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Kinetics of Enzymatic Synthesis gives insight into different aspects of chemical reactions that are catalyzed by enzymes. This book is divided into two sections: ""Enzyme Kinetics"" and ""Enzymatic Synthesis"". The first section consists of two chapters with a halophilic enzyme kinetics and thermodynamic approach towards analyzing the influence of co-solvents on the Michaelis constants of enzyme-catalyzed reactions. The second section consists of three chapters. Production of isoamyl acetate using the enzymatic synthesis method between acetic anhydride and isoamyl alcohol by having enzyme Candida antarctica Lipase B as catalyst in a solvent-free system is discussed in the third chapter. The integrated scheme with the use of the filtrate from the pretreatment of the CS and the growth conditions of Pleurotus cystidiosus is studied in the fourth chapter. The last chapter of this section provides the conditions of the key parameters in microfluidic systems (residence times, flow rates, concentrations) applied for a sequential process from liquid/liquid extraction of LVV-h7.
Biochemistry. --- Enzyme kinetics. --- Enzymes --- Synthesis. --- Enzyme synthesis --- Dynamics, Enzyme --- Enzyme dynamics --- Kinetics, Enzyme --- Chemical kinetics --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Medical sciences --- Kinetics --- Composition --- Life Sciences --- Genetics and Molecular Biology --- Biochemistry --- Enzymology
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This Special Issue examines state-of-the-art in-cell NMR spectroscopy as it relates to biological systems of increasing complexity. The compendia of research and recent innovations from prominent laboratories in the field of solid state and solution in-cell NMR spectroscopy, metabolomics and technology development are presented. The work establishes in-cell NMR spectroscopy as the premier method for determining the structures and interaction capabilities of biological molecules at high resolution within the delicately intricate interior of living cells, and the means of utilizing cells as living laboratories to directly assess the effects of exogenous and endogenous stimuli on cell physiology.]
protein NMR --- time-resolved NMR --- Ribosome --- structural calculation 4 --- crystalline and amorphous starch --- in-cell NMR --- protein dynamics --- DNP --- protein modification --- Tau --- spectrum reconstruction 3 --- mRNA --- Thioredoxin --- protein structure --- protein interactions --- drug discovery --- protein structure determination 1 --- review --- enzyme activity --- MARK2 phosphorylation --- post-translational modifications --- Dihydrofolate reductase --- mammalian cells --- target engagement --- non-uniform sampling 2 --- paramagnetic effects --- protein structure-function --- cross-correlated relaxation --- structure function --- rRNA --- 2D INADEQUATE --- lipid membrane --- Thymidylate synthase --- whole cell NMR --- enzyme kinetics --- magic-angle spinning --- live cell --- solid-state NMR --- Adenylate kinase --- DNA --- in-situ NMR --- antimicrobial peptide --- NMR spectroscopy --- intrinsically disordered proteins
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This book has been written with the purpose of providing a vision of a topic which is on the edge of biology and chemistry. As well, we want to provide an updated vision of the potentials and limitations of biocatalysis, especially with respect to applications in processes of organic synthesis, fine chemicals, and medicine. This book pretends to illustrate the potential of an excellent overview of recent progress on the assessment of granted patents as a useful tool in asymmetric synthesis. Some distinguished researchers have contributed to this endeavor with their knowledge, their commitment and their encouragement
ferulic acid esters --- octyl ferulate --- esterification --- Box-Behnken design --- response surface methodology --- molar conversion --- optimum condition --- Bacillus --- glycosyltransferase --- 8-hydroxydaidzein --- industrial biotechnology --- electrochemistry --- biohydrogen --- biocatalysis --- process development --- bacteria --- Enantioselectivity --- enzyme cascade --- hydroxynitrile lyase --- lipase --- hydrocyanation --- transesterification --- glycosidases --- transglycosylation --- cyclodextrin glycosyltransferases --- alkyl glucosides --- biosurfactants --- MDR—medium-chain reductase/dehydrogenase --- ADH—alcohol dehydrogenase --- enzyme kinetics --- EDTA (Ethylenediaminetetraacetic acid) chelation --- ultrafiltration --- pseudokinases --- signal transduction --- cancer therapy --- tyrosine/serine/threonine phosphorylation --- new drug targets --- interactome --- asymmetric synthesis --- patents --- lipases --- oxidoreductases --- lyases --- transaminases --- n/a --- MDR-medium-chain reductase/dehydrogenase --- ADH-alcohol dehydrogenase
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Contamination of foods and agricultural commodities by various types of toxigenic fungi is a concerning issue for human and animal health. Moulds naturally present in foods can produce mycotoxins and contaminate foodstuffs under favourable conditions of temperature, relative humidity, pH, and nutrient availability. Mycotoxins are, in general, stable molecules that are difficult to remove from foods once they have been produced. Therefore, the prevention of mycotoxin contamination is one of the main goals of the agriculture and food industries. Chemical control or decontamination techniques may be quite efficient; however, the more sustainable and restricted use of fungicides, the lack of efficiency in some foods, and the consumer demand for chemical-residue-free foods require new approaches to control this hazard. Therefore, food safety demands continued research efforts for exploring new strategies to reduce mycotoxin contamination. This Special Issue contains original contributions and reviews that advance the knowledge about the most current promising approaches to minimize mycotoxin contamination, including biological control agents, phytochemical antifungal compounds, enzyme detoxification, and the use of novel technologies.
