7485-51-0Relevant articles and documents
Heterologous expression of a thermostable α-glucosidase from Geobacillus sp. Strain HTA-462 by Escherichia coli and its potential application for isomaltose–oligosaccharide synthesis
Zhang, Fan,Wang, Weiyang,Bah, Fatoumata Binta Maci,Song, Chengcheng,Zhou, Yifa,Ji, Li,Yuan, Ye
, (2019/05/02)
Isomaltose–oligosaccharides (IMOs), as food ingredients with prebiotic functionality, can be prepared via enzymatic synthesis using α-glucosidase. In the present study, the α-glucosidase (GSJ) from Geobacillus sp. strain HTA-462 was cloned and expressed in Escherichia coli BL21 (DE3). Recombinant GSJ was purified and biochemically characterized. The optimum temperature condition of the recombinant enzyme was 65 ?C, and the half-life was 84 h at 60 ?C, whereas the enzyme was active over the range of pH 6.0–10.0 with maximal activity at pH 7.0. The α-glucosidase activity in shake flasks reached 107.9 U/mL and using 4-Nitrophenyl β-D-glucopyranoside (pNPG) as substrate, the Km and Vmax values were 2.321 mM and 306.3 U/mg, respectively. The divalent ions Mn2+ and Ca2+ could improve GSJ activity by 32.1% and 13.8%. Moreover, the hydrolysis ability of recombinant α-glucosidase was almost the same as that of the commercial α-glucosidase (Bacillus stearothermophilus). In terms of the transglycosylation reaction, with 30% maltose syrup under the condition of 60 ?C and pH 7.0, IMOs were synthesized with a conversion rate of 37%. These studies lay the basis for the industrial application of recombinant α-glucosidase.
COMBINED USE OF DIPEPTIDYL PEPTIDASE IV INHIBITOR COMPOUND AND SWEETENER
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, (2010/01/29)
The present invention provides a novel therapeutic or preventive method, a pharmaceutical composition and use thereof, that exhibit superior anti-obesity effects (body weight-reducing (losing) effects and/or body fat mass-reducing effects). Specifically, the present invention provides a pharmaceutical composition comprising the combination of a dipeptidyl peptidase 4 inhibitor and a sweetener having a GLP-1 secretion-stimulating action, as well as use thereof for the manufacture of a medicament. The present invention also provides a method for treating or preventing obesity, comprising administering an effective amount of (a) a dipeptidyl peptidase 4 inhibitor and (b) a sweetener having a GLP-1 secretion-stimulating action to a patient suffering from symptoms of obesity.
Heterologous expression and biochemical characterization of α-glucosidase from aspergillus niger by pichia pastroris
Chen, Dong-Li,Tong, Xing,Chen, Shang-Wei,Chen, Sheng,Wu, Dan,Fang, Shu-Guang,Wu, Jing,Chen, Jian
experimental part, p. 4819 - 4824 (2011/08/03)
The aglu of Aspergillus niger encodes the pro-protein of α-glucosidase, and the mature form of wild-type enzyme is a heterosubunit protein. In the present study, the cDNA of α-glucosidase was cloned and expressed in Pichia pastoris strain KM71. The activity of recombinant enzyme in a 3 L fermentor reached 2.07 U/mL after 96 h of induction. The recombinant α-glucosidase was able to produce oligoisomaltose. The molecular weight of the recombinant enzyme was estimated to be about 145 kDa by SDS-PAGE, and it reduced to 106 kDa after deglycosylation. The enzymatic activity of recombinant α-glucosidase was not significantly affected by a range of metal ions. The optimum temperature of the enzyme was 60 °C, and it was stable below 50 °C. The enzyme was active over the range of pH 3.0-7.0 with maximal activity at pH 4.5. Using pNPG as substrate, the Km and Vmax values were 0.446 mM and 43.48 U/mg, respectively. These studies provided the basis for the application of recombinant α-glucosidase in the industry of functional oligosaccharides.
