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- W3016688230 abstract "Lipases are the main fat digestive enzymes present in the digestive system of many animals, microorganisms and plants. Probiotic microorganisms that can possibly produce enzymes are of crucial importance since it can have an effect on human health. Two of the main probiotic strains are Lactobacillus rhamnosus and Biffidobacterium longum, in each there was a putative lipase encoded on the DNA and there is lack of information on these two putative lipases. Both strains are Gram-positive and anaerobic which adds an extra difficulty on the production of the enzymes. For that reason, recombinant production of the enzymes was chosen. Recombinant production was carried out at first with three strains of E. coli to establish the best one for the production. Production of the lipases was possible with the E. coli BL21 (DE3) strain and the same strain was used to test the possible bioreactor scale production using a 2.5 L counter top bioreactor. Once the best strain was chosen; the production in lab scale was tried and then purification of the lipases was tested with Ion Metal Affinity Chromatography (IMAC). With established production and purification, the kinetic characterization of the putative lipases was carried out and it included calculation of the activity constants, determination of optimal temperature and pH and activity over long storage time. Oligomerization of the lipases on the optimal conditions was tested using Asymmetric flow-field flow fractionation (AF4). The production of the lipases was successful in both lab scale and bioreactor scale and then the characterization was conducted on those lipases produced by the trials. Activity was measured and the kinetic parameters were established showing substrate inhibition for the Lactobacillus rhamnosus (LR) lipase while the Biffidobacterium longum (BL) lipase never reached the substrate saturation plateau. The optimal conditions were determined and they were matching the physiological conditions of pH 6-7 and temperature of 30°C - 40°C. Storage time at 37°C was established and the LR lipase had a half time of 3 days while the BL lipase was not stable at that temperature. From AF4 analysis both lipases seem to be as monomers in the optimal conditions but the results are not conclusive. (Less)" @default.
- W3016688230 created "2020-04-24" @default.
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- W3016688230 date "2020-01-01" @default.
- W3016688230 modified "2023-09-27" @default.
- W3016688230 title "Study on putative lipases from Bifidobactirium longum and Lactobacillus rhamnosus" @default.
- W3016688230 hasPublicationYear "2020" @default.
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