Enzymicals AG

Greifswald, Germany

Enzymicals AG

Greifswald, Germany
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Grant
Agency: European Commission | Branch: FP7 | Program: CP-TP | Phase: KBBE.2011.3.6-01 | Award Amount: 2.98M | Year: 2011

Two academic groups and eight SMEs who all work on different aspects of protein engineering will collaborate and produce a website that will consist of a portal with an embedded workbench to provide users a self-service system for in silico protein engineering. This interactive self-service portal will give users access to a wide variety of protein engineering facilities and information systems, and will allow them to interactively work with a comprehensive set of well-documented, well-integrated computational protein engineering tools. The databases that will be provided will be curated, and the software and protocols will be validated by performing a variety of protein engineering experiments on a series of enzyme classes. The portal and the interactive workbench will be freely available, and they will be solidly based in modern information technology. The usability for protein engineering will be thoroughly experimentally validated.


Grant
Agency: European Commission | Branch: H2020 | Program: IA | Phase: BIOTEC-3-2014 | Award Amount: 9.25M | Year: 2015

C-C bond forming reactions are at the heart of industrial organic synthesis, but remain largely unexplored due to long development timelines and the lack of broad biocatalytic reaction platforms. CARBAZYMES addresses these challenges by assembling an interdisciplinary and intersectoral consortium as a powerful synergistic tool to promote innovation in the field of biocatalytic C-C bond formation at large scale, and thus the global competitiveness of the European chemical and pharmaceutical industry. The proposed consortium, with 50% industrial participation, represents academia but also commercial interests in different stages of the research-to-market process. This top-down approach, together with a life-cycle innovation approach ensures an industrial drive to the project. Clearly aligned with the scope of topic BIOTEC3-2014, CARBAZYMES will pursue the biocatalytic synthesis (spanning TRLs 5-7) of 4 APIs and 3 bulk chemicals corresponding to market needs detected by the industrial partners in the Consortium. This will be accomplished through an inter-disciplinary approach which includes: i) a broad platform of 4 types of unique C-C bond-forming enzymes, mostly lyases; ii) the capacity to rapidly evolve enzymes to operate under industrial conditions by means of novel enzyme panels and massive screening methods; iii) application of microreactor technology for bioprocess characterization; iv) demonstration actions comprising technical (up to 100L) and economic viability studies carried out by industrial partners. CARBAZYMES unmistakably aims to have social and economic impact by addressing markets worth bn , developing enzyme evolution technologies beyond the state of the art and creating qualified jobs and technical-scale facilities at the industrial partners sites. CARBAZYMES will also achieve an environmental impact by enforcing that the developed processes replace more energy and resource intensive processes, thus leading to reduced environmental footprints.


Sehl T.,Jülich Research Center | Hailes H.C.,University College London | Ward J.M.,University College London | Wardenga R.,Enzymicals AG | And 5 more authors.
Angewandte Chemie - International Edition | Year: 2013

Two steps in one pot: An enzyme cascade consisting of a lyase and an (R)- or (S)-selective ω-transaminase (TA) provides (1R,2R)-norpseudoephedrine and (1R,2S)-norephedrine in only two steps. The intermediate is not isolated in this one-pot reaction and the products are obtained in high enantio- and diastereomeric purity. Moreover, the by-product from the second reaction can be recycled to serve as the substrate for the first reaction. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.


Sehl T.,Jülich Research Center | Hailes H.C.,University College London | Ward J.M.,University College London | Menyes U.,Enzymicals AG | And 2 more authors.
Green Chemistry | Year: 2014

Chiral 1,2-amino alcohols are important building blocks for chemistry and pharmacy. Here, we developed two different biocatalytic 2-step cascades for the synthesis of all four nor(pseudo)ephedrine (N(P)E) stereoisomers. In the first one, the combination of an (R)-selective thiamine diphosphate (ThDP)-dependent carboligase with an (S)- or (R)-selective ω-transaminase resulted in the formation of (1R,2S)-NE or (1R,2R)-NPE in excellent optical purities (ee >99% and de >98%). For the synthesis of (1R,2R)-NPE, space-time yields up to ∼26 g L-1 d-1 have been achieved. Since a highly (S)-selective carboligase is currently not available for this reaction, another strategy was followed to complement the nor(pseudo)ephedrine platform. Here, the combination of an (S)-selective transaminase with an (S)-selective alcohol dehydrogenase yielded (1S,2S)-NPE with an ee >98% and a de >99%. Although lyophilized whole cells are cheap to prepare and were shown to be appropriate for use as biocatalysts, higher optical purities were observed with purified enzymes. These synthetic enzyme cascade reactions render the N(P)E-products accessible from inexpensive, achiral starting materials in only two reaction steps and without the isolation of the reaction intermediates. This journal is © the Partner Organisations 2014.


