Supplementary data for article: Bihelović, F.; Karadžić, I.; Matović, R.; Saičić, R. Total Synthesis and Biological Evaluation of (-)-Atrop-Abyssomicin C. Organic and Biomolecular Chemistry 2013, 11 (33), 5413–5424. https://doi.org/10.1039/c3ob40692j

Supplementary material for: [https://doi.org/10.1039/c3ob40692j]Related to published version: [http://cherry.chem.bg.ac.rs/handle/123456789/1388

Influence of rhamnolipids, produced by Pseudomonas aeruginosa NCAIM(P), B001380 on Cr(VI) removal capacity in liquid medium

Pseudomonas aeruginosa NCAIM(P), B001380, a propitious bacterial strain isolated from mineral cutting oil was identified to be chromium tolerant and a producer of biosurfactant rhamnolipid (RL) with potential application in heavy metal bioremediation. Culture growth, RL production and Cr(VI) removal capacity of the strain in the presence of 50 mg L-1 (I) and 100 mg L-1 of Cr(VI) (II) were studied. Maximum of RL production were found in the late-stationary phase at 72 h for both Cr(VI)-amended cultures: I (236 mg L-1) and II (160 mg L-1), as well as the maximum of Cr(VI) removal capacity: 70 % (I) and 57 % (II). The amount of Cr in RL preparation II was 22 mg mg-1 determined by flame atomic absorption spectroscopy (FAAS). Appearance of a new band at 914 cm-1 in infrared (IR) spectrum of RL (II) indicated a significant proof for possible coordination of CrO42-ion with RL. The effect of Cr(VI) on monorhamnolipids (RL1) and dirhamnolipids (RL2) distribution and its ratio were studied by electrospray ionization mass spectrometry (ESI-MS). An increase was observed in a RL2/RL1 ratio for II compared to control

Supplementary data for article: Bihelović, F.; Karadžić, I.; Matović, R.; Saičić, R. Total Synthesis and Biological Evaluation of (-)-Atrop-Abyssomicin C. Organic and Biomolecular Chemistry 2013, 11 (33), 5413–5424. https://doi.org/10.1039/c3ob40692j

Supplementary material for: [https://doi.org/10.1039/c3ob40692j]Related to published version: [http://cherry.chem.bg.ac.rs/handle/123456789/1388

Supplementary data for the article: Medić, A.; Lješević, M.; Inui, H.; Beškoski, V.; Kojić, I.; Stojanović, K.; Karadžić, I. Efficient Biodegradation of Petroleum N-Alkanes and Polycyclic Aromatic Hydrocarbons by Polyextremophilic Pseudomonas Aeruginosa San Ai with Multidegradative Capacity. RSC Adv. 2020, 10 (24), 14060–14070. https://doi.org/10.1039/C9RA10371F

Supplementary material for: [https://doi.org/10.1039/c9ra10371f]Related to published version: [http://cherry.chem.bg.ac.rs/handle/123456789/3995

Supplementary data for the article: Izrael Živković, L. T.; Živković, L. S.; Beškoski, V. P.; Gopčević, K. R.; Jokić, B. M.; Radosavljević, D. S.; Karadžić, I. M. The Candida Rugosa Lipase Adsorbed onto Titania as Nano Biocatalyst with Improved Thermostability and Reuse Potential in Aqueous and Organic Media. Journal of Molecular Catalysis B: Enzymatic 2016, 133, S533–S542. https://doi.org/10.1016/j.molcatb.2017.06.001

Supplementary material for: [https://doi.org/10.1016/j.molcatb.2017.06.001]Related to published version: [http://cherry.chem.bg.ac.rs/handle/123456789/315]Related to accepted version: [http://cherry.chem.bg.ac.rs/handle/123456789/3648

Supplementary data for the article: Izrael-Živković, L.; Beškoski, V.; Rikalović, M.; Kazazić, S.; Shapiro, N.; Woyke, T.; Gojgić-Cvijović, G.; Vrvić, M. M.; Maksimović, N.; Karadžić, I. High-Quality Draft Genome Sequence of Pseudomonas Aeruginosa San Ai, an Environmental Isolate Resistant to Heavy Metals. Extremophiles 2019, 23 (4), 399–405. https://doi.org/10.1007/s00792-019-01092-w

Supplementary material for: [https://doi.org/10.1007/s00792-019-01092-w]Related to published version: [http://cherry.chem.bg.ac.rs/handle/123456789/3705

Supplementary material for the article: Izrael-Živković, L.; Rikalović, M.; Gojgić-Cvijović, G.; Kazazić, S.; Vrvić, M.; Brčeski, I.; Beškoski, V.; Lončarević, B.; Gopčević, K.; Karadžić, I. Cadmium Specific Proteomic Responses of a Highly Resistant: Pseudomonas Aeruginosa San Ai. RSC Advances 2018, 8 (19), 10549–10560. https://doi.org/10.1039/c8ra00371h

