A Vikulina has completed her PhD in the field of Biological Science in Lomonosov Moscow State University, Russia. Currently, she is Marie-Curie Fellow in Fraunhofer Institute for Cell Therapy and Immunology, Potsdam, Germany. Her research is focused on the development of drug delivery carriers for controlled drug delivery and testing as well as for deciphering the pathways of biological action and transport of drugs. She has been awarded by prestigeous Alexander Von Humboldt and Marie-Curie Fellowships, served as a member of organizing committees at international conferences and scientific olympiads. She is also a Guest Editor in Micromachines Journal.

Biopolymer based multilayer capsules are novel vectors for advanced drug delivery. Capsules assembled using decomposable and mesoporous CaCO3 vaterite crystals can host enormous amounts of biomolecules (such as proteins and peptides, small drugs, nucleic acids, etc1) and release them in a controlled manner. Protection and controlled release of biomolecules are the main advantages of the capsules; this can be achieved by adjusting the capsule structure by varying the number of layers, polymer nature and distribution into capsules. Loading of biomolecules into capsules at physiologically relevant and mild conditions is indispensable for bio-applications. This work aims to fabricate capsules from a variety of biopolymers and assess their stability and the encapsulation performance. The following biopolymers have been tested for polyanions (chondroitin sulfate, hyaluronic acid, dextran sulfate, and heparin) and polycations (poly-L-lysine, dextran amine, collagen, and protamine). The most attractive pairs of biopolymers, in-terms of capsule integrity are identified and retention of biomolecules within the capsules is considered. Shrinkage of capsules at room temperature during CaCO3 removal is used for capture of biomolecules into capsules and is discussed by taking into account the charge compensation in cooperative interpolymer complexation. Interestingly, occupation of the vaterite crystal pores with polymer during capsule fabrication is also responsible for the observed capsule shrinkage and fusion phenomena

Martin Schomber has completed his Master studies in pharmaceutical biotechnolgy at the age of 25 years from Technische Hochschule Mittelhessen. In his studies, he has been a part of different research work groups in molecular, enzymantical and industrial parts of biotechnology. During a research stay at the University of Auckland (New Zealand), he was involved in a methodical studie to identify beta-1,3 glucan in wood for specific identification of different kinds of wood for industrial application.

Bioethanol is produced in general by starch fermentation from corn or sugar beets. An alternative is the use of lignocellulose by digesting cellulose to glucose. This digestion is an enzymatic process in which endocellulases, cellobiohydrolses and β-glucosidase, named as cellulase complex, are interacting together. The most common used fungal strain for cellulase production, Trichoderma reseei, has been studied intensively and optimized in recent years. The metabolism of cellulase production has been described in different literatures for fungis but is not exactly understood so far. The problem of cellulase production by Trichoderma reseei is based on a not well balanced enzyme complex. There is a low production rate of beta-glucosidase in this fungi that leads to the addition of the minor enzyme in industrial scale fermentation. Our studies focuses on a cellulase production with Penicillium verruculosum mutants that has a more balanced cellulase complex. Beech wood is used as lignocellulose substrate in this study which is pretreated by organosolv process technology for separation of hemicellulose, lignin and cellulose. This poster will present first fermentation results by using different substrates and varying fermentation methods to optimize the enzyme production in both, lab and pilot scale.

Marion Champeaud graduated with a Bachelor of Biology five years ago, a Master’s degree in Agro-Industry three years ago from Bordeaux University in France and she is currently doing a PhD in partnership between a biotechnology company Fermentalg and Poitiers University in France (UMR CNRS 7267). Her research studies in engineering process and microalgae culture area resulted in 2 patents-pending and 2 publication in progress.

Utilization of whey or whey permeate is one of major concerns of the dairy industry nowadays, especially the acid whey, which mostly remains untreated prior to disposal. In 2010, 734 million tons of milk, and 160 - 180 million tons of whey per year were produced worldwide (Guimaraes et al., 2010). In 2014, milk production was higher than 800 million tons and is constantly increasing over the years. Despite the different strategies considered by the industrials to valorize whey: lactose crystallization, food applications in bakery products, dry mixes, snack, and milk replacer, alcoholic fermentation, or biogas conversion, only 50 % of this whey is processed (Mollea et al., 2013 ; Siso1996). In this study we present an industrial fermentation model to valorize these dairy by-products to obtain added-value bio-products at the same time. We demonstrate that the microalgae Galdieria sulphuraria is able to consume 100% lactose, 98% of lactate and 79 % of the citrate present in whey permeate. Specific transport experiments show that lactose uptake by Galdieria sulphuraria involves the induction of a specific low affinity transport system ( Km = 53 ± 2.9). The biomass production is whey permeate specific and range from 30 to more than 110 g/l of dry matter. In addition to direct the bio-remediation of industrial dairy waste, the algae biomass produced show a real nutritional interest due to its high protein content (> 50 %) and is naturally rich in essential amino acid.

