Properties and applications of β‐glycosidase from Bacteroides thetaiotaomicron that specifically hydrolyses isoflavone glycosides

To modify the glycan part of glycosides, the gene encoding β‐glycosidase was cloned from Bacteroides thetaiotaomicron VPI‐5482. The cloned gene, bt_1780, was expressed in Escherichia coli MC1061 and the expressed enzyme was purified using Ni‐NTA affinity chromatography. The purified enzyme, BTBG, showed optimal activity at 50 °C and pH 5.5. Interestingly, this enzyme did not have any hydrolysing activity on ordinary β‐linkage–containing substrates such as xylobiose, lactose and cello‐oligosaccharide, but specifically hydrolysed isoflavone glycosides such as daidzin, genistin and glycitin. Compared to a commercial beta glucosidase, BTBG selectively hydrolysed isoflavone glycosides in soybean extract mixture solution. These results suggest that BTBG may be a specialized enzyme for the hydrolysis of glycosides and that the substrate specificity of BTBG is applicable for the bioconversion of isoflavone glycosides in the food industry.     

InGaN microring light-emitting diodes

The fabrication and performance of an InGaN light-emitting diode (LED) array based on a microring device geometry is reported. This design has been adopted in order to increase the surface area for light extraction and to minimize losses due to internal reflections and reabsorption. Electrical characteristics of these devices are similar to those of a conventional large-area LED, while the directed light extraction proves to be superior. In fact, these devices are found to be more efficient when operated at higher currents. This may be attributed to improved heat sinking due to the large surface area to volume ratio. The potential applications of these devices are also discussed.