Biocatalysis
Biotechnology
Enzymes, Immobilized
Chemical Engineering
Enzymes
Catalysis
Biodegradation, Environmental
Hexanes
Solvents
Biotransformation
Stereoisomerism
Protein Engineering
Databases, Factual
Escherichia coli
Substrate Specificity
A modular treatment of molecular traffic through the active site of cholinesterase. (1/2123)
We present a model for the molecular traffic of ligands, substrates, and products through the active site of cholinesterases (ChEs). First, we describe a common treatment of the diffusion to a buried active site of cationic and neutral species. We then explain the specificity of ChEs for cationic ligands and substrates by introducing two additional components to this common treatment. The first module is a surface trap for cationic species at the entrance to the active-site gorge that operates through local, short-range electrostatic interactions and is independent of ionic strength. The second module is an ionic-strength-dependent steering mechanism generated by long-range electrostatic interactions arising from the overall distribution of charges in ChEs. Our calculations show that diffusion of charged ligands relative to neutral isosteric analogs is enhanced approximately 10-fold by the surface trap, while electrostatic steering contributes only a 1.5- to 2-fold rate enhancement at physiological salt concentration. We model clearance of cationic products from the active-site gorge as analogous to the escape of a particle from a one-dimensional well in the presence of a linear electrostatic potential. We evaluate the potential inside the gorge and provide evidence that while contributing to the steering of cationic species toward the active site, it does not appreciably retard their clearance. This optimal fine-tuning of global and local electrostatic interactions endows ChEs with maximum catalytic efficiency and specificity for a positively charged substrate, while at the same time not hindering clearance of the positively charged products. (+info)Quantum catalysis in enzymes: beyond the transition state theory paradigm. A Discussion Meeting held at the Royal Society on 14 and 15 November 2005. (2/2123)
How do enzymes work? What is the physical basis of the phenomenal rate enhancements achieved by enzymes? Do we have a theoretical framework that accounts for observed catalytic rates? These are the foremost questions-with particular emphasis on tunnelling phenomena-debated at this Discussion Meeting by the leading practitioners in the field. (+info)Genome-wide studies of histone demethylation catalysed by the fission yeast homologues of mammalian LSD1. (3/2123)
In order to gain a more global view of the activity of histone demethylases, we report here genome-wide studies of the fission yeast SWIRM and polyamine oxidase (PAO) domain homologues of mammalian LSD1. Consistent with previous work we find that the two S. pombe proteins, which we name Swm1 and Swm2 (after SWIRM1 and SWIRM2), associate together in a complex. However, we find that this complex specifically demethylates lysine 9 in histone H3 (H3K9) and both up- and down-regulates expression of different groups of genes. Using chromatin-immunoprecipitation, to isolate fragments of chromatin containing either H3K4me2 or H3K9me2, and DNA microarray analysis (ChIP-chip), we have studied genome-wide changes in patterns of histone methylation, and their correlation with gene expression, upon deletion of the swm1(+) gene. Using hyper-geometric probability comparisons we uncover genetic links between lysine-specific demethylases, the histone deacetylase Clr6, and the chromatin remodeller Hrp1. The data presented here demonstrate that in fission yeast the SWIRM/PAO domain proteins Swm1 and Swm2 are associated in complexes that can remove methyl groups from lysine 9 methylated histone H3. In vitro, we show that bacterially expressed Swm1 also possesses lysine 9 demethylase activity. In vivo, loss of Swm1 increases the global levels of both H3K9me2 and H3K4me2. A significant accumulation of H3K4me2 is observed at genes that are up-regulated in a swm1 deletion strain. In addition, H3K9me2 accumulates at some genes known to be direct Swm1/2 targets that are down-regulated in the swm1Delta strain. The in vivo data indicate that Swm1 acts in concert with the HDAC Clr6 and the chromatin remodeller Hrp1 to repress gene expression. In addition, our in vitro analyses suggest that the H3K9 demethylase activity requires an unidentified post-translational modification to allow it to act. Thus, our results highlight complex interactions between histone demethylase, deacetylase and chromatin remodelling activities in the regulation of gene expression. (+info)Functional effects of single nucleotide polymorphisms in the coding region of human N-acetyltransferase 1. (4/2123)
