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© 2020 Wiley Periodicals LLC Today's Biochemical Engineer may contribute to advances in a wide range of technical areas. The recent Biochemical and Molecular Engineering XXI conference focused on “The Next Generation of Biochemical and Molecular Engineering: The role of emerging technologies in tomorrow's products and processes”. On the basis of topical discussions at this conference, this perspective synthesizes one vision on where investment in research areas is needed for biotechnology to continue contributing to some of the world's grand challenges.

Summary Bispecific antibodies (Bispecifics) demonstrate exceptional clinical potential to address some of the most complex diseases. However, Bispecific production in a single cell often requires the correct pairing of multiple polypeptide chains for desired assembly. This is a considerable hurdle that hinders the development of many immunoglobulin G (IgG)-like bispecific formats. Our approach focuses on the rational engineering of charged residues to facilitate the chain pairing of distinct heavy chains (HC). Here, we deploy structure-guided protein design to engineer charge pair mutations (CPMs) placed in the CH3-CH3′ interface of the fragment crystallizable (Fc) region of an antibody (Ab) to correctly steer heavy chain pairing. When used in combination with our stable effector functionless 2 (SEFL2.2) technology, we observed high pairing efficiency without significant losses in expression yields. Furthermore, we investigate the relationship between CPMs and the sequence diversity in the parental antibodies, proposing a rational strategy to deploy these engineering technologies., Graphical abstract, Highlights • Crystal structures unveil molecular basis of SEFL2.2 and CPM technologies • Next gen structure-guided design of CPMs to steer HC-HC pairing • Top CPMs show high pairing efficiency and optimal expression and stability • Balancing CPM charge distribution minimizes impact of sequence diversity, Biochemistry; Bioengineering; Biomolecular engineering; Structural biology

Protein interactions communicate critical information from the environment into cells to orchestrate functional responses relevant to health and disease. Whereas the natural repertoire of protein interfaces is finite, biomolecular engineering tools provide access to an unlimited scope of potential interactions that can be custom-designed for affinity, specificity, mechanism, or other properties of interest. This review highlights recent developments in protein interface engineering that offer insight into human physiology to inform the design of new pharmaceuticals, with a particular focus on immunotherapeutics. We cover three innovative and translationally promising approaches: (1) reprogramming receptor oligomerization to manipulate signaling pathways; (2) computational protein interface design strategies; and (3) engineering bioorthogonal protein interaction networks.

One of the central themes of biomolecular engineering is the challenge of exploiting the properties of biological materials. Part of this challenge has been uncovering and harnessing properties of biological components that only emerge following their ordered self-assembly. One biomolecular building block that has received significant interest in the past decade is the M13 bacteriophage. There have been a number of recent attempts to trigger the ordered assembly of M13 bacteriophage into multivirion structures, relying on the innate tendency of M13 to form liquid crystals at high concentrations. These, in general, yield planar two-dimensional materials. Presented here is the production of multivirion assemblies of M13 bacteriophage via the chemical modification of its surface by the covalent attachment of the xanthene-based dye tetramethylrhodamine (TMR) isothiocyanate (TRITC). We show that TMR induces the formation of three-dimensional aster-like assemblies of M13 by providing "adhesive" action between bacteriophage particles through the formation of H-aggregates (face-to-face stacking of dye molecules). We also show that the H-aggregation of TMR is greatly enhanced by covalent attachment to M13 and is enhanced further still upon the ordered self-assembly of M13, leading to the suggestion that M13 could be used to promote the self-assembly of dyes that form J-aggregates, a desirable arrangement of fluorescent dye, which has interesting optical properties and potential applications in the fields of medicine and light harvesting technology.

The alkyne functionality has attracted much interest due to its diverse chemical and biological applications. We recently elucidated an acyl carrier protein (ACP)-dependent alkyne biosynthetic pathway, however, little is known about ACP interactions with the alkyne biosynthetic enzymes, an acyl-ACP ligase (JamA) and a membrane-bound bi-functional desaturase/acetylenase (JamB). Here, we showed that JamB has a more stringent interaction with ACP than JamA. In addition, site directed mutagenesis of a non-cognate ACP significantly improved its compatibility with JamB, suggesting a possible electrostatic interaction at the ACP-JamB interface. Finally, error-prone PCR and screening of a second non-cognate ACP identified hot spots on the ACP that are important for interacting with JamB and yielded mutants which were better recognized by JamB. Our data thus not only provide insights into the ACP interactions in alkyne biosynthesis, but it also potentially aids in future combinatorial biosynthesis of alkyne-tagged metabolites for chemical and biological applications.Topical HeadingBiomolecular Engineering, Bioengineering, Biochemicals, Biofuels, and Food

