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Vilnius, Lithuania

Javmen A.,State Scientific Research Institute Center for Innovative Medicine | Mauricas M.,State Scientific Research Institute Center for Innovative Medicine | Nemeikaite-Ceniene A.,State Scientific Research Institute Center for Innovative Medicine | Grigiskis S.,JSC Biocentras
International Workshop on Artificial Immune Systems, AIS 2015/ICSI3 2015 - Systems Immunology, Immunoinformatics and Immune-computation: Immunology without Borders, Proceedings | Year: 2014

Nowadays non-cellulosic, β-glucans from the different source are intensively investigated due to the fact that these biological polymers are recognized as potent immunological stimulators for the mammal's immune system. Dendritic cells are the most important antigen presenting cells for activating naive T cells. The research goals of the recent investigation were to determine how the different molecular weight Saccharomyces cerevisiae β- glucan preparations affect such properties of the murine DC as phagocytosis, proliferation and cytokine synthesis in vitro. © 2015 IEEE. Source


Siekstele R.,Vilnius University | Veteikyte A.,Vilnius University | Tvaska B.,JSC Biocentras | Matijosyte I.,Vilnius University
Journal of Industrial Microbiology and Biotechnology | Year: 2015

Many microbial lipases have been successfully expressed in yeasts, but not in industrially attractive Kluyveromyces lactis, which among other benefits can be cultivated on a medium supplemented with whey––cheap and easily available industrial waste. A new bacterial lipase from Serratia sp. was isolated and for the first time expressed into the yeast Kluyveromyces lactis by heterologous protein expression system based on a strong promoter of Kluyveromyces marxianus triosephosphate isomerase gene and signal peptide of Kluyveromyces marxianus endopolygalacturonase gene. In addition, the bacterial lipase gene was synthesized de novo by taking into account a codon usage bias optimal for K. lactis and was expressed into the yeast K. lactis also. Both resulting strains were characterized by high output level of the target protein secreted extracellularly. Secreted lipases were characterized for activity and stability. © 2015, Society for Industrial Microbiology and Biotechnology. Source


Kleinaite E.,Vilnius University | Jaska V.,JSC Biocentras | Tvaska B.,JSC Biocentras | Matijosyte I.,Vilnius University
Journal of Cleaner Production | Year: 2014

By this study we aimed to develop a green and cleaner alternative to the existing oil-derived lubricant production by providing the market biolubricant synthesis catalyzed by enzymes. Moreover, the use of biodiesel to develop a higher added-value product is a very attractive solution for biodiesel production manufacturers in extending their production supply and the potential sales markets, especially in the East Europe region. The synthesis of 2-ethyl-1-hexyl oleate (biolubricant) was studied using commercially available immobilized lipase Lipozyme TL IM, biodiesel as a source of fatty acids and relatively cheap 2-ethyl-1-hexanol. The transesterification reaction was performed in solvent-free and water-free system. 2-Ethyl-1-hexyl oleate was successfully synthesized in 50 L scale with 100 % conversion in 10 h of reaction time at 60 °C temperature. The physico-chemical properties of 2-ethyl-1-hexyl oleate were estimated. © 2014 Elsevier Ltd. All rights reserved. Source


Javmen A.,JSC Biocentras | Javmen A.,State Scientific Research Institute Center for Innovative Medicine | Grigiskis S.,JSC Biocentras | Rudenkov M.,Vilnius Gediminas Technical University | Mauricas M.,State Scientific Research Institute Center for Innovative Medicine
Protein Journal | Year: 2013

A β-1,3-endoglucanase produced by Streptomyces rutgersensis was purified to a homogeneity by the fractional precipitation with ammonium sulfate, ion exchange chromatography on Q-Sepharose and hydrophobic chromatography on Butyl Sepharose. A typical procedure provided 11.74-fold purification with 12.53 % yield. SDS-PAGE of the purified protein showed one protein band. The exact molecular mass of the enzyme obtained by mass spectrometry was 41.25 kDa; the isoelectric point was between pH 4.2-4.4. The optimal β-glucanase catalytic activity was at pH 7 and 50 C. An enzyme was only active toward glucose polymers containing β-1,3 linkages and hydrolyzed Saccharomyces cerevisiae cell wall β-glucan in an endo-like way: reaction products were different molecular size β-glucans, which were larger than glucose. © 2013 Springer Science+Business Media New York. Source


Matikeviciene V.,JSC Biocentras | Grigiskis S.,JSC Biocentras | Levisauskas D.,Kaunas University of Technology | Sirvydyte K.,JSC Biocentras | And 3 more authors.
Vide. Tehnologija. Resursi - Environment, Technology, Resources | Year: 2011

The aim of this study was to identify and optimize significant technological parameters influencing keratinolytic enzyme production by A. fradiae 119 and to study its ability to degrade keratin. In the present work chicken feathers meal (CFM) was found to be an excellent substrate for keratinase induction by A. fradiae 119. The strain produced 164 KU/mL keratinolytic activity in basal medium containing 7.5 g/L CFM as the sole source of carbon and nitrogen. Increased keratinolytic activity was achieved in media with ammonium sulfate as nitrogen source, the application of additional nitrogen sources to media containing CFM slightly decreased keratinase synthesis. Optimal parameters of the cultivation process were determined: pH of cultivation medium - 7.2, temperature - 34 °C and inoculum's size - 8%, using the response surface methodology. The yield of keratinase activity was increased by 46% (267 KU/mL) after optimization of the cultivation process. The good ability of cultural liquid to degrade feathers and wool was detected. Source

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