ARTES Biotechnology GmbH

Langenfeld, Germany

ARTES Biotechnology GmbH

Langenfeld, Germany
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Grant
Agency: European Commission | Branch: FP7 | Program: CP-IP | Phase: KBBE-2007-3-2-07 | Award Amount: 8.23M | Year: 2009

The PolyModE project convenes an international, interdisciplinary, and intersectorial consortium to identify, characterise, and optimise novel polysaccharide modifying enzymes, and to develop robust fermentation strategies for their large-scale production, to exploit the potential of biopolymers for food, pharmaceutical, cosmetic, and technical applications. We have selected the six complex carbohydrates with the highest current market share or expected future market potential, namely alginate, carrageenan, chitosan, glycosaminoglycan, pectin, and xanthan gum. For each of these, the industrial partners have identified those enzymes which will answer to the most pressing needs or offer the most promising potential for improved production of polysaccharides with novel physico-chemical properties and biological functionalities. Primary targets will be alginate epimerases, carrageenan sulfatases, chitosan de-acetylases, glycosaminoglycan sulfatases, pectin de-acetylases, and xanthan gum de-acetylases. These enzymes together with secondary target enzymes, e.g. sequence specific lyases and hydrolases, will allow the generation and analysis of polymers and oligomers with novel, non-random patterns of modification. Two parallel approaches will be followed for each type of polysaccharide modifying enzyme, namely a knowledge-based genomic approach and a broad, un-biased metagenomic approach, e.g. using soil or sludge samples with a history of contact with the polysaccharide in question. A pipeline of three levels of fermentation systems will be established, ranging from lab-scale innovative expression systems with features shaped according to the specific characteristics of our target enzymes, through medium-scale, novel and unusual fermentation systems provided by a number of SME with highly specialised knowledge and expertise in developing and using such systems, to the established large-scale fermentation systems and facilities of market leaders in White Biotechnology.


Grant
Agency: European Commission | Branch: FP7 | Program: CP-TP | Phase: KBBE.2013.3.6-01 | Award Amount: 11.70M | Year: 2013

The Nano3Bio project convenes a consortium of world renowned experts from 8 EU universities, 1 large company, and 14 SME, to develop biotechnological production systems for nanoformulated chitosans. Chitosans, chitin-derived polysaccharides varying in their degree of polymerisation (DP), degree of acetylation (DA), and pattern of acetylation (PA), are among the most versatile and most promising biopolymers, with excellent physico-chemical and material properties, and a wide range of biological functionalities, but their economic potential is far from being exploited due to i) problems with reproducibility of biological activities as todays chitosans are rather poorly defined mixtures, and ii) the threat of allergen contamination from their typical animal origin. The Nano3Bio project will overcome these hurdles to market entry and penetration by producing in vitro and in vivo defined oligo- and polymers with controlled, tailor-made DP, DA, and PA. Genes for chitin synthases, chitin deacetylases, and transglycosylating chitinases/chitosanases will be mined from different (meta)genomic sources and heterologously expressed, the recombinant enzymes characterized and optimized by protein engineering through rational design and molecular evolution, e.g. targeting engineered glycosynthases. These enzymes and genes will be used for in vitro and in vivo biosynthesis in microbial and microalgal systems, focusing on bacteria and diatoms. The bioinspired chitosans will be formulated into biomineralised hydrogels, nanoparticles, nanoscaffolds, etc., to impart novel properties, including by surface nano-imprinting, and will be bench-marked against their conventional counterparts in a variety of cell based assays and routine industrial tests for e.g. cosmetics and pharma markets. The process will be accompanied by comprehensive life cycle assessments including thorough legal landscaping, and by dissemination activities targeted to the scientific community and the general public.


Grant
Agency: European Commission | Branch: FP7 | Program: BSG-SME | Phase: SME-2013-1 | Award Amount: 1.72M | Year: 2013

The aim of TA101GOCLIN Project is to take TA101 into the clinical stage of development for rheumatoid arthritis and prepare the product for a novel mode of administration in the market of biologic therapeutics. Rheumatoid Arthritis is still today a debilitating disease with an unmet medical need for effective and reasonably priced treatments despite much effort to cure or control the disease. TA101 is a small domain antibody that is being developed for the treatment of rheumatoid arthritis and has passed through preclinical efficacy studies with much success. TA101 will now undergo an upscaling process of production to enter clinical trials. TA101GOCLIN project is within the scope of the clinical development of TA101 and is aimed at providing safety data in humans through a clinical trial of Phase Ia and Ib. Concomitantly, TA101GOCLIN will develop a novel mode of administration for TA101 to be used after project end. This will provide a major competitive advantage for the product already during development stages. The innovative administration will use microneedle patches, a new method that allows the autonomous administration of the drug through the skin without the pain of conventional injections. To achieve the above mentioned objectives, TA101GOCLIN gathered three competitive SMEs from Portugal, Belgium and The Netherlands. TechnoPhage, Q-Biologicals and MyLife Technologies, respectively, will be responsible for developing the clinical data of Phase I for TA101, develop an upscale method for production of the drug, and develop the microneedle device for administration of TA101. Overall, TA101GOCLIN holds the promise that an innovative product for the treatment of Rheumatoid Arthritis will enter the clinical phases of development with the confidence that the technologies that are at its base will create a new solution for the patients, with the major benefits of efficacy, safety, convenience and affordability.


