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Published on: February 17, 2017
Tagatose: properties, applications, and biotechnological processes.
1Department of Bioscience and Biotechnology, Konkuk University, 1 Hwayang-Dong Gwangjin-Gu, Seoul, 143-701, South Korea. deokkun@konkuk.ac.kr
Applied Microbiology and Biotechnology
|May 12, 2007
Summary
D-Tagatose, a low-calorie sweetener, can be produced from D-galactose using L-arabinose isomerase. This review compares enzyme characteristics and discusses protein engineering for improved D-tagatose production.
Area of Science:
- Biotechnology and Biocatalysis
- Carbohydrate Chemistry
- Enzyme Engineering
Background:
- D-Tagatose is a functional sweetener with health benefits, similar to sucrose.
- It serves as a low-calorie sweetener and a versatile intermediate in chemical synthesis.
- D-Tagatose finds applications in food, detergent, cosmetic, and pharmaceutical industries.
Purpose of the Study:
- To compare the characterization of various L-arabinose isomerases for D-tagatose production.
- To review methods for enhancing D-tagatose yield from D-galactose.
- To explore protein engineering and enzyme immobilization strategies.
Main Methods:
- Comparative analysis of L-arabinose isomerase characteristics.
- Review of biotransformation processes for D-tagatose synthesis.
- Examination of protein engineering and immobilization techniques.
Main Results:
- L-arabinose isomerase is a key biocatalyst for D-tagatose production from D-galactose.
- Enzyme characteristics significantly influence D-tagatose conversion efficiency.
- Protein engineering and immobilization show potential for increased yield.
Conclusions:
- L-arabinose isomerases are industrially relevant for D-tagatose production.
- Optimizing enzyme properties through engineering and immobilization is crucial for efficient biotransformation.
- Further research can enhance the economic viability of D-tagatose manufacturing.
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