Improved substrate specificity for D-galactose of L-arabinose isomerase for industrial application

Add time:07/27/2019    Source:sciencedirect.com

L-Arabinose isomerase isolated from Geobacillus stearothermophilus (GSAI) was modified to improve its substrate specificity for D-galactose for the production of D-tagatose, a potential reduced-energy sweetener. Among the selected residues, mutation at residue 18 produced a mutant strain, H18T, which exhibited increased activity for D-galactose compared with the wild-type (WT) enzyme. Analysis of the substrate specificity of H18T showed a 45.4% improvement for D-galactose. Replacing histidine with threonine at residue 18 resulted in approximately 2.7-fold and 1.8-fold higher substrate binding and catalytic efficiency, respectively, for D-galactose. Further enhancement of the specific activity and catalytic efficiency of H18T for D-galactose by up to 2.7-fold and 4.3-fold, respectively, was achieved by adding borate during L-arabinose isomerase catalysis. Moreover, H18T showed thermostability and no destabilization was detected, which is promising for the industrial production of D-tagatose.

We also recommend Trading Suppliers and Manufacturers of D-(+)-GALACTOSE (cas 10257-28-0). Pls Click Website Link as below: cas 10257-28-0 suppliers

Prev:Effects of sulforaphane on D-galactose-induced liver aging in rats: Role of keap-1/nrf-2 pathway.
Next:Structural changes of orthorhombic α-D-galactose crystal by using Raman spectroscopy at high pressure)