Molecular hydrogen is a promising currency in the future energy economy due to the uncertain availability of finite fossil fuel resources and environmental effects from their combustion. It also has important uses in the production of fertilizers and platform chemicals as well as in upgrading conventional fuels. Conventional methods for producing molecular hydrogen from natural gas produce carbon dioxide and use a finite resource as feedstock. However, these issues can be overcome by using light energy from the Sun combined with microorganisms and their molecular machinery capable of photosynthesis. In the presence of light, the proteins involved in photosynthesis coupled with appropriate catalysts in higher plants, algae, and cyanobacteria can produce molecular hydrogen, and optimization via genetic modifications and biomolecular engineering further improves production rates. In this review, we will discuss techniques that have been utilized to improve rates of hydrogen production in biological systems based on the protein machinery of photosynthesis coupled with appropriate catalysts. We will also suggest areas for improvement and future directions for work in the field.

A central question in protein evolution is the extent to which naturally occurring proteins sample the space of folded structures accessible to the polypeptide chain. Repeat proteins composed of multiple tandem copies of a modular structure unit are widespread in nature and have critical roles in molecular recognition, signalling, and other essential biological processes. Naturally occurring repeat proteins have been re-engineered for molecular recognition and modular scaffolding applications. Here we use computational protein design to investigate the space of folded structures that can be generated by tandem repeating a simple helix-loop-helix-loop structural motif. Eighty-three designs with sequences unrelated to known repeat proteins were experimentally characterized. Of these, 53 are monomeric and stable at 95 °C, and 43 have solution X-ray scattering spectra consistent with the design models. Crystal structures of 15 designs spanning a broad range of curvatures are in close agreement with the design models with root mean square deviations ranging from 0.7 to 2.5 Å. Our results show that existing repeat proteins occupy only a small fraction of the possible repeat protein sequence and structure space and that it is possible to design novel repeat proteins with precisely specified geometries, opening up a wide array of new possibilities for biomolecular engineering.

Virus-like particles (VLPs) are repetitive organizations of viral proteins assembled in an appropriate physicochemical environment. VLPs can stimulate both innate and adaptive immune responses, due to their particulate structure enabling uptake by antigen presenting cells. These characteristics have led to successful development of VLP-vaccine products, and will ensure their vast potential in years to come. Future success of VLP therapeutic products will be determined by advances in their bioengineering, and also by the development of tools to design for their stability, function and application. This review focuses on approaches for VLP assembly in controlled chemical environments in vivo and in vitro, and the application of computational tools for improved chemical sequence design, and fundamental understanding of assembly.

Novel methods of molecular modeling help solving urgent problems in drug design, directed evolution of biocatalysts and biosensors, and a lot of other research fields. Implementation of such methods to organophosphorus hydrolase being perfect research object that hydrolyzes dangerous neurotoxic organophosphates could intensify development of antidote and protective preparations to treat poisoning. Structures of enzyme-polyelectrolyte complexes (EPCs) based on hexahistidine-tagged organophosphorus hydrolase (His6-OPH) with different biopolymers (various modifications of polyglutamic and polyaspartic acid, as well as hydroxyethyl starch and succinylated gelatin) were simulated at different pH using molecular docking. A number of EPCs with expected “positive” effect on maintaining the maximum level of His6-OPH activity, and some “negative” options were produced, and their catalytic performance was studied. The theoretical results were experimentally confirmed for four of the six “positive” options. EPCs obtained possessed up to 20–40% higher catalytic efficiency in hydrolysis reactions of Paraoxon and Parathion-methyl as compared with that of the native His6-OPH. The results obtained may be a good proof of concept for implementation of molecular docking to calculate model complexes of proteins with (bio)polymers of 6.4–105.5 kg/mol. Also, the approach used here could be interesting as alternative or addition to the directed modifications of enzymes to alter their catalytic characteristics.

