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Stability studies of β-galactosidase immobilized on gluconic acid coated fullerenes
Brazilian Journal of Chemical Engineering ( IF 1.2 ) Pub Date : 2021-08-26 , DOI: 10.1007/s43153-021-00146-x
Shakeel Ahmed Ansari 1 , Asim Muhammed Alshanberi 2
Affiliation  

The present study demonstrates the coating of fullerenes with gluconic acid for the immobilization of Aspergillus oryzae β-galactosidase. The prepared nanomatrix provided 86% immobilization yield, and broadened the biocatalytic activity of immobilized enzyme at higher pH and temperature ranges. Immobilized β-galactosidase exhibited 60% activity even at 5.0% galactose concentration as compared to 23% enzyme activity obtained by soluble enzyme under similar experimental conditions. Reusability of the enzyme was improved considerably as a result of covalent immobilization. Immobilized β-galactosidase showed 89% activity even after sixth repeated use and could be recovered easily. The noticeable improvement in lactose hydrolysis was observed in batch reactors by immobilized enzyme in contrast to the soluble enzyme at high temperature ranges. At 50 °C, 89% lactose conversion was achieved by immobilized enzyme as compared to 77%, obtained by free β-galactosidase under similar incubation conditions. Hence, the developed immobilized enzyme preparation could be exploited for converting lactose into its monosaccharides in a convenient and cheaper way.



中文翻译:

固定在葡萄糖酸涂层富勒烯上的 β-半乳糖苷酶的稳定性研究

本研究证明了用葡萄糖酸包裹富勒烯以固定米曲霉β-半乳糖苷酶。制备的纳米基质提供了 86% 的固定化产率,并拓宽了固定化酶在较高 pH 和温度范围内的生物催化活性。与在类似实验条件下通过可溶性酶获得的 23% 酶活性相比,固定化 β-半乳糖苷酶即使在 5.0% 半乳糖浓度下也表现出 60% 的活性。由于共价固定,酶的可重复使用性大大提高。即使在第六次重复使用后,固定化 β-半乳糖苷酶仍显示 89% 的活性,并且很容易恢复。在高温范围内,固定化酶与可溶性酶相比,在间歇式反应器中观察到乳糖水解的显着改善。在 50 °C 时,固定化酶实现了 89% 的乳糖转化率,而 77%,在类似的孵育条件下通过游离 β-半乳糖苷酶获得。因此,开发的固定化酶制剂可用于以方便和便宜的方式将乳糖转化为其单糖。

更新日期:2021-08-26
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