Instituto de Medicina Molecular y Celular Aplicada (IMMCA), SIPROSA-CONICET-UNT. Dorrego 1080, T4000NXB, San Miguel de Tucumán, Tucumán, Argentina.
Planta Piloto de Procesos Industriales Microbiológicos (PROIMI-CONICET), Belgrano and Caseros corner, T4001MVB, San Miguel de Tucumán, Tucumán, Argentina.
Food Chem. 2020 Nov 30;331:127322. doi: 10.1016/j.foodchem.2020.127322. Epub 2020 Jun 11.
Here we report a novel strategy for the immobilization of invertase using amyloid-like fibrils as a support. Optimal conditions to get Tyr-Tyr covalent binding between invertase and the support were determined using a photocrosslinking approach. The biological fibrils with invertase activity turn into microstructured catalysts according to electron microscopy outcomes. Thermal and storage stability as well as optimal pH and temperature of the enzyme were conserved. Moreover, the immobilized enzyme recovered by low g-force centrifugation retained 83% of its initial enzymatic activity after 15 reuse cycles. Considering that enzyme cost is the most significant part of the overall fee of enzymatic biomass conversion, the highly efficient recovery/reuse strategy described herein becomes relevant. Besides, it can also be applied to the immobilization of other enzymes for industrial biocatalysis.
在这里，我们报告了一种使用类似淀粉样纤维作为载体固定转化酶的新策略。使用光交联方法确定了获得转化酶和载体之间 Tyr-Tyr 共价结合的最佳条件。根据电子显微镜结果，具有转化酶活性的生物纤维变成微结构催化剂。热稳定性和储存稳定性以及酶的最佳 pH 值和温度得以保留。此外，通过低离心力回收的固定化酶在 15 次重复使用循环后保留了其初始酶活性的 83%。考虑到酶成本是酶生物质转化总成本的最重要部分，因此本文所述的高效回收/再利用策略变得相关。此外，它还可以应用于其他酶的固定化，用于工业生物催化。
