Oh Deok-Kun
Department of Bioscience and Biotechnology, Konkuk University, 1 Hwayang-Dong Gwangjin-Gu, Seoul, 143-701, South Korea.
Appl Microbiol Biotechnol. 2007 Aug;76(1):1-8. doi: 10.1007/s00253-007-0981-1. Epub 2007 May 10.
D-Tagatose has attracted a great deal of attention in recent years due to its health benefits and similar properties to sucrose. D-Tagatose can be used as a low-calorie sweetener, as an intermediate for synthesis of other optically active compounds, and as an additive in detergent, cosmetic, and pharmaceutical formulation. Biotransformation of D-tagatose has been produced using several biocatalyst sources. Among the biocatalysts, L-arabinose isomerase has been mostly applied for D-tagatose production because of the industrial feasibility for the use of D-galactose as a substrate. In this article, the characterization of many L-arabinose isomerases and their D-tagatose production is compared. Protein engineering and immobilization of the enzyme for increasing the conversion rate of D-galactose to D-tagatose are also reviewed.
近年来，D-塔格糖因其对健康有益且性质与蔗糖相似而备受关注。D-塔格糖可用作低热量甜味剂、合成其他旋光性化合物的中间体，以及洗涤剂、化妆品和药物制剂中的添加剂。已使用多种生物催化剂来源生产D-塔格糖的生物转化。在这些生物催化剂中，L-阿拉伯糖异构酶由于使用D-半乳糖作为底物具有工业可行性，因而在D-塔格糖生产中应用最为广泛。本文比较了多种L-阿拉伯糖异构酶的特性及其D-塔格糖生产情况。还综述了通过蛋白质工程和酶固定化来提高D-半乳糖向D-塔格糖的转化率。