Genetic variants of human N-acetyltransferase 1 (NAT1) are associated with cancer and birth defects. N- and O-acetyltransferase catalytic activities, Michaelis-Menten kinetic constants (K(m) and V(max)) and steady-state expression levels of NAT1-specific mRNA and protein were determined for the reference NAT1*4 and variant human NAT1 haplotypes possessing single nucleotide polymorphisms (SNPs) in the open reading frame. Although none of the SNPs caused a significant effect on steady-state levels of NAT1-specific mRNA, C97T(R33stop), C190T(R64W), C559T (R187stop) and A752T(D251V) each reduced NAT1 protein level and/or N- and O-acetyltransferase catalytic activities to levels below detection. G560A(R187Q) substantially reduced NAT1 protein level and catalytic activities and increased substrate K(m). The G445A(V149I), G459A(synonymous) and T640G(S214A) haplotype present in NAT1*11 significantly (P<0.05) increased NAT1 protein level and catalytic activity. Neither T21G(synonymous), T402C(synonymous), A613G(M205V), T777C(synonymous), G781A(E261K) nor A787G(I263V) significantly affected K(m), catalytic activity, mRNA or protein level. These results suggest heterogeneity among slow NAT1 acetylator phenotypes. (+info)Light-activated deoxyguanosine: photochemical regulation of peroxidase activity. (5/2123)
(+info)An albumin-butyrylcholinesterase for cocaine toxicity and addiction: catalytic and pharmacokinetic properties. (6/2123)
(+info)Molecular characterization of propionyllysines in non-histone proteins. (7/2123)
(+info)Optimization of labile esters for esterase-assisted accumulation of nitroxides into cells: a model for in vivo EPR imaging. (8/2123)
(+info)Biocatalysis is the use of living organisms or their components, such as enzymes, to accelerate chemical reactions. In other words, it is the process by which biological systems, including cells, tissues, and organs, catalyze chemical transformations. Biocatalysts, such as enzymes, can increase the rate of a reaction by lowering the activation energy required for the reaction to occur. They are highly specific and efficient, making them valuable tools in various industries, including pharmaceuticals, food and beverage, and biofuels.
In medicine, biocatalysis is used in the production of drugs, such as antibiotics and hormones, as well as in diagnostic tests. Enzymes are also used in medical treatments, such as enzyme replacement therapy for genetic disorders that affect enzyme function. Overall, biocatalysis plays a critical role in many areas of medicine and healthcare.
Biotechnology is defined in the medical field as a branch of technology that utilizes biological processes, organisms, or systems to create products that are technologically useful. This can include various methods and techniques such as genetic engineering, cell culture, fermentation, and others. The goal of biotechnology is to harness the power of biology to produce drugs, vaccines, diagnostic tests, biofuels, and other industrial products, as well as to advance our understanding of living systems for medical and scientific research.
The use of biotechnology has led to significant advances in medicine, including the development of new treatments for genetic diseases, improved methods for diagnosing illnesses, and the creation of vaccines to prevent infectious diseases. However, it also raises ethical and societal concerns related to issues such as genetic modification of organisms, cloning, and biosecurity.
Immobilized enzymes refer to enzymes that have been restricted or fixed in a specific location and are unable to move freely. This is typically achieved through physical or chemical methods that attach the enzyme to a solid support or matrix. The immobilization of enzymes can provide several advantages, including increased stability, reusability, and ease of separation from the reaction mixture.
Immobilized enzymes are widely used in various industrial applications, such as biotransformations, biosensors, and diagnostic kits. They can also be used for the production of pharmaceuticals, food additives, and other fine chemicals. The immobilization techniques include adsorption, covalent binding, entrapment, and cross-linking.