Grant
Agency: European Commission | Branch: H2020 | Program: RIA | Phase: ISIB-05-2014 | Award Amount: 10.81M | Year: 2015

The COSMOS proposal aims to reduce Europes dependence on imported coconut and palm kernel oils and fatty acids and castor oil as sources for medium-chain fatty acids (MCFA, C10C14) and medium-chain polymer building blocks. These are needed by the oleochemical industry for the production of plastics, surfactants, detergents, lubricants, plasticisers and other products. In COSMOS, camelina and crambe will be turned into profitable, sustainable, multipurpose, non-GMO European oil crops for the production of oleochemicals. Seed properties will be screened and optimised through genetic techniques aiming at high yield, low resource inputs, optimization of the value generated from vegetative tissues and fatty acid profiles adapted to industrial needs. Large-scale field trials will be performed at different locations in Europe to assess the potential of the crops in terms of cultivation practices, seed yield, oil content, ease of harvesting, and resource inputs. Extracted oils will be fractionated into various fatty acid types (monounsaturated versus polyunsaturated) by selective enzyme technologies and extraction processes. The monounsaturated long-chain fatty acids so obtained will be converted to MCFA and high-value building blocks for bio-plastics and flavour and fragrance ingredients through chemical and enzymatic chain cleavage processes. The 3-rich PUFA fraction will be purified for use in food and feed ingredients. Vegetative tissues such as straw, leaves and press cake will be fed to insects producing high-value proteins, chitin and fats. Insect fats and proteins will be isolated and prepared for use in food and feed products. The overall economic, social and environmental sustainability as well as life cycle of the whole value chain will be assessed. The impact of the project for Europe will be assessed in terms of value chain potentials for value creation and number of jobs that can be created.


Grant
Agency: European Commission | Branch: H2020 | Program: MSCA-ITN-EID | Phase: MSCA-ITN-2014-EID | Award Amount: 2.79M | Year: 2015

In BIOCASCADES, nine early-stage researchers (ESRs) will investigate the development of sustainable (chemo)enzymatic cascade reactions under the green chemistry philosophy. The proposed BIOCASCADES project combines different techniques such as compartmentalization, protein engineering and reaction engineering in order to develop commercially viable and environmentally benign one pot reactions. By avoiding intermediate downstream- and purification-steps, cascade reactions minimize production costs, energy demand and waste production and are thus expected to make a major contribution for the development of sustainable and efficient production processes. Small- and medium sized enterprises (SMEs) are emerging as main drivers of European Research. They are dynamic, explore new areas and create new ideas, while large companies rely more and more on outsourcing research or involving SMEs by joint ventures. However, small companies are not strong enough as stand-alone enterprises, which requires them to form networks with other SMEs and academia. This creates a strong demand for young researchers who can move freely in an international and interdisciplinary environment. In a tailor-made training program BIOCASCADES aims to provide the nine early stage researchers with specific scientific and transferable skills for careers in the highly dynamic European biotechnology sector. Training at leading laboratories of biocatalysis will develop their scientific skills, while secondments to the industry and specific workshops will develop their entrepreneurship. The graduates of this doctorate program will be highly qualified for collaborative research between European academia and industry. The consortium is formed by leading academic laboratories from biocatalysis and protein engineering together with a network of four innovative biotech companies. By combining their versatile expertise, the consortium can achieve a success that would not be possible in isolated projects.


Staudt S.,Friedrich - Alexander - University, Erlangen - Nuremberg | Bornscheuer U.T.,Institute of Biochemistry | Menyes U.,Enzymicals AG | Hummel W.,Heinrich Heine University Düsseldorf | And 2 more authors.
Enzyme and Microbial Technology | Year: 2013

The development of a biocatalytic process concept for ε-caprolactone, which directly converts cyclohexanol as an easily available industrial raw material into the desired ε-caprolactone in a one-pot fashion while only requiring air as sole reagent, is reported. The desired product ε-caprolactone was obtained with 94-97% conversion when operating at a substrate concentration in the range of 20-60. mM. At higher substrate concentrations, however, a significant drop of conversion was found. Subsequent detailed studies on the impact of the starting material, intermediate and product components revealed a significant inhibition and partial deactivation of the BVMO by the product ε-caprolactone (in particular at higher concentrations) as well as an inhibition of the BVMO by cyclohexanol and cyclohexanone. © 2013 Elsevier Inc.


Mallin H.,University of Greifswald | Menyes U.,Enzymicals AG | Vorhaben T.,Neoplas GmbH | Hohne M.,University of Greifswald | Bornscheuer U.T.,University of Greifswald
ChemCatChem | Year: 2013

Two (R)-selective amine transaminases from Gibberella zeae (GibZea) and from Neosartorya fischeri (NeoFis) were immobilized on chitosan as a carrier to improve their application in the biocatalytic synthesis of chiral (R)-amines. An (S)-selective enzyme from Vibrio fluvialis (VfTA) was used for comparison. After improving the immobilization conditions, all enzymes could be efficiently immobilized. Additionally, the thermal stability of GibZea and NeoFis could be improved and also a slight shift of the pH optimum was observed for GibZea. All enzymes showed good activity in the conversion of α-methylbenzylamine. In the asymmetric synthesis of (R)-2-aminohexane from the corresponding ketone, a 13.4-fold higher conversion (>99%) was found for the immobilized GibZea compared to the free enzyme. Hence, the covalent binding with glutaraldehyde of these enzymes on chitosan beads resulted in a significant stabilization of the amine transaminases investigated. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.


The invention is related to a method for the identification of enzymes having potential halohydrin dehalogenase activity from sequences disclosed in a biomolecule database based on the use of characteristic amino acid sequence motifs. Additionally, the invention is related to the use of the identified halohydrin dehalogenases in the conversion of halohydrins into epoxides as well as to the use of the identified halohydrin dehalogenases in the conversion of epoxides into alcohols.


Patent
Enzymicals AG | Date: 2015-07-29

The present invention is related to a method for producing polyesters, wherein a lactone is converted to a polyester by a lipase, characterized- in that the lipase is Lipase A from Candida antarctica (CAL-A) according to SEQ ID NO 1 or a homologue enzyme having sequence identity of at least 25% with SEQ ID NO 1 and having the same function as CAL-A and- in that the conversion is done in an essentially aqueous medium.

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