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Coexpression of β-D-galactosidase and L-arabinose Isomerase in the Production of D-tagatose: A Functional Sweetener

Yijing Zhan, Zheng Xu, Sha Li, Xiaoliu Liu, Lu Xu, Xiaohai Feng, Hong Xu

J Agric Food Chem. 2014 Mar 19;62(11):2412-7.

PMID: 24568679

Abstract:

The functional sweetener, d-tagatose, is commonly transformed from galactose by l-arabinose isomerase. To make use of a much cheaper starting material, lactose, hydrolization, and isomerization are required to take place collaboratively. Therefore, a single-step method involving β-d-galactosidase was explored for d-tagatose production. The two vital genes, β-d-galactosidase gene (lacZ) and l-arabinose isomerase mutant gene (araA') were extracted separately from Escherichia coli strains and incorporated into E. coli simultaneously. This gave us E. coli-ZY, a recombinant producing strain capable of coexpressing the two key enzymes. The resulted cells exhibited maximum d-tagatose producing activity at 34 °C and pH 6.5 and in the presence of borate, 10 mM Fe(2+), and 1 mM Mn(2+). Further monitoring showed that the recombinant cells could hydrolyze more than 95% lactose and convert 43% d-galactose into d-tagatose. This research has verified the feasibility of single-step d-tagatose fermentation, thereby laying down the foundation for industrial usage of lactose.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
AP9031112-C β-Galactosidase, E. coli β-Galactosidase, E. coli 9031-11-2 Price
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