Adsorption involves physically attaching the enzyme to a solid support through weak forces such as van der Waals interactions or hydrogen bonding. Covalent binding involves forming chemical bonds between the enzyme and the support matrix. Entrapment involves encapsulating the enzyme within a porous matrix, while cross-linking involves chemically linking multiple enzyme molecules together to form a stable structure.
Overall, immobilized enzymes offer several advantages over free enzymes, including improved stability, reusability, and ease of separation from the reaction mixture, making them valuable tools in various industrial applications.
Microbiology is the branch of biology that deals with the study of microorganisms, which are tiny living organisms including bacteria, viruses, fungi, parasites, algae, and some types of yeasts and molds. These organisms are usually too small to be seen with the naked eye and require the use of a microscope for observation.
Microbiology encompasses various subdisciplines, including bacteriology (the study of bacteria), virology (the study of viruses), mycology (the study of fungi), parasitology (the study of parasites), and protozoology (the study of protozoa).
Microbiologists study the structure, function, ecology, evolution, and classification of microorganisms. They also investigate their role in human health and disease, as well as their impact on the environment, agriculture, and industry. Microbiology has numerous applications in medicine, including the development of vaccines, antibiotics, and other therapeutic agents, as well as in the diagnosis and treatment of infectious diseases.
Chemical engineering is a branch of engineering that deals with the design, construction, and operation of plants and machinery for the large-scale production or processing of chemicals, fuels, foods, pharmaceuticals, and biologicals, as well as the development of new materials and technologies. It involves the application of principles of chemistry, physics, mathematics, biology, and economics to optimize chemical processes that convert raw materials into valuable products. Chemical engineers are also involved in developing and improving environmental protection methods, such as pollution control and waste management. They work in a variety of industries, including pharmaceuticals, energy, food processing, and environmental protection.
Enzymes are complex proteins that act as catalysts to speed up chemical reactions in the body. They help to lower activation energy required for reactions to occur, thereby enabling the reaction to happen faster and at lower temperatures. Enzymes work by binding to specific molecules, called substrates, and converting them into different molecules, called products. This process is known as catalysis.
Enzymes are highly specific and will only catalyze one particular reaction with a specific substrate. The shape of the enzyme's active site, where the substrate binds, determines this specificity. Enzymes can be regulated by various factors such as temperature, pH, and the presence of inhibitors or activators. They play a crucial role in many biological processes, including digestion, metabolism, and DNA replication.
Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which remains unchanged at the end of the reaction. A catalyst lowers the activation energy required for the reaction to occur, thereby allowing the reaction to proceed more quickly and efficiently. This can be particularly important in biological systems, where enzymes act as catalysts to speed up metabolic reactions that are essential for life.
Environmental biodegradation is the breakdown of materials, especially man-made substances such as plastics and industrial chemicals, by microorganisms such as bacteria and fungi in order to use them as a source of energy or nutrients. This process occurs naturally in the environment and helps to break down organic matter into simpler compounds that can be more easily absorbed and assimilated by living organisms.
Biodegradation in the environment is influenced by various factors, including the chemical composition of the substance being degraded, the environmental conditions (such as temperature, moisture, and pH), and the type and abundance of microorganisms present. Some substances are more easily biodegraded than others, and some may even be resistant to biodegradation altogether.
Biodegradation is an important process for maintaining the health and balance of ecosystems, as it helps to prevent the accumulation of harmful substances in the environment. However, some man-made substances, such as certain types of plastics and industrial chemicals, may persist in the environment for long periods of time due to their resistance to biodegradation, leading to negative impacts on wildlife and ecosystems.
In recent years, there has been increasing interest in developing biodegradable materials that can break down more easily in the environment as a way to reduce waste and minimize environmental harm. These efforts have led to the development of various biodegradable plastics, coatings, and other materials that are designed to degrade under specific environmental conditions.
Heptanes are a group of hydrocarbons that are composed of straight-chain or branched arrangements of six carbon atoms and are commonly found in gasoline. They are colorless liquids at room temperature with a characteristic odor. In a medical context, exposure to heptanes can occur through inhalation, skin contact, or ingestion, and can cause symptoms such as headache, dizziness, nausea, and irritation of the eyes, nose, and throat. Chronic exposure has been linked to more serious health effects, including neurological damage and cancer. Proper handling and use of heptanes, as well as adequate ventilation, are important to minimize exposure and potential health risks.
