Abstract:-Lactobionic acid has a number of applications, such as in cosmetic formulations and detergents, as well as in the medical field, where it is used for the preservation of organs destined for transplantation. Previous studies have reported that a promising alternative procedure for the production of lactobionic acid is the biotechnological route, using permeabilized cells of Zymomonas mobilis to produce sorbitol and lactobionic acid from fructose and lactose. However, the acid produced during the process accumu… Show more
“…The Chemical Engineering Program’s Bioprocesses Laboratory at COPPE, Federal University of Rio de Janeiro, Brazil, has used the bacterium Zymomonas mobilis for years to study the production of various substances, like ethanol, glyconic acid, sorbitol, lactobionic acid, and L-asparaginase [ 11 – 16 ]. The L-asparaginase obtained from Z .…”
L-asparaginase is an enzyme used as a chemotherapeutic agent, mainly for treating acute lymphoblastic leukemia. In this study, the gene of L-asparaginase from Zymomonas mobilis was cloned in pET vectors, fused to a histidine tag, and had its codons optimized. The L-asparaginase was expressed extracellularly and intracellularly (cytoplasmically) in Escherichia coli in far larger quantities than obtained from the microorganism of origin, and sufficient for initial cytotoxicity tests on leukemic cells. The in silico analysis of the protein from Z. mobilis indicated the presence of a signal peptide in the sequence, as well as high identity to other sequences of L-asparaginases with antileukemic activity. The protein was expressed in a bioreactor with a complex culture medium, yielding 0.13 IU/mL extracellular L-asparaginase and 3.6 IU/mL intracellular L-asparaginase after 4 h of induction with IPTG. The cytotoxicity results suggest that recombinant L-asparaginase from Z. mobilis expressed extracellularly in E.coli has a cytotoxic and cytostatic effect on leukemic cells.
“…The Chemical Engineering Program’s Bioprocesses Laboratory at COPPE, Federal University of Rio de Janeiro, Brazil, has used the bacterium Zymomonas mobilis for years to study the production of various substances, like ethanol, glyconic acid, sorbitol, lactobionic acid, and L-asparaginase [ 11 – 16 ]. The L-asparaginase obtained from Z .…”
L-asparaginase is an enzyme used as a chemotherapeutic agent, mainly for treating acute lymphoblastic leukemia. In this study, the gene of L-asparaginase from Zymomonas mobilis was cloned in pET vectors, fused to a histidine tag, and had its codons optimized. The L-asparaginase was expressed extracellularly and intracellularly (cytoplasmically) in Escherichia coli in far larger quantities than obtained from the microorganism of origin, and sufficient for initial cytotoxicity tests on leukemic cells. The in silico analysis of the protein from Z. mobilis indicated the presence of a signal peptide in the sequence, as well as high identity to other sequences of L-asparaginases with antileukemic activity. The protein was expressed in a bioreactor with a complex culture medium, yielding 0.13 IU/mL extracellular L-asparaginase and 3.6 IU/mL intracellular L-asparaginase after 4 h of induction with IPTG. The cytotoxicity results suggest that recombinant L-asparaginase from Z. mobilis expressed extracellularly in E.coli has a cytotoxic and cytostatic effect on leukemic cells.
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