Eilert E.,ARTES Biotechnology GmbH | Eilert E.,Heinrich Heine University Düsseldorf | Kranz A.,ARTES Biotechnology GmbH | Hollenberg C.P.,ARTES Biotechnology GmbH | And 3 more authors.
Journal of Biotechnology | Year: 2013

Ectoine and 5-hydroxyectoine belong to the family of compatible solutes which are known to mainly contribute to the adaptation of the cell to osmotic stress by mediation of a constant turgor. In addition the cell's essential functions are maintained under stress conditions like high salinity, heat or aridity stress. Hansenula polymorpha was engineered to catalyze the transformation of monomeric substrates to 5-hydroxyectoine. For this purpose four genes encoding the enzymes of the 5-hydroxyectoine biosynthesis pathway of Halomonas elongata, EctA, EctB, EctC, and EctD, were inserted into the genome of H. polymorpha. Subsequently the syntheses of ectoine and 5-hydroxyectoine were analyzed and optimized. We showed that H. polymorpha is a suitable system for recombinant 5-hydroxyectoine synthesis in gram per liter scale (2.8gL-1 culture supernatant, 365μmol/g dcw) in which almost 100% conversion of ectoine to 5-hydroxyectoine without necessity of high salinity were achieved. © 2013 Elsevier B.V..


Eilert E.,ARTES Biotechnology GmbH | Hollenberg C.P.,Heinrich Heine University Düsseldorf | Piontek M.,ARTES Biotechnology GmbH | Suckow M.,ARTES Biotechnology GmbH
Journal of Biotechnology | Year: 2012

The iron storage protein ferritin is a member of the non-heme iron protein family. It can store and release iron, therefore it prevents the cell from damage caused by iron-dioxygen reactions as well as it provides iron for biological processing. To study whether the human ferritin heavy chain (FTH1) can be expressed in Hansenula polymorpha, we integrated an expression cassette for FTH1 and analyzed the protein expression. We found very efficient expression of FTH1 and obtained yields up to 1.9. g/L under non-optimized conditions. Based on this result we designed a FTH1-PTH fusion protein to successfully express the parathyroid hormone fragment 1-34 (PTH) for the first time intracellular in H. polymorpha. © 2012 Elsevier B.V.


Boer E.,Leibniz Institute of Plant Genetics and Crop Plant Research | Breuer F.S.,Leibniz Institute of Plant Genetics and Crop Plant Research | Weniger M.,ARTES Biotechnology GmbH | Denter S.,ARTES Biotechnology GmbH | And 2 more authors.
Applied Microbiology and Biotechnology | Year: 2011

Tannase (tannin acyl hydrolase, EC 3.1.1.20) hydrolyses the ester and depside bonds of gallotannins and gallic acid esters and is an important industrial enzyme. In the present study, transgenic Arxula adeninivorans strains were optimised for tannase production. Various plasmids carrying one or two expression modules for constitutive expression of tannase were constructed. Transformant strains that overexpress the ATAN1 gene from the strong A. adeninivorans TEF1 promoter produce levels of up to 1,642 UL -1 when grown in glucose medium in shake flasks. The effect of fed-batch fermentation on tannase productivity was then investigated in detail. Under these conditions, a transgenic strain containing one ATAN1 expression module produced 51,900 U of tannase activity per litre after 142 h of fermentation at a dry cell weight of 162 gL -1. The highest yield obtained from a transgenic strain with two ATAN1 expression modules was 31,300 U after 232 h at a dry cell weight of 104 gL -1. Interestingly, the maximum achieved yield coefficients [Y(P/X)] for the two strains were essentially identical. © Springer-Verlag 2011.


Giersberg M.,Leibniz Institute of Plant Genetics and Crop Plant Research | Degelmann A.,ARTES Biotechnology GmbH | Bode R.,University of Greifswald | Piontek M.,ARTES Biotechnology GmbH | Kunze G.,Leibniz Institute of Plant Genetics and Crop Plant Research
Journal of Industrial Microbiology and Biotechnology | Year: 2012

The Xplor 2 transformation/expression platform was employed for comparative assessment of three different yeast species as hosts for synthesis of a thermostable nicotinamide adenine dinucleotide (NAD?)- dependent medium-chain alcohol dehydrogenase from Rhodococcus ruber strain 219. Using yeast ribosomal DNA (rDNA) integrative expression cassettes (YRCs) and yeast integrative expression cassettes (YICs) equipped with a selection-marker module and one, two or four expression modules for transformation of auxotrophic Arxula adeninivorans, Hansenula polymorpha, and Saccharomyces cerevisiae strains, quantitative comparison of the yield of recombinant alcohol dehydrogenase RR-ADH6Hp in all three species was carried out. In all cases, the RR-ADH6H gene was expressed under the control of the strong constitutive A. adeninivorans-derived TEF1 promoter, which functions in all yeast species analyzed. Recombinant RRADH6Hp accumulated intracellularly in all strains tested. The best yields of active enzyme were obtained from A. adeninivorans, with S. cerevisiae producing intermediate amounts. Although H. polymorpha was the least efficient producer overall, the product obtained was most similar to the enzyme synthesized by R. ruber 219 with respect to its thermostability. © Society for Industrial Microbiology and Biotechnology 2012.