Fungi are a prolific source of bioactive compounds, some of which have been developed as essential medicines and life-enhancing drugs. Genome sequencing has revealed that fungi have the potential to produce considerably more natural products (NPs) than are typically observed in the laboratory. Recently, there have been significant advances in the identification, understanding, and engineering of fungal biosynthetic gene clusters (BGCs). This review briefly describes examples of the engineering of fungal NP biosynthesis at the global, pathway, and enzyme level using in vivo and in vitro approaches and refers to the range and scale of heterologous expression systems available, developments in combinatorial biosynthesis, progress in understanding how fungal BGCs are regulated, and the applications of these novel biosynthetic enzymes as biocatalysts.

Si-Shen Feng Author for correspondence: Department of Chemical & Biomolecular Engineering, Department of Bioengineering, & Nanoscience & Nanotechnology Initiative (NUSNNI/NanoCore), National University of Singapore, Block E3, 05–29, 2 Engineering Drive 3, 117576, Singapore Tel.: +65 6576 3835 Fax: +65 6779 1936 chefess@nus.edu.sg Star-shaped block polymers as a molecular biomaterial for nanomedicine development

Nanomedicine is an emerging field that integrates nanotechnology, biomolecular engineering, life sciences and medicine; it is expected to produce major breakthroughs in medical diagnostics and therapeutics. Nano-scale structures and devices are compatible in size with proteins and nucleic acids in living cells. Therefore, the design, characterization and application of nano-scale probes, carriers and machines may provide unprecedented opportunities for achieving a better control of biological processes, and drastic improvements in disease detection, therapy, and prevention. Recent advances in nanomedicine include the development of nanoparticle-based probes for molecular imaging, nano-carriers for drug/gene delivery, multi-functional nanoparticles for theranostics, and molecular machines for biological and medical studies. This article provides an overview of the nanomedicine field, with an emphasis on nanoparticles for imaging and therapy, as well as engineered nucleases for genome editing. The challenges in translating nanomedicine approaches to clinical applications are discussed.

Spider silk is an extraordinary material with physical properties comparable to the best scaffolding/structural materials, and as a fiber it can be manipulated with ease into a variety of configurations. Our work here demonstrates that natural spider silk fibers can also be used to organize biological components on and in devices through rapid and simple means. Micron scale spider silk fibers (5-10 μm in diameter) were surface modified with a variety of biological entities engineered with pentaglutamine tags via microbial transglutaminase (mTG). Enzymes, enzyme pathways, antibodies, and fluorescent proteins were all assembled onto spider silk fibers using this biomolecular engineering/biofabrication process. Additionally, arrangement of biofunctionalized fiber should in of itself generate a secondary level of biomolecular organization. Toward this end, as proofs of principle, spatially defined arrangement of biofunctionalized spider silk fiber was shown to generate effects specific to silk position in two cases. In one instance, arrangement perpendicular to a flow produced selective head and neck carcinoma cell capture on silk with antibodies complexed to conjugated protein G. In a second scenario, asymmetric bacterial chemotaxis arose from asymmetric conjugation of enzymes to arranged silk. Overall, the biofabrication processes used here were rapid, required no complex chemistries, were biologically benign, and also the resulting engineered silk microfibers were flexible, readily manipulated and functionally active. Deployed here in microfluidic environments, biofunctional spider silk fiber provides a means to convey complex biological functions over a range of scales, further extending its potential as a biomaterial in biotechnological settings. Biotechnol. Bioeng. 2017;114: 83-95. © 2016 Wiley Periodicals, Inc.

With recent advances in biomolecular engineering, the bioremediation of persistent organic pollutants (POPs) using genetically modified microorganisms has become a rapidly growing area of research for environmental protection. Two main biomolecular approaches, rational design and directed evolution, have been developed to engineer enhanced microorganisms and enzymes for the biodegradation of POPs. This review describes the most recent developments and applications of these biomolecular tools for enhancing the capability of microorganisms to bioremediate three major classes of POPs – polycyclic aromatic hydrocabons (PAHs), polychlorinated biphenyls (PCBs) and pesticides. Most of the examples focused on the redesign of various features of the enzymes involved in the bioremediation of POPs, including the enzyme expression level, enzymatic activity and substrate specificity. Overall, the rapidly expanding potential of biomolecular engineering techniques has created the exciting potential of remediating some of the most recalcitrant and hazardous compounds in the environment.