Do Yeal Ryu is an integrated PhD student from Chung Ang University in Republic of South Korea. He has majored in reproduction. He has published 11 papers in reputed journals (3 papers as a first author).

Conventional semen analysis has limitations to predict male fertility in livestock industry. Although several studies have been performed to overcome the limitation, the current solution to prediction is still unsatisfactory. It is generally accepted that peroxiredoxin I (PRDX I) have a critical role in the regulation of male fertility. Therefore, the current study was designed to investigate the correlation between PRDX I and male fertility. PRDX I was examined on spermatozoa collected from 14 individual boars with different litter size (10.3-14.2). 530 saws were artificially inseminated to determine the littersize. Subsequently, several sperm function were evaluated. Our study showed that there is a significant positive correlation between littersize and PRDX I (r=0.686 and p = 0.007) as well as hyperactivity (r=0.5769 and p=0.031). Subsequently, the prediction accuracy of boar fertility was determined by the receiver operating characteristic (ROC) curves. The ROC analysis showed that PRDX I can predict litter size with overall accuracy 92.86% (sensitivity 90%, specificity 100%, negative predictive value 80%, and positive predictive value 100%). In addition, hyperactivity also showed 80% overall accuracy to predict litter size (sensitivity 70%, specificity 75%, negative predictive value 50%, and positive predictive value 87.5%). As a biomarker, PRDX I and hyperactivity are expected to increase pups than average litter size (0.54 and 0.45, respectively). As far we know no other authors have found the correlation between PRDX I and littersize. Consequently, PRDX I might be the novel candidate biomarker for diagnosing male fertility and littersize in livestock industry.

Katia dos Reis completed her Bachelor of Chemistry and Master of Biochemistry at the Federal University of Rio de Janeiro. She is a Professor of Chemistry in the State Department of Rio de Janeiro and did her PhD Graduate Program in Technology of Chemical and Biochemical Processes of the School of Chemistry at the Federal University of Rio de Janeiro. Currently, she has been a Patent Analyst at the Bio-Manguinhos Technological Transfer Office (TTO-BIO), advising researchers on the protection of products and processes from Bio-Manguinhos/Fiocruz Technological Development.

Over the past 10 years, there has been an increasing demand for biopharmaceuticals, especially monoclonal antibodies. The rate of these biological products was significantly higher than the rate of traditional pharmaceuticals. Biopharmaceuticals now account for more than 15% of the total market and there is a forecast that sales of biopharmaceuticals should exceed $250,000,000,000 by 2020. The growth in demand of these products can be justified by the high specificity of monoclonal antibodies and the need for researchers and the market to develop new products, new technologies that could be used to combat various diseases. Multidrug-resistant bacteria strains are a global problem and the use of monoclonal antibodies to combat hospital infections may be a valuable alternative to public health. Another important aspect is the patent protection of these new assets, especially in the Institute of Immunobiological Technology (Bio-Manguinhos), a unit of the Oswaldo Cruz Foundation (Fiocruz) responsible for research, innovation, technological development and production of vaccines, rapid test devices and biopharmaceuticals aimed at meeting the demands of national public health.

Iris Munhoz Costa is a PhD student in the graduate program in Pharmaceutical Technology-Biochemistry in the School of Pharmaceutical Sciences at University of São Paulo. She works with biopharmaceutical research for the treatment of acute lymphoblastic leukemia. She has obtained her Master’s degree in Pharmaceutical Technology-Biochemistry at University of São Paulo in 2015; Graduation in Pharmacy and Biochemistry at Universidade Paulista in 2012. She was a student of scientific initiation in the Department of Pharmaceutical Biochemical Technology in the Faculty of Pharmaceutical Sciences at the University of São Paulo in the area of molecular biology and antioxidant response in 2011.