Supplementary material for: [https://doi.org/10.1039/c8ra00371h]Related to published version: [http://cherry.chem.bg.ac.rs/handle/123456789/2118

Supplementary material for the article: Izrael-Živković, L.; Rikalović, M.; Gojgić-Cvijović, G.; Kazazić, S.; Vrvić, M.; Brčeski, I.; Beškoski, V.; Lončarević, B.; Gopčević, K.; Karadžić, I. Cadmium Specific Proteomic Responses of a Highly Resistant: Pseudomonas Aeruginosa San Ai. RSC Advances 2018, 8 (19), 10549–10560. https://doi.org/10.1039/c8ra00371h

Supplementary material for: [https://doi.org/10.1039/c8ra00371h]Related to published version: [http://cherry.chem.bg.ac.rs/handle/123456789/2118

Cadmium specific proteomic responses of a highly resistant Pseudomonas aeruginosa san ai

Pseudomonas aeruginosa san ai is a promising candidate for bioremediation of cadmium pollution, as it resists a high concentration of up to 7.2 mM of cadmium. Leaving biomass of P. aeruginosa san ai exposed to cadmium has a large biosorption potential, implying its capacity to extract heavy metal from contaminated medium. In the present study, we investigated tolerance and accumulation of cadmium on protein level by shotgun proteomics approach based on liquid chromatography and tandem mass spectrometry coupled with bioinformatics to identify proteins. Size exclusion chromatography was used for protein prefractionation to preserve native forms of metalloproteins and protein complexes. Using this approach a total of 60 proteins were observed as up-regulated in cadmium-amended culture. Almost a third of the total numbers of up-regulated were metalloproteins. Particularly interesting are denitrification proteins which are over expressed but not active, suggesting their protective role in conditions of heavy metal exposure. P. aeruginosa san ai developed a complex mechanism to adapt to cadmium, based on: extracellular biosorption, bioaccumulation, the formation of biofilm, controlled siderophore production, enhanced respiration and modified protein profile. An increased abundance of proteins involved in: cell energy metabolism, including denitrification proteins; amino acid metabolism; cell motility and posttranslational modifications, primarily based on thiol-disulfide exchange, were observed. Enhanced oxygen consumption of biomass in cadmium-amended culture versus control was found. Our results signify that P. aeruginosa san ai is naturally well equipped to overcome and survive high doses of cadmium and, as such, has a great potential for application in bioremediation of cadmium polluted sites.Supplementary material: [http://cherry.chem.bg.ac.rs/handle/123456789/3179

The Candida rugosa lipase adsorbed onto titania as nano biocatalyst with improved thermostability and reuse potential in aqueous and organic media

The immobilization of Candida rugosa lipase by adsorption was performed onto commercial titania powder (Degussa P25). The change of titania particles surface was diagnosed by means of FTIR and FESEM analysis, as well as by shift of zeta potential value towards that of lipase. A detailed study of the effect of immobilization on enzyme kinetic, temperature stability, as well as on potential for its reuse in aqueous organic media was undertaken. Immobilization of lipase altered enzyme affinity toward substrates with different length of carbon chain in hydrolytic reaction. The Vmax value decreased 2–8-fold, where major constraint was registered for the ester containing the longest carbon chain. Thermostability of lipase improved more than 7-fold at 60 °C. Significant potential for reuse in water solutions was also found after immobilization. In cyclohexane immobilized lipase catalyzed synthesis of amyl octanoate by ping-pong bi–bi mechanism with inhibition by amyl alcohol. Obtained kinetic constants were Vmax = 26.4 μmol min−1, KAc = 0.52 mol/L, KAl = 0.2 mol/L and Ki,Al = 0.644 mol/L. Esterification activity remained 60% after 5 reuse cycles in cyclohexane indicating moderate reuse stability. © 2017 Elsevier B.V.This is peer-reviewed version of the following article: Izrael Živković, L. T.; Živković, L. S.; Beškoski, V. P.; Gopčević, K. R.; Jokić, B. M.; Radosavljević, D. S.; Karadžić, I. M. The Candida Rugosa Lipase Adsorbed onto Titania as Nano Biocatalyst with Improved Thermostability and Reuse Potential in Aqueous and Organic Media. Journal of Molecular Catalysis B: Enzymatic 2016, 133, S533–S542. [https://doi.org/10.1016/j.molcatb.2017.06.001]Supplementary material: [http://cherry.chem.bg.ac.rs/handle/123456789/3649