一种有前途的漆酶固定化方法，用于从水溶液中去除双酚 A。
A promising laccase immobilization approach for Bisphenol A removal from aqueous solutions.
机构信息
Université des Sciences et de la Technologie Houari Boumediene (USTHB), Laboratoire des Sciences du Génie des Procédés Industriels, Faculté de Génie Mécanique et de Génie des Procédés, BP 32, El-Alia 16111, Algiers, Algeria; Centre de Développement des Energies Renouvelables, CDER, 16340 Algiers, Algeria.
Université des Sciences et de la Technologie Houari Boumediene (USTHB), Laboratoire des Sciences du Génie des Procédés Industriels, Faculté de Génie Mécanique et de Génie des Procédés, BP 32, El-Alia 16111, Algiers, Algeria.
出版信息
Bioresour Technol. 2019 Jan;271:360-367. doi: 10.1016/j.biortech.2018.09.129. Epub 2018 Sep 27.
The immobilization of crude laccase from Trametes pubescens by glutaraldehyde crosslinking prior to entrapment into Ca-alginate beads increased the immobilization yield by 30% and reduced the leaking by 7-fold compared to the immobilization with no crosslinking. The performance of the newly developed biocatalyst to degrade Bisphenol A (BPA) from aqueous solutions was tested. Thus, operating at optimal conditions (i.e. pH 5, 30 °C, 20 mg L BPA and 1500 U L laccase), a BPA removal higher than 99% in 2 h was achieved. This value is higher than those reported to date for BPA removal by immobilized laccases. In addition, the biocatalyst was able to remove BPA in 10 successive batches with an efficiency higher than 70% at the end of the last batch. BPA adsorption on the alginate beads was negligible, therefore BPA removal was only due to laccase action. Moreover, Fourier-transform Infrared (FTIR) spectroscopy suggested BPA transformation by laccase.
戊二醛交联固定化提高了糙皮侧耳漆酶的固定化收率，降低了漏出率，与未经交联固定化相比，固定化收率提高了 30%，漏出率降低了 7 倍。新开发的生物催化剂用于降解水溶液中的双酚 A（BPA）的性能进行了测试。在最佳条件下（即 pH5、30°C、20mgL BPA 和 1500U L 漆酶）运行时，在 2 h 内实现了高于 99%的 BPA 去除率。该值高于迄今为止报道的固定化漆酶去除 BPA 的去除率。此外，该生物催化剂能够在 10 个连续批次中去除 BPA，最后一个批次结束时的效率高于 70%。BPA 在藻酸盐珠上的吸附可以忽略不计，因此 BPA 的去除仅归因于漆酶的作用。此外，傅里叶变换红外（FTIR）光谱表明 BPA 经漆酶转化。
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