n/a --- decontamination --- superheated steam --- quercetin glycosides --- antagonism --- mode of action --- corn --- Botrytis sp. --- AITC --- binding --- degradation --- brine shrimp bioassay --- apple pomace --- nanoparticles --- enzymatic detoxification --- Bacillus --- estrogen response element --- Fusarium --- biological detoxification --- abiotic factors --- stability --- fumonisin esterase FumD --- mycotoxigenic fungi --- Aspergillus flavus --- Aflatoxin M1 --- Fusarium graminearum --- milk --- Penicillium digitatum --- biocontrol agents --- biological control --- dry-cured ham --- mycotoxin reduction --- Fusarium sp. --- enzyme kinetics --- Penicillium nordicum --- Satureja montana --- roasted coffee --- fermentation --- crisp biscuit --- detoxification --- essential oils --- gene expression --- probiotics --- zearalenone --- mycotoxins --- degradation products --- Geothrichum citri-aurantii --- garlic-derived extracts --- Zearalenone --- biodegradation --- EU limits --- storage --- Origanum virens --- aflatoxin --- fungal growth reduction --- green chemistry --- Penicillium italicum --- deoxynivalenol --- ?-Fe2O3 --- ochratoxin A (OTA) --- wheat --- cell-free extracts of Aspergillus oryzae --- photocatalysis --- wheat quality --- post-harvest phytopathogen --- cold plasma --- pinnatifidanoside D --- ochratoxin A --- oats --- cell proliferation --- estrogen receptor --- Penicillium verrucosum --- pig production performance --- phloridzin --- maize --- biotransformation --- fumonisin --- fungi
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Iron–sulfur (FeS) centers are essential protein cofactors in all forms of life. They are involved in many key biological processes. In particular, Fe-S centers not only serve as enzyme cofactors in catalysis and electron transfer, they are also indispensable for the biosynthesis of complex metal-containing cofactors. Among these cofactors are the molybdenum (Moco) and tungsten (Wco) cofactors. Both Moco/Wco biosynthesis and Fe-S cluster assembly are highly conserved among all kingdoms of life. After formation, Fe-S clusters are transferred to carrier proteins, which insert them into recipient apo-proteins. Moco/Wco cofactors are composed of a tricyclic pterin compound, with the metal coordinated to its unique dithiolene group. Moco/Wco biosynthesis starts with an Fe-S cluster-dependent step involving radical/S-adenosylmethionine (SAM) chemistry. The current lack of knowledge of the connection of the assembly/biosynthesis of complex metal-containing cofactors is due to the sheer complexity of their synthesis with regard to both the (genetic) regulation and (chemical) metal center assembly. Studies on these metal-cofactors/cofactor-containing enzymes are important for understanding fundamental cellular processes. They will also provide a comprehensive view of the complex biosynthesis and the catalytic mechanism of metalloenzymes that underlie metal-related human diseases.
