15^th World Congress on Biotechnology and Biotech Industries Meet March 20-21, 2017 Rome, Italy

Biography:

Lukasz Opalinski has completed his MS in Biotechnology from the University of Wroclaw, Poland. In 2012, he obtained his PhD from the University of Groningen, Netherlands. His PhD work was focused on peroxisome proliferation and involvement of peroxisomes in antibiotics production by filamentous fungi. In 2012, he obtained EMBO Long Term Fellowship to study molecular mechanisms of mitochondria biogenesis at the University of Freiburg, Germany. Since 2015, he is working as a Faculty of Biotechnology in the University of Wroclaw, Poland, where he is working on the endocytosis of antibody fragments generated against FGFR1.

Abstract:

Fibroblast growth factors (FGFs) and their plasma membrane-localized receptors (FGFRs) regulate signaling pathways that govern developmental processes and metabolism. Numerous tumors are characterized by the overproduction of FGFR and this is considered a bad prognostic factor for patient survival. Antibody drug conjugates (ADCs) targeting cancer cells with the elevated level of FGFR represent one of the most attractive therapeutic strategies. ADCs are composed of the antibodies raised against tumor-specific biomarkers linked to the highly cytotoxic drugs. After selective binding to the cancer cells ADCs are internalized and delivered to the lysosomes by intracellular vesicular transport system. The lysosomal proteolysis of ADCs results in the release of the cytotoxic drugs, leading to the cell death. A prerequisite for an ADC approach is efficient internalization of the antibody-target complex. Although the biology of FGFRs and their ligands has been broadly studied, the requirements for the effective internalization of antibodies that target FGFR remain elusive. We analyzed the internalization of antibody fragments in various formats that target FGFR1. The antibody fragments in the monovalent scFv format bind to FGFR1, but are not internalized into the model cells that overproduce FGFR1. In contrast, the same scFv proteins in the bivalent scFv-Fc format are efficiently internalized via FGFR1-mediated clathrin and dynamin dependent endocytosis. Interestingly, the receptor kinase function of FGFR1 is dispensable for endocytosis of scFv-Fc-FGFR1 complexes. Binding of the bivalent scFv-Fc induces FGFR1 dimerization without simultaneous receptor activation, suggesting that oligomerization of FGFR1 triggers receptor endocytosis.

Biography:

Madalin Enache - principal investigator into field of halophilic microorganisms at the Institute of Biology Bucharest of the Romanian Academy (IBB). Graduated of University of Bucharest in biochemistry field. In the present acting also as Head of Microbiology Department of the IBB - coordinating research and administrative activity of the Departament of Microbiology (IBB); Research activities in fields of microbiology, biochemistry, biology, ecology. Coordinating laboratory work, dissemination of the scientific results (scientific papers, participation to conferences and symposia – oral and posters presentations), application for research project, scientific reports, project coordinating. Used with various techniques of general microbiology, microscopy, biochemistry, molecular biology. Research topics: diversity and phylogeny of halophilic microorganisms; ecology of extremely halophilic archaea, enzymology of halophilic microorganisms; nanobiotechnology

Abstract:

The mural painting can be bio-deteriorated by micro-organisms in different ways depending on the taxonomic affiliation of micro-organisms, their biology and succession while on a surface. The rate of bio-deterioration is dependent on microclimate conditions, the chemical structure of deposits, the interrelation between bio-deteriogenes and some chemical processes. During colonization of the mural painting surface, some species of micro-organisms synthesize pigments which could be released into the substrate or remain localized within cells but the mural painting surface appears colored. The bio-pigmentation change esthetical appearance of the mural painting or mortar where micro bio-deteriogenes develop. In our case studies (the refectory of Hurezi Monastery and the pre-nave of Humor Monastery), the pink bio-pigmentation is the result of mural painting colonization by halophilic bacteria, namely new strain of Garicola genus and some strains of Halobacillus spp. They have the ability to grow in media with negligible salt concentration until saturation (extremely halophilic archaea). Taking into account the complexity of salt composition in mural paintings, it appears that these could be a favorable environment from several moderately halophilic micro-organisms. On the other hand, the investigated halophilic micro-organisms showed various growth answers when their culture medium was supplemented with TiO₂ nanoparticles. Such kinds of nanomaterials are currently investigated for their potential use in re-saturation procedures of bio-deteriorated historical monuments. 

