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β-半乳糖苷酶的挑战与展望。

Challenges and perspectives of the β-galactosidase enzyme.

机构信息

Faculty of Agronomy and Veterinary Medicine (FAMV), Postgraduate Program in Food Science and Technology (PPGCTA), University of Passo Fundo (UPF), Passo Fundo, RS, Brazil.

Faculty of Engineering and Architecture (FEAR), Chemical Engineering Course, University of Passo Fundo (UPF), Passo Fundo, RS, Brazil.

出版信息

Appl Microbiol Biotechnol. 2021 Jul;105(13):5281-5298. doi: 10.1007/s00253-021-11423-7. Epub 2021 Jul 5.

DOI:10.1007/s00253-021-11423-7
PMID:34223948
Abstract

The enzyme β-galactosidase has great potential for application in the food and pharmaceutical industries due to its ability to perform the hydrolysis of lactose, a disaccharide present in milk and in dairy by-products. It can be used in free form, in batch processes, or in immobilized form, which allows continuous operation and provides greater enzymatic stability. The choice of method and support for enzyme immobilization is essential, as the performance of the biocatalyst is strongly influenced by the properties of the material used and by the interaction mechanisms between support and enzyme. Therefore, this review showed the main enzyme immobilization techniques, and the most used supports for the constitution of biocatalysts. Also, materials with the potential for immobilization of β-galactosidases and the importance of their biotechnological application are presented. KEY POINTS: • The main methods of immobilization are physical adsorption, covalent bonding, and crosslinking. • The structural conditions of the supports are determining factors in the performance of the biocatalysts. • Enzymatic hydrolysis plays an important role in the biotechnology industry.

摘要

β-半乳糖苷酶由于能够水解乳糖(牛奶和乳制品副产物中的一种二糖),因此在食品和制药行业具有很大的应用潜力。它可以以游离形式、分批处理或固定化形式使用,这允许连续操作并提供更高的酶稳定性。酶固定化方法和载体的选择至关重要,因为生物催化剂的性能受所用材料的性质和载体与酶之间的相互作用机制的强烈影响。因此,本文综述了主要的酶固定化技术以及构成生物催化剂最常用的载体。还介绍了具有固定化β-半乳糖苷酶潜力的材料及其在生物技术应用中的重要性。关键点:

  1. 主要的固定化方法是物理吸附、共价键合和交联。

  2. 载体的结构条件是生物催化剂性能的决定因素。

  3. 酶水解在生物技术行业中起着重要作用。

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