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HydrolysisTrypsinSubstrate SpecificityKineticsMolecular Sequence DataAmino Acid SequenceBinding SitesCatalysisAdenosine TriphosphateHydrogen-Ion ConcentrationModels, MolecularTrypsin Inhibitor, Kunitz SoybeanChymotrypsinTrypsin Inhibitor, Kazal PancreaticEscherichia coliProtein BindingProtein ConformationRecombinant ProteinsMolecular WeightCattleAdenosine TriphosphatasesTrypsin Inhibitor, Bowman-Birk SoybeanCatalytic DomainChromatography, High Pressure LiquidAprotininStructure-Activity RelationshipBase SequenceProtein Structure, TertiaryEndopeptidasesSequence Homology, Amino AcidPeptide FragmentsMutagenesis, Site-DirectedAmino AcidsTrypsinogenPeptide HydrolasesBacterial ProteinsMutationEnzyme ActivationCrystallography, X-RayChromatography, GelTemperatureGuanosine TriphosphateProtease InhibitorsEstersPeptidesSerine EndopeptidasesMolecular StructurePhosphatidylinositolsModels, ChemicalCloning, MolecularPhosphorylationCell LineAdenosine DiphosphateStereoisomerismCell MembraneOxidation-ReductionCarboxylic Ester HydrolasesOligopeptidesEnzyme StabilityRabbitsPancreasChemistryChemical PhenomenaMagnetic Resonance SpectroscopyElectrophoresis, Polyacrylamide GelEscherichia coli ProteinsLipaseSequence AlignmentMass SpectrometryLiverIsoenzymesGlycoside HydrolasesSwinePhosphatesBiological TransportModels, BiologicalTime FactorsEsterasesAmidohydrolasesAmino Acid SubstitutionCells, CulturedMacromolecular SubstancesCalciumSaccharomyces cerevisiaeDNAHot TemperatureReceptor, PAR-2CarboxypeptidasesEnzyme InhibitorsPhospholipasesProteinsBenzoylarginine NitroanilideLysineChromatography, Thin LayerDipeptidesSerine Proteinase InhibitorsPapainNucleotidesCarrier ProteinsThermodynamics

EnzymesEnzymaticSpecificityPeptidesLysinePeptideProteinsInhibitChymotrypsinPeptidaseCatalyticHydrolysatesCarboxyl sideSerine proteaseResiduesPolypeptideAnother moleculeAnalogsRigidityEsterCovering a broad physiological rangeReactionMolecular WeightTemperatureActivitySubstanceReactionsBreakdownCovalentSubunitFree enzymeResidueDependentConcentrationBondsPancreaticActionsMechanismOrganic

Enzymes10

• His research focused mainly on the proteolytic enzymes, which catalyze the hydrolysis of protein substrates. (wikipedia.org)
• Neurath's work on proteolytic enzymes included studies of trypsin, carboxypeptidase and thermolysin. (wikipedia.org)
• Different specific and non-specific enzymes are used to obtain hydrolysates (trypsin, pepsin, pancreatin and alcalase). (intechopen.com)
• The processive type of cellulase is crucial for efficient cellulose hydrolysis, and most of the characterized processive enzymes are exoglucanases, although endoglucanases of the processive type have been identified 6 . (nature.com)
• The lumen's pH ( 45 -5.0) (2) is optimal for the enzymes involved in hydrolysis, similar to the exertion of the stomach. (infinitylearn.com)
• CytoSoft® products accommodate the harvesting of cells using enzymes such as trypsin and collagenase. (cellsystems.eu)
• By dissolving the pneumococcus in bile and testing the cell-free solution on suitable substrates, enzymes are readily demonstrable. (nih.gov)
• An enzyme works only on a specific substance, called a substrate, which fits perfectly into the enzymes activity site. (naturalproductsinsider.com)
• For food protein hydrolysates, the substrate and enzymes are mixed in huge, tempered tanks, and require continuous stirring, as well as a constant temperature and pH level for several hours. (springeropen.com)
• All three enzymes are synthesized by the pancreatic acinar cells, secreted in the small intestine and are responsible for catalyzing the hydrolysis of peptide bonds . (wikidoc.org)

