 0.039 mg/mL and 747.9 +/- 1.2 U - mg(-1), respectively, whereas pectin from apple as substrate. BPN3 activity was remarkably affected by metal ions, modulators, and detergents. Digalacturonic acid (GA(2)) was the major oligosaccharide produced by hydrolysis of BPN3 Immobilized BPN3 was active over a pH range (8.1-11.5), temperature (50-60)degrees C, and remained stable with 63.34 and 43.41% of its relative activity during second and third cycle, respectively. Desized cotton exhibited highest reducing sugar liberation through optimized conditions of bioscouring. Bioscouring effectiveness of BPN3 was characterized by the comparison of weight loss for purified BPN3 with commercial pectinase and comparison of BPN3 with grey fabric. BPN3 was simple to purify, had high thermal stability, and was stable over a broad pH range that suggests its suitability for bioscouring application as an industrial catalyst.
机译：果胶降解酶在作为生物催化剂的工业应用中越来越受到关注，例如果汁，纺织和葡萄酒工业。从流行的韩国传统食品（泡菜）中分离到的副芽孢杆菌CBS3产生了一种新型的细胞外热稳定碱性内聚半乳糖醛酸酶（BPN3）。在这项研究中，通过凝胶过滤和阴离子交换柱色谱法将BPN3纯化至22.04倍，回收率18.93％，比活性为2216.41 U / mg。通过SDS-PAGE和果胶酶谱分析，BPN3的分子量约为53kDa。 BPN3的N末端序列是AIPVILAX。 BPN3在较宽的pH范围（8.14-11.47）内稳定，在50-60℃时具有热稳定性，在60℃时在pH 9.1下具有最佳功能。BPN3的Km和V-max值为0.039 mg / mL和747.9 +/- 1.2 U-mg（-1）分别来自苹果的果胶作为底物。 BPN3活性受金属离子，调节剂和去污剂的显着影响。半乳糖醛酸（GA（2））是BPN3水解产生的主要寡糖，固定的BPN3在pH范围（8.1-11.5），温度（50-60）摄氏度下具有活性，并以其63.34和43.41％的比例保持稳定相对活动分别在第二和第三周期。通过优化生物煮练条件，变性棉表现出最高的还原糖释放率。 BPN3的生物洗涤效果通过比较纯化的BPN3与商业果胶酶的重量损失和BPN3与坯布的比较来表征。 BPN3易于纯化，具有很高的热稳定性，并且在很宽的pH范围内都保持稳定，这表明BPN3适合用作工业催化剂的生物精练应用。

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