BACKGROUND β-glucosidases (BGs) catalyze the hydrolysis of β-glycosidic bonds in glucose derivatives. They constitute an important group of enzymes with biotechnological interest like supporting cellulases in degradation of lignocellulose to fermentable sugars. In the latter context, the glucose tolerant BGs are of particular interest. These BGs often show peculiar kinetics, including inhibitor...

The supernatants (the solution part received after centrifugation) of squid pens fermented by four species of Paenibacillus showed potent inhibitory activity against α-glucosidases derived from yeast (79-98%) and rats (76-83%). The inhibition of acarbose-a commercial antidiabetic drug, used against yeast and rat α-glucosidases-was tested for comparison; it showed inhibitory activity of 64% and ...

Lower termites need symbiotic microbes for cellulose digestion. Elizabethkingia miricola strain BM10 has been proposed as a microbe that assists in low-temperature digestion and metabolism of Reticulitermes speratus KMT1, termite on Bukhan Mountain, Seoul, Korea. In E. BM10, β-glucosidase genes expressed at 10°C were identified, the psychrophilic enzymatic characteristic was confirmed by hetero...

BACKGROUND Postprandial hyperglycemia is an early defect of type 2 diabetes and one of primary anti-diabetic targets. Treatment of postprandial hyperglycemia can be achieved by inhibiting intestinal α-glucosidase, the key enzyme for oligosaccharide digestion and further glucose absorption. Grape pomace is winemaking byproduct rich in bioactive food compounds such as phenolic antioxidants. This ...

BACKGROUND Enzyme end-product inhibition is a major challenge in the hydrolysis of lignocellulose at a high dry matter consistency. β-glucosidases (BGs) hydrolyze cellobiose into two molecules of glucose, thereby relieving the product inhibition of cellobiohydrolases (CBHs). However, BG inhibition by glucose will eventually lead to the accumulation of cellobiose and the inhibition of CBHs. Ther...

Here the statistics concerning X-ray data processing and structure refinement are given, together with the substrate preference analysis for ThBgl1 and ThBgl2. Finally, the analysis of the influence of temperature and pH on the activities of both enzymes are shown.