Solvents, in a medical context, are substances that are capable of dissolving or dispersing other materials, often used in the preparation of medications and solutions. They are commonly organic chemicals that can liquefy various substances, making it possible to administer them in different forms, such as oral solutions, topical creams, or injectable drugs.
However, it is essential to recognize that solvents may pose health risks if mishandled or misused, particularly when they contain volatile organic compounds (VOCs). Prolonged exposure to these VOCs can lead to adverse health effects, including respiratory issues, neurological damage, and even cancer. Therefore, it is crucial to handle solvents with care and follow safety guidelines to minimize potential health hazards.
Biotransformation is the metabolic modification of a chemical compound, typically a xenobiotic (a foreign chemical substance found within an living organism), by a biological system. This process often involves enzymatic conversion of the parent compound to one or more metabolites, which may be more or less active, toxic, or mutagenic than the original substance.
In the context of pharmacology and toxicology, biotransformation is an important aspect of drug metabolism and elimination from the body. The liver is the primary site of biotransformation, but other organs such as the kidneys, lungs, and gastrointestinal tract can also play a role.
Biotransformation can occur in two phases: phase I reactions involve functionalization of the parent compound through oxidation, reduction, or hydrolysis, while phase II reactions involve conjugation of the metabolite with endogenous molecules such as glucuronic acid, sulfate, or acetate to increase its water solubility and facilitate excretion.
Stereoisomerism is a type of isomerism (structural arrangement of atoms) in which molecules have the same molecular formula and sequence of bonded atoms, but differ in the three-dimensional orientation of their atoms in space. This occurs when the molecule contains asymmetric carbon atoms or other rigid structures that prevent free rotation, leading to distinct spatial arrangements of groups of atoms around a central point. Stereoisomers can have different chemical and physical properties, such as optical activity, boiling points, and reactivities, due to differences in their shape and the way they interact with other molecules.
There are two main types of stereoisomerism: enantiomers (mirror-image isomers) and diastereomers (non-mirror-image isomers). Enantiomers are pairs of stereoisomers that are mirror images of each other, but cannot be superimposed on one another. Diastereomers, on the other hand, are non-mirror-image stereoisomers that have different physical and chemical properties.
Stereoisomerism is an important concept in chemistry and biology, as it can affect the biological activity of molecules, such as drugs and natural products. For example, some enantiomers of a drug may be active, while others are inactive or even toxic. Therefore, understanding stereoisomerism is crucial for designing and synthesizing effective and safe drugs.
Protein engineering is a branch of molecular biology that involves the modification of proteins to achieve desired changes in their structure and function. This can be accomplished through various techniques, including site-directed mutagenesis, gene shuffling, directed evolution, and rational design. The goal of protein engineering may be to improve the stability, activity, specificity, or other properties of a protein for therapeutic, diagnostic, industrial, or research purposes. It is an interdisciplinary field that combines knowledge from genetics, biochemistry, structural biology, and computational modeling.
A factual database in the medical context is a collection of organized and structured data that contains verified and accurate information related to medicine, healthcare, or health sciences. These databases serve as reliable resources for various stakeholders, including healthcare professionals, researchers, students, and patients, to access evidence-based information for making informed decisions and enhancing knowledge.
Examples of factual medical databases include:
1. PubMed: A comprehensive database of biomedical literature maintained by the US National Library of Medicine (NLM). It contains citations and abstracts from life sciences journals, books, and conference proceedings.
2. MEDLINE: A subset of PubMed, MEDLINE focuses on high-quality, peer-reviewed articles related to biomedicine and health. It is the primary component of the NLM's database and serves as a critical resource for healthcare professionals and researchers worldwide.
3. Cochrane Library: A collection of systematic reviews and meta-analyses focused on evidence-based medicine. The library aims to provide unbiased, high-quality information to support clinical decision-making and improve patient outcomes.