Acute lymphoblastic leukemia (ALL) is the most frequent neoplasm in children and adolescents. Treatment of the disease is performed with L-asparaginase (ASNase), an enzyme obtained from the bacteria Escherichia coli and Erwinia chrysanthemi (Erwinase). ASNase hydrolyzes L-asparagine and prevents tumor cells from obtaining this amino acid from the bloodstream for protein synthesis, leading to ALL cell death by apoptosis. However, both formulations are associated with a high rate of adverse effects as the production of anti-asparaginase antibodies and hypersensitivity, which compromise the efficacy of the treatment. The development of mutant proteoforms from commercially available bacterial enzymes may contribute to the development of an enzyme with lower adverse effects. Therefore, we created a mutant library using the ASNase of E. chrysanthemi by error prone PCR, and a double mutant proteoform (DM) presented higher specific activity for L-asparagine and a 30% increase in the kcat in relation to the wild-type (WT) enzyme. In addition, DM enzyme showed less recognition by anti-asparaginase antibodies and is able to kill the same amount of ALL cell line MOLT-4 than WT enzyme, using a smaller amount of protein. The results indicated that the DM enzyme has cytotoxic potential and may have fewer adverse effects.

Tales A Costa-Silva has completed his Graduation in Biological Sciences at Federal University of Alfenas, Brazil and is pursuing his PhD at Sao Paulo University, Brazil. He has experience in Microbiology, focusing on Industrial Microbiology, acting on the following subjects: Industrial Enzymology (Production, Purification, Immobilization, Characterization and Application) and Pharmaceutical Biotechnology.

L-asparaginase (E.C.3.5.1.1) produced by bacteria is used in the treatment of acute lymphocytic leukemia (ALL). However, innumerable side effects were registered by the usage of bacterial L-ASNase during ALL treatment. Other drawbacks associated with prokaryotic L-asparaginase treatment are hypersensitivity reactions, low thermal stability, human proteases degradation and rapid clearance. Some techniques have been used to overcome these downsides such as bioprospecting eukaryotic sources or modification of commercial bacterial L-asparaginases by site-directed mutagenesis. In order to find eukaryotic sources of L-ASNase, 20 filamentous fungi were used in this study, which were isolated from the microbiome of the jellyfish Olindias sambaquiensis. Six fungi samples isolated from jellyfish tentacles (brown structures in jelly fish responsible to toxin production) showed L-asparaginase production by submerged fermentation process. The highest activity was shown by Strain OS02 with 2.7 U/g. This strain was selected for optimization of L-asparaginase production by central composite design of response surface methodology. For maximum enzyme production (11.45 U/g), the best condition was modified Czapek–Dox medium supplemented with L-asparagine and adjusted to pH 7.4 at 32.5 °C and 190 rpm. Regarding protein engineering of commercial bacterial L-asparaginases we used site-directed mutagenesis to obtain L-asparaginase protease-resistance: a new Escherichia coli L-asparaginase (EcAII) variant, triple mutant. The preliminary results showed that mutant enzyme was expressed in E. coli BL21 (DE3) and preserved original L-asparaginase activity. These L-asparaginases proteoforms may be alternative biopharmaceuticals with the potential of further improving outcome in ALL treatment.

Javeria Ejaz is emerging young scholar at the age of 24 , and currently, doing Ph.D in Plant Biotechnology at University of Poonch Faculty of Agriculture, Rawalakot (Azad Kashmir), and focusing on the fate of Biotechnology in the plant Breeding & Molecular genetics. She has participated in many national and international conferences and seminars, and give presentationabout her research work. She has good scientific publications as well.

Heavy metals are major environmental concern when they present in high concentration in soil. Heavy metals in agricultural land and products are of great attention throughout the world as they are toxic to both plants and human health. The present study aimed to elucidate the Photosynthetic performance, antioxidant enzymatic activities, anthocyanin contents, anthocyanin biosynthetic genes expression and vanadium uptake in two mustard genotypes purple and green differing in photosynthetic capacity under vanadium stress. The results indicated that vanadium significantly reduced photosynthetic activity and protein contents in both genotypes. The activities of antioxidant enzymes were increased significantly in responce to vanadium stress, however, the purple mustard genotypes had significantly higher antioxidant enzymatic activities. The anthocyanin contents were also significantly reduced under vanadium stress. The anthocyanin biosynthetic genes were highly expressed in the purple genotype, especially the genes TT8, F3H, and MYBL2 under vanadium. The expression of all biosynthesis genes were higher in vanadium-treated purple mustard genotype than green mustard, however with the increase in vanadium concentrations these expression level decreases consecutively. These results indicate that induction of TT8, F3H, and MYBL2 genes was associated with upregulation of biosynthetic genes for higher anthocyanin biosynthesis in purple mustard as compare to green mustard. The vanadium uptake by the roots was always higher than the shoots in the both mustard genotypes. The results showed that the purple had higher vanadium tolerance than the green genotype. Future work should be directed to unveil the mechanistic explainations of genes expression and inter-relatioship of vanadium and plants that are currently being unraveled.