Abstract

The highly demanding conditions of industrial processes may lower the stability and affect the activity of enzymes used as biocatalysts. Enzyme immobilization emerged as an approach to promote stabilization and easy removal of enzymes for their reusability. The aim of this review is to go through the principal immobilization strategies addressed to achieve optimal industrial processes with special care on those reported for two types of enzymes: β-galactosidases and fructosyltransferases. The main methods used to immobilize these two enzymes are adsorption, entrapment, covalent coupling and cross-linking or aggregation (no support is used), all of them having pros and cons. Regarding the support, it should be cost-effective, assure the reusability and an easy recovery of the enzyme, increasing its stability and durability. The discussion provided showed that the type of enzyme, its origin, its purity, together with the type of immobilization method and the support will affect the performance during the enzymatic synthesis. Enzymes’ immobilization involves interdisciplinary knowledge including enzymology, nanotechnology, molecular dynamics, cellular physiology and process design. The increasing availability of facilities has opened a variety of possibilities to define strategies to optimize the activity and re-usability of β-galactosidases and fructosyltransferases, but there is still great place for innovative developments.

摘要

工业过程的高要求条件可能会降低稳定性并影响用作生物催化剂的酶的活性。酶固定化作为一种​​促进稳定和易于去除酶的方法出现，以实现其可重复使用性。这篇综述的目的是通过主要的固定化策略来实现最佳的工业过程，特别注意那些报道的两种酶：β-半乳糖苷酶和果糖基转移酶。用于固定这两种酶的主要方法是吸附、截留、共价偶联和交联或聚集（不使用支持物），它们各有利弊。关于支持，它应该具有成本效益，确保酶的可重复使用性和容易回收，增加其稳定性和耐用性。所提供的讨论表明，酶的类型、来源、纯度以及固定方法和载体的类型将影响酶促合成过程中的性能。酶的固定化涉及跨学科知识，包括酶学、纳米技术、分子动力学、细胞生理学和工艺设计。设施可用性的增加为定义优化 β-半乳糖苷酶和果糖基转移酶的活性和可重用性的策略提供了多种可能性，但仍有很大的创新发展空间。酶的固定化涉及跨学科知识，包括酶学、纳米技术、分子动力学、细胞生理学和工艺设计。设施可用性的增加为定义优化 β-半乳糖苷酶和果糖基转移酶的活性和可重用性的策略提供了多种可能性，但仍有很大的创新发展空间。酶的固定化涉及跨学科知识，包括酶学、纳米技术、分子动力学、细胞生理学和工艺设计。设施可用性的增加为定义优化 β-半乳糖苷酶和果糖基转移酶的活性和可重用性的策略提供了多种可能性，但仍有很大的创新发展空间。