Biography:

Mija Sezun has completed her PhD in Biological and Biotechnological Sciences. Her Doctoral thesis included Environmental Biotechnology area. Currently, she is working at Pulp and Paper Institute and mainly deals with biotechnology in the paper industry through the use of enzymes in the process of paper production. Currently, her research focuses on “The production of enzymes by using fungi by applying paper mill sludge, as the substrate for the cultivation of fungi”. In addition to the fungal enzyme production, she also deals with the use of commercial enzymes to improve the efficiency of processes in the paper industry.

Abstract:

At Pulp and Paper Institute, enzymatic applications for the main processes in pulp and paper industry i.e. deinking, fibrillation, bleaching and papermaking was investigated in the last years. In our study, we were focusing on improvement of fibrillation and deinking process. During the fibrillation process, objective was to reduce energy consumption while in the deinking process we tried to replace environmentally unfriendly chemicals with enzymes. The deinking is a process for the removal of contaminants from reusable paper fibers. Basically, deinking is carried out in two major phases: The disintegration of printed paper and the separation of ink particles and contaminants from the fibrous suspension by washing or flotation. The enzymatic/neutral deinking is an alternative to counteract the intensive use of chemicals in the conventional process, a process that reduces the environmental impact, efficient and fast, and with which similar results to what has been achieved in deinking using chemical substances are obtained. Paper production is extremely energy-intensive process as 18 to 25% of all the energy needed for the cellulose fibrillation. Cellulose fibrillation is one of the most important processes in the papermaking. This has a major impact on the mechanical properties and, consequently, the mechanical properties of the paper products. The effect of enzymatic treatment (cellulase) on the degree of refining and on the basic, mechanical and optical properties of produced laboratory sheets (thickness, grammage, density, breaking length, tear index, stretch, tensile index, burst index and ISO brightness) was investigated. Enzymatic treatment performed before the refining reduced the refining time for 10%, while treatment after the refining has proven to be ineffective. Enzyme had a positive effect on virtually all measured properties of laboratory sheets made of short eucalyptus`s fibers and slightly inferior effect on sheets produced from long fibers of coniferous. According to results of deinking process efficiency, we can conclude that enzymatic treatment had a positive effect on ISO brightness of all treated samples. Highest ISO brightness was determined after using a mix of enzymes (cellulase, laccase and lipase). Enzymatic treatment had a slightly inferior effect on tensile index of all samples and even the other measured properties were batter with using enzymes.

Biography:

Ewa Å»ymanczyk-Duda has done his MSc in Biotechnology (1990), PhD in Chemistry (1995) Wroclaw University of Science and Technology, Poland. She has also worked as an Assistant Professor (2008) at the Wroclaw University of Science and Technology, Poland. She was the Vice Dean of Chemistry Department, Coordinator of Teaching Program in the area of Biotechnology. She has published more than 40 papers in reputed journals and has been serving as a reviewer   for various journals.

Abstract:

Chirality is a crucial feature in the world of living organisms. This is responsible for the specific interactions between biologically active compounds in nature; therefore, it is also fundamental for designing the novel compounds. Among P-C compounds, structures are phosphonate derivatives such as amino phosphonates, keto phosphonates, hydroxy phosphonates. These are analogues of physiological compounds, so they are applied as moderators of activity of particular enzymes involved in natural compounds metabolic pathways. For such purposes, it is necessary to receive them as defined optical isomers. Chemical synthesis of such phosphonates is of low-effectiveness, also for the economic reasons, so biocatalytical approach appeared to be a good alternative. Good results were achieved for the kinetic resolutions of the racemic mixtures of amino- and hydroxy-phosphonates. This was performed via selective oxidation and employing following fungal genera: Penicillium, Beauveria, Cunninghamella, Verticillium, Cladosporium, Rhodotorula and Saccharomyces (as whole-cells biocatalysts). The same fungal mycelia were able to selectively reduce (thermodynamic process) prochiral keto phosphonates. The above mentioned experiments succeeded based on the laboratory scale and the most effective ones were selected for scaling- up process. This was the hardest part, because it required the modifications of the biotransformation procedures and the biocatalyst form. Experiments were performed with the use of batch and continuous reactors, and the fungal mycelia were immobilized with the use of polyurethane foams.