Enzymatic7

• Plants possess different ACE inhibitory peptides which can be obtained by enzymatic hydrolysis [ 11 , 12 ]. (hindawi.com)
• Nowadays the most common way to obtain bioactive peptides is by enzymatic hydrolysis of protein solutions. (intechopen.com)
• Enzymatic hydrolysis is the best way to hydrolyze fish skin without losing nutritional value (Huang et al. (e-fas.org)
• The A1 fragment is responsible for the intracellular enzymatic activities of the toxin in the presence of the membrane Arf factor, including NAD hydrolysis in ADP ribose and nicotinamide, and transfer of ADP ribose to Arg-187 of the α-subunit of the stimulatory protein Gsα, leading to a continuous stimulation of adenylyl cyclase and elevated intracellular cAMP. (medscape.com)
• Hydrolysis is conducted by an enzymatic or acidic breakdown of proteins (Tsugita and Scheffler 1982 ). (springeropen.com)
• When substrate concentration increases, the velocity of enzymatic reaction increases at first. (bankofbiology.com)
• Pretreatment increases the efficiency of subsequent enzymatic hydrolysis of plant polysaccharides. (biomedcentral.com)

Specificity2

• Differs from pancreatic elastase in specificity on synthetic substrates and in inhibitor sensitivity. (enzyme-database.org)
• We show here that recombining the N-terminal subdomain from coagulation factor X with the C-terminal subdomain from trypsin creates a potent enzyme (fXYa) with novel properties, in particular a broad substrate specificity. (nih.gov)

Peptides5

• The most studied substrates used to produce bioactive peptides are milk proteins in the form of co-products from dairy industries: caseins, cheese whey, buttermilk, whey protein concentrates and isolates or even pure single proteins that can be obtained at a reasonable price on an industrial scale (e.g. β-lactoglobulin, β-Lg). (intechopen.com)
• Fish protein hydrolysates contain peptides of 2-20 amino acid sequences after hydrolysis, and these peptides usually have biological activity. (e-fas.org)
• Trypsin cleaves peptides on the C-terminal side of lysine and arginine residues. (sigmaaldrich.com)
• Chymotrypsin -- An enzyme that catalyses the hydrolysis (the breakdown) of proteins into peptides or amino acids in the small intestine. (nih.gov)
• In an activated form, they hydrolyze the protein substrate at specific sites and the released peptides can be absorbed. (springeropen.com)

Lysine4

• A Hammett plot of the catalytic rate constants gave a straight line with a p value of - 1.79 at 37°C thus indicating that electron withdrawing substituents inhibit the trypsin-catalysed hydrolysis of the new lysine substrates. (edu.ng)
• We have employed this device to measure the kinetics of a model reaction, namely the hydrolysis of N2-(carbobenzyloxy)-L-lysine-p-nitrophenyl ester-catalyzed by trypsin. (kent.ac.uk)
• It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. (lookformedical.com)
• This can then interact with positively-charged residues such as arginine and lysine on the substrate peptide to be cleaved. (wikidoc.org)

Peptide9

• Protease activity was measured by monitoring the hydrolysis of peptide-based substrates. (qub.ac.uk)
• EDTA is added to trypsin solutions as a chelating agent that neutralizes calcium and magnesium ions that obscure the peptide bonds on which trypsin acts. (sigmaaldrich.com)
• Trypsin consists of a single chain polypeptide of 223 amino acid residues, produced by the removal of the N-terminal hexapeptide from trypsinogen which is cleaved at the Lys - lle peptide bond. (sigmaaldrich.com)
• Some of the first synthetic inhibitors designed to target the proteasome were peptide aldehydes that act as substrate analogues and potent transition-state inhibitors, primarily of the chymotrypsin-like activity of the 20S proteasome [41]. (innovation-ecosystems-agora.com)
• The correct amino acid sequence of E. coli isoleucyl-tRNA synthetase (IleRS) was established by means of peptide mapping by MALDI mass spectrometry, using a set of four endoproteases (trypsin, LysC, AspN and GluC). (openbiochemistryjournal.com)
• The enzyme specific peptide fingerprint produced with this proteolytic capillary reactor system correlated with the degree of hydrolysis, which can be controlled over the residence time by adjusting the flow rate. (springeropen.com)
• Trypsin is responsible for cleaving peptide bonds following a positively-charged amino acid residue. (wikidoc.org)
• The catalysis of the peptide cleavage can be seen as a ping-pong catalysis, in which a substrate binds (in this case, the polypeptide being cleaved), a product is released (the N-terminus "half" of the peptide), another substrate binds (in this case, water), and another product is released (the C-terminus "half" of the peptide). (wikidoc.org)
• The serine has an -OH group that is able to act as a nucleophile , attacking the carbonyl carbon of the scissile peptide bond of the substrate. (wikidoc.org)

