Enzymatic Synthesis of Oligosaccharides, Alkyl and Terpenyl Glucosides, by Recombinant Escherichia coli-Expressed Pichia etchellsii β-Glucosidase II

2004 ◽  
Vol 118 (1-3) ◽  
pp. 269-282 ◽  
Author(s):  
Preeti Bachhawat ◽  
Saroj Mishra ◽  
Yukti Bhatia ◽  
V. S. Bisaria
Keyword(s):  
Escherichia Coli ◽  
Enzymatic Synthesis ◽  
Glucosidase Ii ◽  
Pichia Etchellsii

Expression and characterization of Pichia etchellsii β-glucosidase in Escherichia coli

Gene ◽  
1997 ◽  
Vol 190 (1) ◽  
pp. 45-51 ◽  
Author(s):  
Manjula Pandey ◽  
Saroj Mishra
Keyword(s):  
Escherichia Coli ◽  
Pichia Etchellsii

scholarly journals Enzymatic synthesis of nucleosides by nucleoside phosphorylase co-expressed in Escherichia coli

2010 ◽  
Vol 11 (11) ◽  
pp. 880-888 ◽  
Author(s):  
Qing-bao Ding ◽  
Ling Ou ◽  
Dong-zhi Wei ◽  
Xiao-kun Wei ◽  
Yan-mei Xu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Enzymatic Synthesis ◽  
Nucleoside Phosphorylase

scholarly journals Heterologous Expression of a Thermostable α-Glucosidase from Geobacillus sp. Strain HTA-462 by Escherichia coli and Its Potential Application for Isomaltose–Oligosaccharide Synthesis

Molecules ◽  
2019 ◽  
Vol 24 (7) ◽  
pp. 1413
Author(s):  
Fan Zhang ◽  
Weiyang Wang ◽  
Fatoumata Binta Maci Bah ◽  
Chengcheng Song ◽  
Yifa Zhou ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Enzymatic Synthesis ◽  
Bacillus Stearothermophilus ◽  
Maximal Activity ◽  
Oligosaccharide Synthesis ◽  
Optimum Temperature ◽  
Divalent Ions ◽  
Food Ingredients ◽  
Shake Flasks ◽  
Maltose Syrup

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.

Enzymatic synthesis of cell wall mucopeptide in a particulate preparation of Escherichia coli

1966 ◽  
Vol 23 (4) ◽  
pp. 466-472 ◽  
Author(s):  
Y. Araki ◽  
R. Shirai ◽  
A. Shimada ◽  
N. Ishimoto ◽  
E. Ito
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Enzymatic Synthesis

Enzymatic synthesis of L-aspartic acid by Escherichia coli cultured with a cost-effective corn plasm medium

2014 ◽  
Vol 64 (4) ◽  
pp. 1615-1621 ◽  
Author(s):  
Genhai Zhao ◽  
Guohong Gong ◽  
Peng Wang ◽  
Li Wang ◽  
Hui Liu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Aspartic Acid ◽  
Enzymatic Synthesis ◽  
Cost Effective
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