The advances in high throughput screening technology for discovery of target molecules and the accumulation of functional genomics and proteomics data at an ever-accelerating rate will enable us to design and discover novel biomolecules and proteins on a rational basis in diverse areas of pharmaceutical, agricultural, industrial, and environmental applications. The biomolecular engineering will no doubt become one of the most important scientific disciplines in that it will enable us to comprehensively analyze gene expression patterns in both normal and diseased cells and to discover many new biologically active molecules rationally and systematically. As an applied molecular evolution technology, DNA shuffling will play a key role in biomolecular engineering. In contrast to the point mutation techniques, DNA shuffling exchanges large functional domains of sequences to search for the best candidate molecule, thus mimicking and accelerating the process of sexual recombination in the evolution of life. The phage-display system of combinatorial peptide libraries will be extensively exploited to design and create many more novel proteins, due to the relative ease of screening and identifying desirable proteins. Its application will be extended further into the science of protein–receptor or protein–ligand interactions. The bioinformatics including EST-based or SAGE-tag-based functional genomics and proteomics will continue to advance rapidly. Its biological knowledge base will expand the scope of biomolecular engineering, and the impact of well-coordinated biomolecular engineering research will be very significant on our understanding of gene expression, upregulation and downregulation, and posttranslational protein processing in healthy and diseased cells. The bioinformatics for genome and proteome analysis will contribute substantially toward ever more accelerated advances in pharmaceutical industry. When the functional genomics database, EST and SAGE techniques, microarray technique, and proteome analysis by 2-dimensional gel electrophoresis or capillary electrophoresis are all put to good use, the biomolecular engineering research will yield new drug discoveries, improved therapies, and new or significantly improved bioprocesses. With the advances in biomolecular engineering, the rate of finding new high-value peptides or proteins including antibodies, vaccines, enzymes, and therapeutic peptides will continue to be accelerated. The targets for rational design of biomolecules will be very broad, diverse, and complex, but many application goals can be achieved through the expansion of knowledge base on biomolecules of interest and their roles and functions in cells and tissues. In the near future, more therapeutic drugs and high-value biomolecules will be designed and produced for the treatment or prevention of not-so-easily-cured diseases such as cancers, genetic diseases, age-related diseases, and other metabolic diseases. Also anticipated are many more industrial enzymes that will be engineered to confer desirable properties for the process improvement and manufacturing of many high-value biomolecular products. Many more new metabolites including novel antibiotics that are active against resistant strains will be also produced by recombinant organisms having de novo engineered biosynthetic pathway enzyme systems. The biomolecular engineering era is here and a great deal of benefits can be derived from this field of scientific research for many years to come if we are willing to put it to good use.

Biomolecular engineering is a technology to create novel structures of high-value biomolecules for use in medicine and industry, through the directed alteration of proteins and/or biologically active molecules in living cells to produce a novel biometabolites as well as engineered protein itself. For the development of new drugs by biomolecular engineering, desired biomolecules have to be rationally designed based on their structure-stability/structure-activity relationship, and then screened through well-established mutation and selection program. Over the past decade, there has been significant progress in mutation and selection methodology; DNA shuffling technology mimicking natural evolution for artificial DNA recombination and phage-displayed combinatorial peptide library for rapid selection of proteins expressed from mutated genes. Bioinformatic tools including functional genomics and proteomics have been also developed for the ready access to the information related to the protein-function and genome-protein, leading to the design and identification of new drug targets. Throughout the use of an enormous amount of bioinformatic databases, many protein/peptide drugs and biometabolite molecules have been designed. The candidates of new drugs are monoclonal antibodies, vaccines, enzymes, antibiotics, therapeutic peptides, and so on. Two humanized monoclonal antibodies approved by FDA became the first line of drugs designed by biomolecular engineering approach. They are Herceptin and Synagis, for the treatment of breast cancer and pediatric respiratory syncytial viral infection, respectively. Many more newly engineered biomolecules are under developing for medicinal application. Some clinical trials for therapeutic applications are now in progress, and very positive results are already anticipated.

Huimin Zhao is a professor of Chemical and Biomolecular Engineering at the University of Illinois at Urbana-Champaign and the holder of Centennial Chair. His research interests encompass many different aspects of synthetic biology and chemical biology. They include directed evolution and rational design of proteins and pathways, novel approaches for protein, pathway, and genome engineering, the molecular genetics and enzymology of natural product biosynthesis, the fundamental aspects of biocatalysis, and the use of protein engineering and metabolic engineering methods in designing platform organisms including E. coli and S. cerevisiae for the synthesis of important chemicals, antibiotics, and biofuels from renewable feedstocks.