Proteins5

• Hydrolysis of proteins, including elastin. (enzyme-database.org)
• substrate proteins to degradation might be influenced by purified endopeptidases (chymotrypsin and trypsin). (123dok.net)
• The apical domain is located at the entrance of the cylinder and binds GroES and substrate proteins using hydrophobic surfaces [6,7]. (scirp.org)
• During the folding cycle of substrate proteins by GroEL, GroES and ATP bind to one of the two rings of the GroEL molecule, called the cis-ring, and form a bullet-type complex [9-13]. (scirp.org)
• Common food proteins like casein, sunflower and lupin protein isolates were tested for continuous hydrolysis in the developed reactor system. (springeropen.com)

Inhibit1

• hydrates to simpler products, and of splitting esters to fatty acids, In demonstrating carbohydrate cleavage, however, bile was found to inhibit completely the hydrolysis of sucrose and starch, and another method of Preparing the enzyme solution was necessary. (nih.gov)

Chymotrypsin5

• Chymotrypsin also catalyses the hydrolysis of ester bonds. (nih.gov)
• 18]SNDecreased 20S chymotrypsin-like, trypsin-like, and caspase-like activities. (innovation-ecosystems-agora.com)
• Decreased 20S chymotrypsin-like, trypsin-like, and caspase-like actions. (innovation-ecosystems-agora.com)
• The three serine proteases of the chymotrypsin-like clan that have been studied in greatest detail are chymotrypsin , trypsin , and elastase . (wikidoc.org)
• The pocket that is in "trypsin" and "chymotrypsin" is now partially filled with valine and threonine , rendering it a mere depression, which can accommodate these smaller amino acid residues. (wikidoc.org)

Peptidase2

• In peptidase family S1 (trypsin family). (enzyme-database.org)
• The absence of haemolytic activity and proteinase (trypsin) and the presence of a strong peptidase (leucine-arylamidase) and esterase-lipase (C4 and C8) were observed in this LAB strain. (biomedcentral.com)

Catalytic2

• The catalytic activity of some of them is quite specific and the composition of the hydrolysate is predictable when substrates are quite pure [ 1 ]. (intechopen.com)
• A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. (lookformedical.com)

Hydrolysates1

• 2012 ). Fish by-products like skin and frame need to be processed into fish hydrolysates either by fermentation or by hydrolysis techniques before they can be effectively utilized. (e-fas.org)

Carboxyl side1

• The rate of hydrolysis of this reaction is slowed if an acidic residue is on either side of the cleavage site and hydrolysis is stopped if a proline residue is on the carboxyl side of the cleavage site. (sigmaaldrich.com)

Serine protease1

• Trypsin is a member of the serine protease family. (sigmaaldrich.com)

Residues1

• Analysis by MALDI mass spectrometry designated cysteines-462 and -718 as the target residues of the substrate analog IBMK on E. coli IleRS, whereas VBMK, NleBMK and FBMK labeled in common His-394, His-478 and Cys-718. (openbiochemistryjournal.com)

Polypeptide1

• GroEL interacts with cochaperone GroES, a single heptamer ring of 10-kDa subunits, in an ATP-dependent manner and forms an enclosed cavity with a hydrophilic wall chamber where folding of the non-native polypeptide substrate occurs [1-5]. (scirp.org)

Another molecule2

• Here, the enzyme breaks it down into usable partssuch as lactose broken into glucose and galactosethen releases the parts and is ready to act on another molecule of that substrate. (naturalproductsinsider.com)
• The terminal phosphate groups are highly reactive in the sense that their hydrolysis, or transfer to another molecule, takes place with the release of a large amount of free energy. (nih.gov)

