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https://www.selleckchem.com/products/gdc-0084.html The minor flavonoid baohuoside I from Herba epimedii has better bioactivities than its precursor compounds icariin and other major epimedium flavonoids. In this study, a novel β-glucosidase gene (Igag_0940) was cloned and expressed to improve the conversion efficiency in the process of baohuoside I production. For the first time, the recombinant IagBgl1 was purified and then identified uniquely as a trimer in GH 1 family protein from Archaea. The maximum activity of recombinant IagBgl1 was exhibited at 95 °C, pH 6.5, and it retained more than 70% after incubation at 90 °C for 4 h. IagBgl1 had a high catalytic activity towards icariin with a Kcat/Km ratio of 488.19 mM-1·s-1. Under optimized conditions (65 °C, pH 6.5, 0.8 U/mL enzyme, and 90 min), 10 g/L icariin was transformed into 7.564 g/L baohuoside I with a molar conversion of 99.48%. Meanwhile, 2.434 g/L baohuoside I was obtained from 10 g/L total epimedium flavonoids by a two-step conversion system built with IagBgl1 and two other thermostable enzymes. This is the first report of enzymatic conversion for producing baohuoside I by thermostable enzymes.Nowadays, the discovery and development of α-glucosidase inhibitors from natural products or their derivatives represents an attractive approach. Here we reported studies on a series of novel N-acyl-2-aminothiazoles fused (+)-nootkatone and evaluation for their α-glucosidase inhibitory activities. Most of (+)-nootkatone derivatives exhibited more potent α-glucosidase inhibitory ability than the positive drug acarbose. In particular, compounds II7 and II14 showed the most promising α-glucosidase inhibitory ability with IC50 values of 13.2 and 13.8 µM. II7 and II14 also exhibited relatively low cytotoxicities towards normal LO2 cells. Kinetic study indicated that compounds II7 and II14 inhibited the α-glucosidase in a noncompetitive manner, and molecular docking results were in line with the noncompetitive characteri

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