Department of Chemical & Biomolecular Engineering, National University of Singapore, 4 Engineering Drive 4, Singapore 117576, Singapore and Division of Bioengineering, National University of Singapore, 7 Engineering Drive 1, Singapore 117576, Singapore and Nanoscience & Nanotechnology Initiative, National University of Singapore, 2 Engineering Drive 3, Singapore 117587, Singapore Targeted nanomedicine for detection and treatment of circulating tumor cells

Virus-like particles (VLPs) are of interest in vaccination, gene therapy and drug delivery, but their potential has yet to be fully realized. This is because existing laboratory processes, when scaled, do not easily give a compositionally and architecturally consistent product. Research suggests that new process routes might ultimately be based on chemical processing by self-assembly, involving the precision manufacture of precursor capsomeres followed by in vitro VLP self-assembly and scale-up to required levels. A synergistic interaction of biomolecular design and bioprocess engineering (i.e. biomolecular engineering) is required if these alternative process routes and, thus, the promise of new VLP products, are to be realized.

This paper contributes selected examples based on the research and development of sub–micrometric and nanoscale structures at FEMTO–ST. In particular, exploitation of bandgap materials such as lithium niobate is a specialty of the institute and is applied in active photonic and phononic devices. Another area of active research concerns instrumentation at the microscale and nanoscale. More recently, biomolecular engineering and nanobiocharacterisation have been developed for nanobiotechnology and biosensors.

The last century witnessed spectacular advances in both microelectronics and biotechnology yet there was little synergy between the two. A challenge to their integration is that biological and electronic systems are constructed using divergent fabrication paradigms. Biology fabricates bottom-up with labile components, while microelectronic devices are fabricated top-down using methods that are 'bio-incompatible'. Biofabrication--the use of biological materials and mechanisms for construction--offers the opportunity to span these fabrication paradigms by providing convergent approaches for building the bio-device interface. Integral to biofabrication are stimuli-responsive materials (e.g. film-forming polysaccharides) that allow directed assembly under near physiological conditions in response to device-imposed signals. Biomolecular engineering, through recombinant technology, allows biological components to be endowed with information for assembly (e.g. encoded in a protein's amino acid sequence). Finally, self-assembly and enzymatic assembly provide the mechanisms for construction over a hierarchy of length scales. Here, we review recent advances in the use of biofabrication to build the bio-device interface. We anticipate that the biofabrication toolbox will expand over the next decade as more researchers enlist the unique construction capabilities of biology. Further, we look forward to observing the application of this toolbox to create devices that can better diagnose disease, detect pathogens and discover drugs. Finally, we expect that biofabrication will enable the effective interfacing of biology with electronics to create implantable devices for personalized and regenerative medicine.

On 9 and 10 October 1984 the European Communities' program in biomolecular engineering of crop plants and associated microorganisms met at the Carlsberg Laboratory in order to assess research progress, discuss future plans and coordinate efforts. Major trends and highlights apparent from the presentations are discussed here 1,2 .

This programme is essentially motivated by the need to allow the optimal exploitation by man of recent discoveries in modern biology and to stimulate in the Community v~e developments in applied fields where nations such as the U.S.A. and Japan have gained a considerable advance. Two main themes form ~he basis of the integrated research proposed for Community action. The first one deals with the development of the second generation of enzyme reactors, that is to say, with the exploitation of complex enzymatic reactions for the synthesis of elaborated products important to European industries. The second concerns the application of genetib engineering methods to organisms of importance for European agriculture and industry. Considerable attention is given here to the development of suitable host-vector systems and to the solution of the important practical problems which prevent the control of expression of foreign DNA.