4. OVID: A platform that offers access to various medical and healthcare databases, including MEDLINE, Embase, and PsycINFO. It facilitates the search and retrieval of relevant literature for researchers, clinicians, and students.
5. ClinicalTrials.gov: A registry and results database of publicly and privately supported clinical studies conducted around the world. The platform aims to increase transparency and accessibility of clinical trial data for healthcare professionals, researchers, and patients.
6. UpToDate: An evidence-based, physician-authored clinical decision support resource that provides information on diagnosis, treatment, and prevention of medical conditions. It serves as a point-of-care tool for healthcare professionals to make informed decisions and improve patient care.
7. TRIP Database: A search engine designed to facilitate evidence-based medicine by providing quick access to high-quality resources, including systematic reviews, clinical guidelines, and practice recommendations.
8. National Guideline Clearinghouse (NGC): A database of evidence-based clinical practice guidelines and related documents developed through a rigorous review process. The NGC aims to provide clinicians, healthcare providers, and policymakers with reliable guidance for patient care.
9. DrugBank: A comprehensive, freely accessible online database containing detailed information about drugs, their mechanisms, interactions, and targets. It serves as a valuable resource for researchers, healthcare professionals, and students in the field of pharmacology and drug discovery.
10. Genetic Testing Registry (GTR): A database that provides centralized information about genetic tests, test developers, laboratories offering tests, and clinical validity and utility of genetic tests. It serves as a resource for healthcare professionals, researchers, and patients to make informed decisions regarding genetic testing.
'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.
While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.
E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.
Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).
Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.
Substrate specificity can be categorized as:
1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.
Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.
Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.
Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.
The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.
Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.
Biocatalysis
Biocatalysis & Biotransformation
Ben G. Davis
Nicotinamide
Nicotinonitrile
New Biotechnology
Phenylalanine ammonia-lyase
Cericlamine
Nocardioides
Arthrobacter crystallopoietes
Kitasatospora xanthocidica
Caldanaerovirga
Penicillium oxalicum
Marco Fraaije
Glycogen debranching enzyme
Solvolysis
Health effects of Bisphenol A
Arenobufagin
4-hydroxyacetophenone monooxygenase
Cytophagales
Paenarthrobacter nicotinovorans
Ureibacillus terrenus
Katja Loos
Penicillium miczynskii
Roger A. Sheldon
Monascus
Ribozyme
GIR1 branching ribozyme
Pleurotus eryngii
Melting curve analysis
Biocatalysis - Wikipedia
Transaminase Biocatalysis: Applications and Fundamental Studies | KTH
Green-by-Design: Award-winning Innovations in Biocatalysis - American Chemical Society
CDMO | Biocatalysis | Cambrex
Biosynthesis and Biocatalysis of Natural Products | Florida Atlantic University
View of Industrial Biocatalysis
BioNoCo - Biocatalysis Using Non-Conventional Media (GRK 1166) - RWTH AACHEN UNIVERSITY - English
Biocatalysis performed with Syrris products
View of The Development of Biocatalysis as a Tool for Drug Discovery
Microscale Atmospheric Pressure Plasma Jet as a Source for Plasma-Driven Biocatalysis | TU Delft Repositories
Center for Biocatalysis and Bioengineering of Macromolecules | NSF - National Science Foundation
Brenntag Specialties Pharma provides new tailor-made service that creates sustainable enzyme stability for bio-catalysis |...
tks | publisher, event organiser, media agency | Catalysis & Biocatalysis - Vol. 35(5) - tks | publisher, event organiser,...
A highly efficient synthesis of telaprevir by strategic use of biocatalysis and multicomponent reactions<...
CCBIO Symposium on Industrial Biocatalysis 2023 - Conference Report - Biotechnet Switzerland
INDUSTRIAL BIOCATALYSIS | Università degli studi dell'Insubria
Biocatalysis: Overcoming Equilibrium Issues with Carbonyl Reductase Enzymes - Almac
Enzymatic research lines of Biocatalysis & Organic Chemistry - TU Delft Research Portal
Continuous flow biocatalysis: production and in-line purification of amines by immobilised transaminase from Halomonas elongata...
