One of the important commercial usages of pectinase is the depectinization and clarification of fruit juices. The application of native enzymes for industrial utilization has limitations such as high production cost, instability with operational conditions, difficulty in separation of products from reaction media, and lack of reusability. In this study, pectinase from Aspergillus aculeatus was immobilized on silylated-montmorillonite clay as available and an inexpensive carrier using glutaraldehyde as a cross-linker agent. The pectinase-loaded carriers were characterized using Fourier transform infrared spectroscopy and scanning electron microscopy. The immobilization method did not affect the optimum temperature and the thermal stability of pectinase for achieving the maximum activity, but the immobilized enzyme was more active in acidic pH. Km and Vmax value after immobilization process was decreased. The immobilized pectinase was reused for up to 6 repetitive cycles, retaining 60% of its initial activity. The immobilized pectinase was used for pineapple juice clarification and the clarification rate of the immobilized pectinase was higher than that of the free pectinase throughout the experimental period. The proposed methodology may be a convenient alternative to obtain new biocatalysts the fruit juice industry.

果胶酶的重要商业用途之一是果汁的去果胶和澄清。将天然酶用于工业利用具有局限性，例如生产成本高，在操作条件下不稳定，产物与反应介质分离困难以及缺乏可重复使用性。在这项研究中，从刺曲霉的果胶酶使用戊二醛作为交联剂，将其固定在甲硅烷基化的蒙脱石粘土和便宜的载体上。使用傅里叶变换红外光谱和扫描电子显微镜表征负载果胶酶的载体。固定化方法并没有影响获得最大活性的果胶酶的最佳温度和热稳定性，但固定化酶在酸性pH值下更具活性。固定过程后Km和Vmax值降低。固定的果胶酶可重复使用多达6个重复周期，保留其初始活性的60％。固定化果胶酶用于菠萝汁的澄清，并且在整个实验期间，固定化果胶酶的澄清率高于游离果胶酶的澄清率。