Biography:

Oliver Spadiut has completed his PhD in Biotechnology from BOKU University, Austria. He has done his Post-doctoral studies from KTH Royal Institute of Technology, Stockholm, Sweden. Since 2010, he has been working as an Assistant Professor in Biochemical Engineering at TU Wien, Vienna, Austria. Currently, he is the Principal Investigator of Integrated Bioprocess Development research group. He has published more than 60 papers in reputed journals and has been serving as a reviewer for many journals.         
 

Abstract:

Strong induction of recombinant protein production in E. coli can lead to agglomeration of inactive product, inclusion bodies (IBs), and also imposes a high metabolic burden which can result in cell death. We developed a feeding strategy using glucose as primary carbon source, lactose as secondary carbon source and inducer to tune recombinant protein expression which leads to higher yields of soluble and active product. We successfully applied this system for the production of several biopharmaceuticals. This new feeding approach allows expression of complex products as soluble and active protein that usually results in insoluble and inactive inclusion bodies. Cell viability and growth can be prolonged by this approach which leads to higher overall yields and thus lower production costs. Thus, our strategy might make E. coli a more attractive host for the production of biopharmaceuticals in the future. The audience will get to know a platform technology for the enhanced expression of biopharmaceuticals in E. coli to accelerate bioprocess development and yield higher product titers.

Biography:

Abstract:

F-box motif containing proteins are shown as the component of protein degradation machinery where they function as substrate recruiting factor. Through substrate recruitment and subsequent degradation of recruited substrate by ubiquitin mediated proteasome machinery they regulate variety of cellular functions such as signal transduction and cell cycle transition. The S. cerevisiae cells upon nutrient stress enter into the quiescence stage; at molecular level, this transition is mediated through the recruitment of adenosine deaminase factor Aah1p by the F box motif containing protein Saf1p which constitute the SCF E3 ligase. Here, we have investigated the regulation of the SAF1 gene by various transcription factors during stress. For this we have analyzed the gene expression profiling database (GEO), transcriptional regulation databases and yeast stress expression database. The gene expression profiling database indicated that SAF1 gene expression is up regulated during hypoxia and the drug treatment. The subsequent analysis of transcription factors regulating the SAF1 gene expression revealed RLM1 as novel transcription factor regulating the SAF1 and its substrate AAH1 gene expression during stress condition. The yeast stress expression database analysis revealed that in variety of stress conditions (drug, pH, temperature, microbial toxin and inorganic compound) the RLM1 and SAF1 were constitutively over expressed at log2 FC>1 and adjusted p-value <0.05 setting in comparison to control cells. The RLM1 gene has been implicated in the cell wall integrity checkpoint pathway. It has also been reported that RlmA deficient strains lacks cell wall organization and cell growth in A. fumigatus. Based on the analysis we hypothesized that double knockout of SAF1 and RLM1 genes cells may be resistant to stress condition which need to be tested experimentally. 

Biography:

Tuba Sevgi has completed her MSc from Technical University of Kaiserslautern in Molecular Biotechnology and Systems Biology, Germany. Currently, she is doing her PhD in the Department of Biology, Faculty of Arts and Sciences, Uludag University. She is a Research Assistant in the Department of Biology, Faculty of Arts and Sciences, Uludag University.

Abstract:

In this study, a novel bacterial strain with high protease activity (210 U/ml) was isolated from soil, and then identified by its morphological character and 16S rRNA sequence, and named Bacillus subtilis 168 E6-5. Bacillus protease enzyme and commercial protease enzyme were applied to 100% raw wool fabric and bleached wool fabric. After dyeing with acid dyes, changes in the size of the fabric and color yields were measured. Protease was purified by dialysis+lyophilization, and applied on dyed wool fabric and felting shrinkage values were measured. Enzyme treated and dyed wool fabric possess 8%, however non-treated wool fabric has 11% of felting shrinkage value just after dyeing step. After performing five repeated washing, the enzyme treated raw fabric has 12% and the non-treated raw fabric has 15%. After pre-washing, bleaching and dyeing steps, the felting shrinkage value of the enzyme treated wool fabric was 9%, while non-treated one was 11%. After the processes of pre-treatment, bleaching and dying the K/S value indicating the colour yield of the fabric was measued. The K/S value of the wool fabric that was treated with enzyme before the processes of pretreatment, bleaching and dying was 31.68, while the non-enzyme-treated wool fabric has 26.33. Enzyme application increased the colour yield. This study suggests that the Bacillus protease enzyme shows better results in behaviours of felting and dying than the commercial protease enzyme and applicable on wool fabrics. Therefore, this protease enzyme has potential in textile industry.