Analogs1

• Thereafter, the active site of IleRS was mapped by affinity labeling with reactive analogs of the substrates. (openbiochemistryjournal.com)

Rigidity2

• The rigidity of the substrate to which cells adhere can have a profound effect on cell morphology and gene expression. (cellsystems.eu)
• CytoSoft ® products provide a tool to culture cells on PDMS substrates with various rigidity covering a broad physiological range, including 0.2, 0.5, 2, 8, 16, 32, and 64 kPa. (advancedbiomatrix.com)

Ester1

• Trypsin can also act to cleave ester and amide linkages of synthetic derivatives of amino acids. (sigmaaldrich.com)

Covering a broad physiological range1

• CytoSoft® products provide a tool to culture cells on substrates with various rigidities covering a broad physiological range. (cellsystems.eu)

Reaction1

• After reaching a maximum velocity (Vmax), the reaction is not exceeded by any further rise in the concentration of substrate. (bankofbiology.com)

Molecular Weight1

• immuno-with, for example, substrate or other low molecular weight blotting and activity measurements. (123dok.net)

Temperature2

• Variables including hydrolysis time, enzyme-to-substrate ratio (E/S), pH, and temperature were standardized to acquire the most suitable and optimum ACE inhibition activity. (hindawi.com)
• a) Temperature, pH, concentration of substrate etc. (bankofbiology.com)

Activity3

• In conclusion, the recombinantly produced XT6 demonstrated efficient hydrolysis of starter and grower feeds, and produced XOS that showed prebiotic activity on selected probiotic bacteria. (ru.ac.za)
• The optimal pH for trypsin activity is 7-9. (sigmaaldrich.com)
• 8. a) Effect of change in concentration of substrate on enzyme activity is graphically represented. (bankofbiology.com)

Substance1

• Each enzyme works only on one specific substance (called the substrate). (nih.gov)

Reactions1

• Mass spectrometry offers a potential means of measuring virtually all enzyme-catalyzed reactions by simultaneously measuring the concentrations of substrates, products, and intermediates where there are differences in mass between them. (kent.ac.uk)

Breakdown1

• There is no biochemical breakdown of the substrate during or after enzyme treatment, and there are no residuals of the substrate in the sample retrieved from a CytoSoft® plate. (cellsystems.eu)

Covalent1

• Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. (nih.gov)

Subunit1

• The process is reversed by the alpha subunit, which hydrolyses GTP to GDP followed by reformation of the Gα i (GDP)βγ complex. (elifesciences.org)

Free enzyme2

• In this way we were able to measure the kinetics of substrate depletion, product formation, and changes in both free enzyme and acyl-enzyme intermediate concentration in the approach to steady state. (kent.ac.uk)
• No free enzyme molecules to bind with additional substrate molecules. (bankofbiology.com)

Residue1

• BETA-trypsin can be autolyzed, cleaving at the Lys - Ser residue, to produce alpha-trypsin. (sigmaaldrich.com)

Dependent1

• The concentration of trypsin necessary to dislodge cells from their substrate is dependent primarily on the cell type and the age of the culture. (sigmaaldrich.com)

Concentration1

• Incubating cells with too high a trypsin concentration for a long period can damage cell membranes and kill the cells. (sigmaaldrich.com)

Bonds1

• The fluorescence-labeled substrate was immobilized on a conductive ITO glass slide coated with gold nanoparticles/thiol-ß-cyclodextrin modified TiO2 nanowires (Au-ß-CD@TiO2 NWs) via Au-S bonds. (bvsalud.org)

Pancreatic1

• A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN . (lookformedical.com)

Actions1

• 32]PD cybridsDecreased 20S caspase-like and trypsin-like actions. (innovation-ecosystems-agora.com)

Mechanism1

• Previous studies have provided detailed insight into the molecular mechanism of action of lactacystin by demonstrating that in aqueous environments, lactacystin undergoes spontaneous hydrolysis to clasto-lactacystin dihydroxic acid and N-acetylcysteine, with the intermediacy of clasto-lactacystin-lactone [43]. (innovation-ecosystems-agora.com)

Organic1

• 2015 ). The method is preferred especially in the food and pharmaceutical industries because the hydrolysis process does not leave residual organic solvents or toxic chemicals in its products (Kim and Wijesekara 2010 ). (e-fas.org)