Cell factories have been largely exploited for the controlled production of substances of interest for food, pharma and biotech industries. Although human-controlled microbial production and transformation are much older, the cell factory concept was fully established in the 80’s through the intensive public and private investment. Strongly empowered by the then nascent recombinant DNA technologies and supported by the approval of recombinant insulin [1,2], the principle of controlled biological production as a convenient source of difficult-to-obtain molecules (especially those of high added value) deeply penetrated the industrial tissue, soon becoming a widespread platform aiming at cost-effective large-scale production [3]. The first generation cell factories (mainly composed by plain strains of the bacterium Escherichia coli and the yeast Saccharomyces cerevisae) were soon replaced by engineered variants. Resulting from the application of untargeted mutagenesis and phenotypic selection, conventional genetic modification, metabolic engineering, and more recently by systems metabolic engineering that integrates metabolic engineering with systems biology and synthetic biology, new strains having much enhanced performance have been progressively developed [4-19]. In parallel, mammalian and insect cells for the production of high quality proteins, and other microbial species appealing from an industrial point of view due to their unusual physiological traits, have been incorporated to the cell factory family [20,21]. This comprises algae, fungi, psychrophilic bacteria and moss, among others [22-26]. On the other hand, a set of food-grade lactic acid bacteria are under development as emerging platforms in food microbiology but also as a novel source of metabolites and proteins [27-34]. The physiological diversity of the microbial world offers an intricacy of biosynthetic pathways from which novel bio-products, including nano- or micro-structured materials [35-37], offer promises in even more diverse applications. Still, many substances and materials of industrial interest are nowadays produced by chemical synthesis, and the number of (recombinant) proteins approved for therapeutic use hardly reaches 200, a figure much lower than that initially presumed. However, both environmental concerns and medical and industrial needs strongly push towards a fully sustainable bio-production of a larger spectrum of substances. Then, how much limited is the economic feasibility of microbial production? Have the cell factories reached a plateau in their development? Is there more room for further exploitation of the microbial production? Systems metabolic engineering [38,39] offers a set of methodological and strategic tools for the design and optimization of metabolic and gene regulatory networks for the efficient production of chemicals (from pharmaceuticals to bulk chemicals and fuels) and materials (from plastics to high value materials) [5-7,40]. Furthermore, creation of new metabolic pathways and fine tuning of the existing ones have become possible [8,15]. This is already allowing the production of substances so far reluctant to microbial production under industrial requirements and under cost-effective processes, allowing us to overcome limitations of microbial cell factories. In silico genome-scale metabolic modeling and simulation are playing increasingly important roles in system-wide identification of target genes and pathways to be manipulated to enhance production of desired products. Profiling of transcriptome, proteome, metabolome, and/or fluxome is also becoming a routine practice in metabolic engineering for the better understanding of cellular characteristics under given genetic and/or environmental perturbations. Through the system-wide optimized design and development of microbial cell factories, many industrially important chemicals and materials could be efficiently produced. Some example products include, but not limited to, alcohols other than ethanol including propanol, butanol and isobutanol, dicarboxylic acids such as succinic acid, fumaric acid, malic acid and adipic acid, diols such as 1,3-propanediol, 1,2-propanediol, 1,4-butanediol and 2,3-butanediol, diamines such as putrescine and cadaverine, and even polymers including polyhydroxyalkanoates, polylactic acid, spider silk protein, poly-gamma-glutamic acid, and many others [40]. It is expected that increasingly diverse chemicals and materials that are currently produced by petrochemical industry will be produced by employing microbial cell factories. Improving cell factories by systems biotechnology to an industrially relevant level cannot be successfully reached by individual teams alone. A wide range of expertise is needed for the full development of a novel biotechnological process, including microbiology, chemistry, bioinformatics, biochemical engineering, but also agricultural and plant sciences and economics. After a proof of concept has shown the feasibility of a novel approach for cell factory engineering, large consortia or networks of fully skilled teams should take over in collaboration with Biotech companies to accomplish an economically feasible bioprocess. As an early example, the development of bacteria producing 1,3-propanediol from glucose has been well documented, and required the engineering of more than 70 genes, before process development and scale up were reasonably made [41]. Replacing materials which are produced from mineral oil by biobased products requires not only efficient technology but also the assessment of economical and ecological feasibility, as intensely studied for polylactic acid [42]. As the progress of industrial biotechnology did not accomplish the desired speed of development [43] academic researchers have teamed up with industry in publicly funded research centers worldwide. To name a few, the Joint BioEnergy Institute (JBEI) in the San Francisco Bay Area, the Novo Nordisk Foundation Center for Biosustainability (CFB) at the Technical University of Denmark, the Metabolic and Biomolecular Engineering Laboratory (MBEL) of the Korea Advanced Institute of Science and Technology (KAIST), the Dutch Klyuver Centre for Genomics of Industrial Fermentation, or the Austrian Centre of Industrial Biotechnology (ACIB) share the mission to speed up development of industrial bioprocesses by joining forces of different academic disciplines with industrial collaborators.