Synthesis of γ-L-Glutamylalkylamides Catalyzed by Escherichia coli Having γ-Glutamyltranspeptidase Activity

Advanced Materials Research ◽

10.4028/www.scientific.net/amr.550-553.1177 ◽

2012 ◽

Vol 550-553 ◽

pp. 1177-1181

Author(s):

Fei Zhang ◽

Yin Liu ◽

Pei Xin He

Keyword(s):

Escherichia Coli ◽

Substrate Specificity ◽

Conversion Rate ◽

Medicinal Value

γ-L-glutamyl alkylamines have potential medicinal value. In this research, five different γ-L-glutamyl alkylamines were synthesized. The result showed that substrate specificity of alkylamines, from high to low, is methylamine, ethylamine, n-propylamine, isopropylamine and n-butylamine. The reaction was optimal at pH 9.5 and 45°C, and the optimal substrate mole ratio of L-glutamine to alkylamine was 1:3 (mol/mol).Under these conditions, conversion rate of L-glutamine is about 90% (mol/mol)．

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Faculty Opinions recommendation of The C-terminal domain of the nucleotide-binding domain protein Wzt determines substrate specificity in the ATP-binding cassette transporter for the lipopolysaccharide O-antigens in Escherichia coli serotypes O8 and O9a.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1027346.328490 ◽

2005 ◽

Author(s):

Miguel Valvano

Keyword(s):

Escherichia Coli ◽

Substrate Specificity ◽

Nucleotide Binding ◽

Binding Domain ◽

Atp Binding ◽

Nucleotide Binding Domain ◽

Terminal Domain ◽

Atp Binding Cassette Transporter ◽

Domain Protein ◽

O Antigens

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Expression and characterization of an α-glucosidase from Thermoanaerobacter ethanolicus JW200 with potential for industrial application

Biologia ◽

10.2478/s11756-009-0197-1 ◽

2009 ◽

Vol 64 (6) ◽

Cited By ~ 9

Author(s):

Yue-Hong Wang ◽

Yu Jiang ◽

Zuo-Ying Duan ◽

Wei-Lan Shao ◽

Hua-Zhong Li

Keyword(s):

Escherichia Coli ◽

Heat Shock ◽

Optimal Condition ◽

Industrial Application ◽

Conversion Rate ◽

Hydrolytic Activity ◽

Thermoanaerobacter Ethanolicus ◽

Transglycosylation Activity

AbstractIn this study, a new α-glucosidase gene from Thermoanaerobacter ethanolicus JW200 was cloned and expressed in Escherichia coli by a novel heat-shock vector pHsh. The recombinant α-glucosidase exhibited its maximum hydrolytic activity at 70°C and pH 5.0∼5.5. With p-nitrophenyl-α-D-glucoside as a substrate and under the optimal condition (70°C, pH 5.5), K m and V max of the enzyme was 1.72 mM and 39 U/mg, respectively. The purified α-glucosidase could hydrolyze oligosaccharides with both α-1,4 and α-1,6 linkages. The enzyme also had strong transglycosylation activity when maltose was used as sugar donor. The transglucosylation products towards maltose are isomaltose, maltotriose, panose, isomaltotriose and tetrasaccharides. The enzyme could convert 400 g/L maltose to oligosaccharides with a conversion rate of 52%, and 83% of the oligosaccharides formed were prebiotic isomaltooligosaccharides (containing isomaltose, panose and isomaltotriose).

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