First results of the collaboration between Olon Group, Biosphere and the University of Amsterdam on biocatalysis project
Prozomix - Products - Biocatalysis Enzyme Kits - PRO-HHDHP HHDHs - Halohydrin Dehalogenases - Maximum Diversity Panel (kit of...
How to close the carbon loop with CO2 conversion
Biocatalysis Services | Cambrex
Biocatalysis. Medical search
CDMO | Biocatalysis | Cambrex
Catalysis and Biocatalysis - ICB
Continuous flow biocatalysis - Vapourtec
Biocatalysis - Adrea's Notebook and Journal
Novo Nordisk Fonden - Epigenetic Proteins: Synthesis, Biomolecular Recognition and Biocatalysis - University of Southern...
Biotechnology
Plasma-driven biocatalysis3
- Overall, the μAPPJ presents a promising plasma source for plasma-driven biocatalysis. (tudelft.nl)
- In plasma-driven biocatalysis, we intend to use technical plasmas to drive enzymes that use hydrogen peroxide to convert a substrate into a more valuable product," explains Julia Bandow, Head of the Department of Applied Microbiology. (bioengineer.org)
- They showed in initial studies that although it works for plasma-driven biocatalysis, there are some fundamental limitations. (bioengineer.org)
Enzymes4
- Biocatalysis is the branch of science at the intersection between chemistry and biology and specifcally dedicated to the application of natural evolvable catalysts, i.e. enzymes, in human-designed chemical processes. (kth.se)
- Thierry Schlama (Novartis Pharma AG) gave an overview on how biocatalysis is used at Novartis through early phase to full scale manufacturing and how enzymes are optimized for specific applications. (biotechnet.ch)
- Biocatalysis uses enzymes to achieve reactions that have a commercial value, outside of the biological context in which they were 'designed' to work in. (adreasnow.com)
- Biocatalysis uses enzymes to replace traditional catalysts. (hotdailytrends.com)
Enzymology2
- It is our pleasure to share our knowledge and skill on fermentation, biocatalysis, enzymology and microbiology. (indienz.com)
- Just let us know what you want and we provide you innovative solutions through consultation on fermentation, biocatalysis, enzymology and microbiology. (indienz.com)
20231
- 18 May 2023 - The partnership, which will be continued in the future with other research projects, brings together some of the most advanced expertise in the field of biocatalysis from both academic and industrial spheres, to implement large-scale biocatalysis as an industrial technology used within its production facilities in Italy and around the world. (federchimica.it)
Synthesis1
- The use of biocatalysis to obtain enantiopure compounds can be divided into two different methods: Kinetic resolution of a racemic mixture Biocatalyzed asymmetric synthesis In kinetic resolution of a racemic mixture, the presence of a chiral object (the enzyme) converts one of the stereoisomers of the reactant into its product at a greater reaction rate than for the other reactant stereoisomer. (wikipedia.org)
Biosynthesis1
- The research in my group focuses on the biosynthesis and biocatalysis of marine natural products, especially those with potential applications in medicine, veterinary medicine and agriculture. (fau.edu)
Reactions1
- Biocatalysis refers to the use of living (biological) systems or their parts to speed up (catalyze) chemical reactions. (wikipedia.org)
Processes1
- With the world's largest and most diverse collection of enzyme strains, coupled with a global, robust and reliable supply, Novozymes is here to help you unlock the full potential of your biocatalysis route and make your manufacturing processes more sustainable. (novozymes.com)
Continuous1
- With continuous flow systems offering improved mixing, mass transfer, thermal control, pressurized processing, decreased variation, automation, process analytical technology, and in-line purification, the combination of biocatalysis and flow chemistry opens powerful new process windows. (vapourtec.com)
Fermentation1
- The partnership, bringing together some of the most advanced expertise in the field of biocatalysis from both academic and industrial spheres, unites the Olon Group, Biosphere - an Italian SME specialised in fermentation and industrial biotechnology - and the Biocatalysis Group of the Van't Hoff Institute for Molecular Sciences (HIMS-Biocat) at the University of Amsterdam (UvA). (federchimica.it)