CO dehydrogenase --- dihydrogen --- hydrogenase --- quantum/classical modeling --- density functional theory --- metal–dithiolene --- pyranopterin molybdenum enzymes --- fold-angle --- tungsten enzymes --- electronic structure --- pseudo-Jahn–Teller effect --- thione --- molybdenum cofactor --- Moco --- mixed-valence complex --- dithiolene ligand --- tetra-nuclear nickel complex --- X-ray structure --- magnetic moment --- formate hydrogenlyase --- hydrogen metabolism --- energy conservation --- MRP (multiple resistance and pH)-type Na+/H+ antiporter --- CCCP—carbonyl cyanide m-chlorophenyl-hydrazone --- EIPA—5-(N-ethyl-N-isopropyl)-amiloride --- nicotinamide adenine dinucleotide (NADH) --- electron transfer --- enzyme kinetics --- enzyme structure --- formate dehydrogenase --- carbon assimilation --- Moco biosynthesis --- Fe-S cluster assembly --- l-cysteine desulfurase --- ISC --- SUF --- NIF --- iron --- molybdenum --- sulfur --- tungsten cofactor --- aldehyde:ferredoxin oxidoreductase --- benzoyl-CoA reductase --- acetylene hydratase --- [Fe]-hydrogenase --- FeGP cofactor --- guanylylpyridinol --- conformational changes --- X-ray crystallography --- iron-sulfur cluster --- persulfide --- metallocofactor --- frataxin --- Friedreich’s ataxia --- n/a --- metal-dithiolene --- pseudo-Jahn-Teller effect --- CCCP-carbonyl cyanide m-chlorophenyl-hydrazone --- EIPA-5-(N-ethyl-N-isopropyl)-amiloride --- Friedreich's ataxia
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The scope of this Special Issue is to collect some of the contributions to the First International Electronic Conference on Biosensors, which was held to bring together well-known experts currently working in biosensor technologies from around the globe, and to provide an online forum for presenting and discussing new results. The world of biosensors is definitively a versatile and universally applicable one, as demonstrated by the wide range of topics which were addressed at the Conference, such as: bioengineered and biomimetic receptors; microfluidics for biosensing; biosensors for emergency situations; nanotechnologies and nanomaterials for biosensors; intra- and extracellular biosensing; and advanced applications in clinical, environmental, food safety, and cultural heritage fields.
Listeria monocytogenes --- cell-based biosensor --- bioelectric recognition assay --- membrane-engineering --- lateral flow immunoassay --- antibiotics --- lincomycin --- gold nanoparticles --- quantum dots --- surface-enhanced Raman spectroscopy --- Fumonsin B1 --- aptamers --- UV/VIS spectroscopy --- asymmetric flow field-flow fractionation --- porous silicon membrane --- bacterial detection --- selective lysis --- endolysins --- lysostaphin --- flow-through --- vibrational spectra --- molecular dynamics --- nucleotides --- Au nanoparticle --- SERS --- space biology --- deep space --- biosensors --- space radiation --- microgravity --- CubeSats --- 2D Ti3C2 MXene --- PGE2 --- 8-HOA --- lung cancer --- electrochemical --- DNA biosensors --- KRAS --- liquid biopsy --- cancer point-of-care diagnostic tests --- paper-based sensors --- nitrocellulose --- impedance measurements --- dielectric properties --- parallel-plate electrodes --- interdigital electrodes --- Bacillus thuringiensis --- sensor --- combined slot antenna --- diabetes --- dielectric permeability --- electromagnetic fields --- glucose concentration --- near-field sensor --- non-invasive measurements --- microwave sounding --- chymotrypsin --- β-casein --- nanoparticles --- UV-vis spectroscopy --- dynamic light scattering --- quartz crystal microbalance --- biologically inspired --- electronic eye --- optical methods --- RGB analysis --- tequila --- molecularly imprinted polymer (MIP) --- surface plasmon resonance (SPR) --- plastic optical fiber (POF) --- 2-furaldheide (2-FAL) --- beverages --- optical chemical sensors --- biosensor --- immunosensor --- cardiac troponin I --- single-strand DNA --- electrochemical impedance spectroscopy --- label-free --- proteins --- microfluidic chip --- self-assembled monolayers --- odor sensor --- market analysis --- technology assessment --- application field --- performance profile --- requirement profile --- biointelligence --- biological transformation --- temperature sensor --- Raman spectroscopy --- anti-Stokes/Stokes spectra --- titanium dioxide --- trypsin --- AuNPs --- acoustic wave biosensor --- colorimetric assay --- white light reflectance spectroscopy --- real-time immunosensor --- ELISA --- pesticides --- carbendazim --- fruit juices --- ECIS --- xCELLigence --- cellZscope --- hCMVEC --- endothelial cell --- impedance sensing --- light-addressable potentiometric sensor --- light-addressable electrode --- actuator-sensor system --- enzyme kinetics --- microfluidics --- HIV-1 p24 protein --- surface plasmon resonance --- surface modifications --- label-free detection --- artificial enzymes --- green synthesis --- hexacyanoferrates of transition and noble metals --- peroxidase mimetic --- amperometric (bio)sensor --- glucose oxidase --- glucose analysis --- electrocatalysis --- peroxynitrite --- flow injection analysis --- meat extracts --- myoglobin --- cobalt phthalocyanine --- electrochemical reduction --- screen-printed carbon electrode --- amperometric detection --- decay kinetics
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