A method for producing ectoine or a derivative thereof comprises the steps of (a) preparing host cells from a type of yeast, the host cells containing at least one recombinant DNA sequence encoding each of one or more heterologous enzymes for biosynthesis of ectoine, (b) causing the host cells, with the aid of the recombinant DNA sequences encoding the enzymes, to express the heterologous enzymes, and (c) causing the host cells, with the aid of the expressed heterologous enzymes, to synthesize ectoine and/or the derivative thereof from a precursor. A yeast cell of the orders Saccharomycetales or Schizosaccharomycetales for use as a host cell in such a method contains at least one recombinant DNA sequence encoding each of one or more heterologous enzymes for biosynthesis of ectoine.


Schuttmann I.,Justus Liebig University | Bouws H.,Justus Liebig University | Szweda R.T.,Justus Liebig University | Suckow M.,ARTES Biotechnology GmbH | And 2 more authors.
Journal of Molecular Catalysis B: Enzymatic | Year: 2014

A β-carotene degrading versatile peroxidase (VP) was successfully induced in submerged cultures of the white-rot basidiomycete Pleurotus sapidus by use of residues of a biogas plant as a carbon and nitrogen source. After three chromatographic steps, the VP was isolated with an overall yield of 12% and a purification factor of 130. The purified enzyme showed a molecular mass of 38 kDa and an isoelectric point of 3.6. Highest affinity to β-carotene (Km = 50 ± 5 μM) was observed at 30 °C and pH 4.5. The purified VP was capable of degrading suspended lignin organosolv particles. N-terminal and internal peptide sequences were obtained from Edman degradation and mass spectrometric peptide sequencing. The VP encoding cDNA was identified by colony hybridization and amplified by PCR. Bioinformatic analyses revealed an open reading frame of 1083 bp and similarities of 90% to VPs from P. eryngii. The recombinant VP was produced successfully with an activity of 450 ± 20 mU mg-1 in cultures of H. polymorpha. © 2013 Elsevier B.V.


Kaur P.,University of Delhi | Singh B.,University of Delhi | Boer E.,Leibniz Institute of Plant Genetics and Crop Plant Research | Straube N.,Leibniz Institute of Plant Genetics and Crop Plant Research | And 3 more authors.
Journal of Biotechnology | Year: 2010

The Pichia anomala gene PPHY, which codes for a cell-bound phytase, was isolated from genomic DNA by PCR, using oligonucleotide sequences derived from the N-terminal region of the purified phytase protein (Pphyp) and a degenerate primer derived from conserved sequences of yeast and fungal phytases as primers. The gene harbours an ORF of 1389bp, encoding a 462-amino-acid protein. The deduced amino acid sequence has similarity, to a varied extent, with those of phosphatases from Pichia stipitis (62%), Candida dubliniensis (51%), Candida albicans (51%), Arxula adeninivorans (35%) and phytases from Debaryomyces castellii (50%) and Pichia fabianii (39%). The sequence contains the phytase consensus heptapeptide motif (-Arg-His-Gly-X-Arg-X-Pro-) as well as two phosphohistidine signature motifs found in histidine acid phosphatases. After transformation of PPHY into the yeasts Saccharomyces cerevisiae, A. adeninivorans and Hansenula polymorpha, the last species was selected as the most suitable for synthesis of recombinant Pphyp. The cell-bound enzyme activities produced by wild-type P. anomala and transgenic H. polymorpha strains bearing the PPHY gene placed under the control of the inducible H. polymorpha-derived FMD promoter were characterized. In both cases, a molecular mass of approximately 380kDa was determined for the native enzyme (corresponding to a hexamer); the pH and temperature optima for the activity were 4.0 and 60°C, respectively. The enzyme was active on phytic acid, p-nitrophenylphosphate, glucose-6-phosphate, ADP, sodium pyrophosphate, AMP, 1-naphthylphosphate and ATP. Based on the Km/Kcat and further biochemical parameters, the enzyme was classified as a cell-bound phytase with acid phosphatase activity and not as acid phosphatase, despite its strong similarity to the latter class of enzymes. The yeast biomass containing phytase has been demonstrated to be useful as a feed additive in poultry and aquaculture, and dephytinization of foods and feeds. © 2010 Elsevier B.V.

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