Instituto de Química (IQ), Universidade Federal do Rio Grande do Sul (UFRGS), Porto Alegre, RS, Brazil.
Instituto de Ciência e Tecnologia de Alimentos (ICTA), Universidade Federal do Rio Grande do Sul (UFRGS), Porto Alegre, RS, Brazil.
Food Chem. 2018 Apr 25;246:343-350. doi: 10.1016/j.foodchem.2017.11.026. Epub 2017 Nov 8.
β-d-Galactosidase is an important enzyme in the dairy industry, and the enzyme from the yeast Kluyveromyces lactis is most widely used. Here, we report immobilization of the enzyme on a silica/chitosan composite support, devised to have 10% and 20% chitosan (SiQT10 and SiQT20, respectively). Morphological and textural characterizations showed that chitosan is dispersed in micrometric regions in silica. For comparison, a silica organofunctionalized with 3-aminopropyltrimethoxysilane (SiOaptms) was prepared. Performance of the biocatalysts was tested for lactose hydrolysis, and the enzyme immobilized in SiQT10 and SiQT20 composites showed higher efficiency (62% and 47%, respectively) compared with the enzyme in SiOaptms. Operational stability in this system was evaluated for the first time. After 200 h of continuous use in a fixed-bed reactor, SiQT10 remained with approximately 90% activity. Thus, in addition to demonstrating compatibility for food processing, these results align the enzyme stabilization properties of chitosan with the mechanical resistance of silica.
β-半乳糖苷酶是乳品工业中的一种重要酶,而来自酵母克鲁维酵母的酶则被广泛应用。在这里,我们报告了将该酶固定在二氧化硅/壳聚糖复合载体上的方法,设计载体中壳聚糖的含量分别为 10%(SiQT10)和 20%(SiQT20)。形态和结构特性表明壳聚糖分散在二氧化硅的微米级区域中。为了进行比较,还制备了用 3-氨丙基三甲氧基硅烷(SiOaptms)官能化的二氧化硅(SiOaptms)。通过乳糖水解实验测试了生物催化剂的性能,与固定在 SiOaptms 上的酶相比,固定在 SiQT10 和 SiQT20 复合材料上的酶具有更高的效率(分别为 62%和 47%)。这是首次对该体系中的操作稳定性进行评估。在固定床反应器中连续使用 200 小时后,SiQT10 仍保持约 90%的活性。因此,除了证明其与食品加工的兼容性外,这些结果还将壳聚糖的酶稳定特性与二氧化硅的机械强度结合起来。