Chemists2
- These reasons, and especially the latter, are the major reasons why synthetic chemists have become interested in biocatalysis. (wikipedia.org)
- Chemists who want to learn how biocatalysis can help them. (scientificupdate.com)
Heterogeneous catalysis1
- However, mechanistically speaking, biocatalysis is simply a special case of heterogeneous catalysis. (wikipedia.org)
Fundamentals1
- Biocatalysis: Fundamentals and Applications, A. S. Bommarius and B. R. Riebel. (uninsubria.eu)
Chemical2
- Biocatalysis underpins some of the oldest chemical transformations known to humans, for brewing predates recorded history. (wikipedia.org)
- More than one hundred years ago, biocatalysis was employed to do chemical transformations on non-natural man-made organic compounds, with the last 30 years seeing a substantial increase in the application of biocatalysis to produce fine chemicals, especially for the pharmaceutical industry. (wikipedia.org)
Applications1
- Individuals from all over the world who have expertise and interest in the field of biocatalysis and its applications are invited to join ESAB and are welcome to submit online their application form to the ESAB Office. (esabweb.org)
Protein1
- The ideal candidate for this project is an experimental chemist, with affinity or interest in biocatalysis, bioinformatics and protein engineering. (hotdailytrends.com)
University2
- The 4th annual CCBIO was organized by ZHAW - Zürich University of Applied Sciences and the Competence Center of Biocatalysis (CCBIO). (biotechnet.ch)
- The project, entitled Biocatalysis for new products based on hemicellulose, includes researchers Henrik Stålbrand (project manager), Tommy Nylander, Patric Jannasch and Ola Wallberg from the Faculty of Science and the Faculty of Engineering at Lund University. (lu.se)
Technology4
- The Graduate Research Training Group supports young researchers who wish to specialize in biocatalysis, an interdisciplinary field of research at the crossroads of biology, chemistry, and process technology. (rwth-aachen.de)
- We have a proven track record of saving time and cost through the integration of our services and application of innovative biocatalysis and technology solutions. (almacgroup.com)
- The international network was created with the objective to launch large-scale biocatalysis as an industrial technology used within Olon production facilities in Italy and around the world. (federchimica.it)
- Despite the growing impact of biocatalysis in industrial chemistry, the full potential of this technology is yet to be unlocked. (hotdailytrends.com)
Advances2
- This one-day symposium provided the opportunity to network and get an update on advances in the field of biocatalysis. (biotechnet.ch)
- It provides an overview of the latest advances in biocatalysis and biotransformations by integrating the know-how of experts and early-career researchers from academia and industry. (biocat-congress.de)
Chemicals1
- Biocatalysis is gaining in significance as it helps to make the building blocks of pharmaceutical ingredients and fine chemicals much more accessible. (rwth-aachen.de)
Research3
- Biocatalysis is increasingly used in industry and is a valuable tool for pharmaceutical research and development. (biotechnet.ch)
- The final exam will start discussing a recent research paper or patent, selected by the candidate, describing an industrially relevant application of biocatalysis. (uninsubria.eu)
- Companies as well as academic, governmental, research and other public Institutions whose activities are related to the field of applied biocatalysis, are welcome to apply for Institutional Membership. (esabweb.org)
Industrial1
- The aims of ESAB are to promote initiatives in areas of growing scientific and industrial interest of importance within the field of Applied Biocatalysis. (esabweb.org)
Products1
- Below is a list of publications involving biocatalysis performed with our products. (syrris.com)
Development1
- ESAB has been founded in 1980 and has the mission of promoting the development of Applied Biocatalysis throughout Europe. (esabweb.org)
Potential1
- The use of a microscale atmospheric pressure plasma jet (μAPPJ) was investigated for its potential to supply hydrogen peroxide in biocatalysis. (tudelft.nl)