Screening of food-grade microorganisms for biotransformation of D-tagatose and cloning and expression of L-arabinose isomerase.
- Author:
Yan MEN
1
;
Yueming ZHU
;
Yuping GUAN
;
Tongcun ZHANG
;
Ken IZUMORI
;
Yuanxia SUN
Author Information
1. College of Biology Engineering, Tianjin University of Science and Technology, Tianjin 300457, China.
- Publication Type:Journal Article
- MeSH:
Aldose-Ketose Isomerases;
biosynthesis;
genetics;
Biotransformation;
Cloning, Molecular;
Escherichia coli;
genetics;
metabolism;
Galactose;
metabolism;
Genetic Vectors;
genetics;
Hexoses;
metabolism;
Pediococcus;
classification;
genetics;
isolation & purification;
Recombinant Proteins;
biosynthesis;
genetics
- From:
Chinese Journal of Biotechnology
2012;28(5):592-601
- CountryChina
- Language:Chinese
-
Abstract:
L-Arabinose isomerase (L-AI) is an intracellular enzyme that catalyzes the reversible isomerization of D-galactose and D-tagatose. Given the widespread use of D-tagatose in the food industry, food-grade microorganisms and the derivation of L-AI for the production of D-tagatose is gaining increased attention. In the current study, food-grade strains from different foods that can convert D-galactose to D-tagatose were screened. According to physiological, biochemical, and 16S rDNA gene analyses, the selected strain was found to share 99% identity with Pediococcus pentosaceus, and was named as Pediococcus pentosaceus PC-5. The araA gene encoding L-AI from Pediococcus pentosaceus PC-5 was cloned and overexpressed in E. coli BL21. The yield of D-tagatose using D-galactose as the substrate catalyzed by the crude enzyme in the presence of Mn2+ was found to be 33% at 40 degrees C.
