State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, 214122, China.
School of Food and Biological Engineering, Jiangsu University, No. 301 Xuefu Road, Zhenjiang, 212013, China.
Bioprocess Biosyst Eng. 2022 Jan;45(1):147-158. doi: 10.1007/s00449-021-02648-x. Epub 2021 Oct 5.
The cross-linked enzyme aggregates (CLEAs) are one of the technologies that quickly immobilize the enzyme without a carrier. In this study, ionic liquid with amino group (1-aminopropyl-3-methylimidazole bromide, FIL) was used as the novel functional surface molecule to modify CRL (Candida rugosa lipase, CRL). The enzymatic properties of CRL-FIL-CLEAs were investigated. The activity of CRL-FIL-CLEAs (5.51 U/mg protein) was 1.9 times higher than that of CRL-CLEAs (2.86 U/mg protein) without surface modification. After incubating in a centrifuge tube for 50 min at 60 °C, CRL-FIL-CLEAs still maintained 61% of its initial activity, while the value for CRL-CLEAs was only 22%. After repeated use for five times, compared with the 22% residual activity of CRL-CLEAs, the value of CRL-FIL-CLEAs was 51%. Based on the above results, it was indicated that this method provided a new idea for the effective synthesis of immobilized enzyme.
交联酶聚集体（CLEAs）是一种无需载体即可快速固定酶的技术。在这项研究中，使用具有氨基的离子液体（1-氨基丙基-3-甲基咪唑溴化物，FIL）作为新型功能表面分子来修饰 CRl（假丝酵母脂肪酶，CRl）。研究了 CRl-FIL-CLEAs 的酶学性质。与未经表面修饰的 CRl-CLEAs（2.86 U/mg 蛋白）相比，CRl-FIL-CLEAs（5.51 U/mg 蛋白）的活性提高了 1.9 倍。在 60°C 的离心管中孵育 50 min 后，CRl-FIL-CLEAs 仍保持其初始活性的 61%，而 CRl-CLEAs 的活性仅为 22%。重复使用五次后，与 CRl-CLEAs 的 22%剩余活性相比，CRl-FIL-CLEAs 的活性为 51%。基于上述结果，表明该方法为固定化酶的有效合成提供了新的思路。
