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Characterization of recombinant aminoacylase from Escherichia coli

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dc.contributor.author YEPREMYAN, H.
dc.date.accessioned 2024-02-12T08:56:56Z
dc.date.available 2024-02-12T08:56:56Z
dc.date.issued 2022
dc.identifier.citation YEPREMYAN, H. Characterization of recombinant aminoacylase from Escherichia coli. In: International Scientific Conference on Microbial Biotechnology, 5th edition, Chișinău, Moldova, October 12-13, 2022. Chişinău, 2022, p. 108-110. ISBN 978-9975-3555-6-8; ISBN 978-9975-3555-7-5. en_US
dc.identifier.isbn 978-9975-3555-6-8
dc.identifier.isbn 978-9975-3555-7-5
dc.identifier.uri https://doi.org/10.52757/imb22.75
dc.identifier.uri http://repository.utm.md/handle/5014/26355
dc.description.abstract In this study, we report on characterization of the recombinant intracellular aminoacylase from E. coli LGE36 with high levels of aminoacylase activity and wide substrate specificity. The E. coli aminoacylase showed higher activity towards α-N-acetyl-L-ornithine and α-N-acetyl-L-lysine rather than towards N-acetyl-L-methionine. The comparison of the substrate specificity of the recombinant intracellular aminoacylase from E. coli with other members of the aminoacylase family suggests an origin of the obtained enzyme. en_US
dc.language.iso en en_US
dc.publisher Institute of Microbiology and Biotechnology, Republic of Moldova en_US
dc.relation.ispartofseries International scientific conference "Microbial Biotechnology", 5th edition, 12-13 October 2022, Chisinau, Republic of Moldova;
dc.rights Attribution-NonCommercial-NoDerivs 3.0 United States *
dc.rights.uri http://creativecommons.org/licenses/by-nc-nd/3.0/us/ *
dc.subject enzymes en_US
dc.subject amino acids en_US
dc.subject Bacteria en_US
dc.subject Escherichia coli en_US
dc.subject Enterobacteriaceae en_US
dc.title Characterization of recombinant aminoacylase from Escherichia coli en_US
dc.type Article en_US


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