Why is Katals used in Enzyme kinetics & what is the best way to use it?
551973
TO CAUSE THE CHANGE CHEMICAL REACTION
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Depends on the enzyme, but in general it doesn't hurt.\n\nA long time ago BSA was always used before they found out that some enzymes work equally well without it.\n\nI am not aware of any case that BSA inhibited the reaction (at least at the usual concentration), so I always add it.
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The activity of an enzyme is tested by measuring how quickly it degrades the substrate or how quickly product is formed in an enzyme-catalyzed reaction.  This can be measured using spectrophotometry.\n\nHowever, you cannot compare these activities in samples with different protein concetrations because the increased enzyme activity may only be due to the fact that there are more enzymes contained in the sample.  Therefore, you divide the activity by the total amount of protein in the sample.  This way you can compare the activities of different samples and get an idea of how well the enzyme is functioning in different environments.\n\nAs for the calculations, just asking me to do them is giving me nightmares about my biochemsitry course I just completed.  If you already have the activity, you divide it by the total mass of protein present in the sample to get the specific activity.  If you are doing a purification procedure, the more you purify the sample, the less protein will be present and as long as the enzyme of interest remains in the assay samples the specific activity should go up.
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The method may depend upon what type of hydrolysis you performed: acid, base or enzyme.\n\nMost methods would depend upon measuring the increase of reducing sugar in the solution (these are aldehydes).  All of these methods are far more complicated than using the disappearance of the blue-black iodine-starch complex.
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The enzyme maltase that is used to reduce maltose is produced in the small intestine. That is where the breaking down of maltose occours because the pH is too low, i.e., it is too acidic in the stomach for any digestion too occur. \n\nRemember that for enzymes to work, there needs to be a specific enviornment.
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At too low a temp. an enzyme remains inactive.\n\nAt too high a temp. It is killed or ineffective or destroyed.
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Enzymes have specificity which means they work on specific substrates. if you add ions to the substrate this will change the substrate slightly enough so that the enzyme will either not work on the substrate or will slow down.
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The enzyme is a catalyst that changes the activation energy requirements of the reaction.  In some cases, an enzyme can take reactants in a lower energy state, and convert them to products in a higher energy state.\n\nSince the laws of thermodynamics dictate that things generally want to be in a lower energy state, the products can, if they can overcome the activation energy, spontaneously revert to their original state as reactants.
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I was confused by your question at first, but I think I understand if you're currently studying kinetics.\n\nThe rate of a reaction can be expressed in a rate law such as: \n Rate = k[concentration]^n.\nIn that equation, k is the rate constant and n is order of the reaction.  A second order rate law would have the form: \nRate = k[ ]^2.   \n\nAlthough they're less talked about in general chemistry, a reaction order could be negative.  (This just would mean you'd have a negative value for n.)  For example, a rate law where n = -1 with respect to oxygen would look like:\n\nRate = k [O2]^-1 = k / [O2]\n\nTo try to verify this experimentally, you would need a method for monitoring the concentration of the oxygen during the reaction (or a different method for measuring it indirectly).  If you had a set of data points for how the concentration of O2 changes with time, you could make a graph with time on the x axis and the concentration of O2 SQUARED on the y axis.  If this graph was of a straight line, that would be experimental evidence that the order of the rate law with respect to O2 is indeed -1.
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An enzyme is a protein that catalyzes, or speeds up, a chemical reaction.\nEnzymes are essential to sustain life because most chemical reactions in biological cells would occur too slowly, or would lead to different products without enzymes\n\nLike all catalysts, enzymes work by providing an alternate pathway of lower activation energy of a reaction, thus allowing the reaction to proceed much faster. Enzymes may speed up reactions by a factor of many millions. An enzyme, like any catalyst, remains unaltered by the completed reaction and can therefore continue to function. Because enzymes do not affect the relative energy between the products and reagents, they do not affect equilibrium of a reaction.
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As no one else has had a go, i will. \n\nCellulase should produce glucose, so you are needing a method to analyse the amount of glucose formed. \n\nIf you have access to a blood glucose monitor, this would be the simplest way. Otherwise, the reaction between glucose and Benedicts solution is quantitative, and you could weigh the amount of Cu2O formed.
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good link below\n\nhttp://en.wikipedia.org/wiki/Kinetic_theory
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here're some informative links http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/E/Enzymes.html , http://en.wikipedia.org/wiki/Enzyme\n\nhope this helps.
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Effect of enzyme on reaction
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B, its specific shape allows specific substrates to bind to the enzyme, thus catalyzing the reaction. If the enzyme DIDN'T have the specific shape, then the substrate would have to take a longer time to break their own bonds themselves.
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That all depends on the enzyme. It could denature a protein involved, making the enzyme useless, or it could speed up the enzyme's activity.
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An enzyme is a protein that catalyzes, or speeds up, a chemical reaction. The word comes from the Greek ένζυμο, énsymo, which comes from én ("at" or "in") and simo ("leaven" or "yeast"). Certain RNAs also have catalytic activity, but to differentiate them from protein enzymes, they are referred to as RNA enzymes or ribozymes.\n\nEnzymes are essential to sustain life because most chemical reactions in biological cells would occur too slowly, or would lead to different products without enzymes. A malfunction (mutation, overproduction, underproduction or deletion) of a single critical enzyme can lead to a severe disease. For example, the most common type of phenylketonuria is caused by a single amino acid mutation in the enzyme phenylalanine hydroxylase, which catalyzes the first step in the degradation of phenylalanine. The resulting build-up of phenylalanine and related products can lead to mental retardation if the disease is untreated.\n\nLike all catalysts, enzymes work by providing an alternate pathway of lower activation energy of a reaction, thus allowing the reaction to proceed much faster. Enzymes may speed up reactions by a factor of many millions. An enzyme, like any catalyst, remains unaltered by the completed reaction and can therefore continue to function. Because enzymes do not affect the relative energy between the products and reagents, they do not affect equilibrium of a reaction. However, the advantage of enzymes compared to most other catalysts is their sterio-, regio- and chemoselectivity and specificity.\n\nEnzyme activity can be affected by other molecules. Inhibitors are naturally occurring or synthetic molecules that decrease or abolish enzyme activity; activators are molecules that increase activity. Some irreversible inhibitors bind enzymes very tightly, effectively inactivating them. Many drugs and poisons act by inhibiting enzymes. Aspirin inhibits the COX-1 and COX-2 enzymes that produce the inflammation messenger prostaglandin, thus suppressing pain and inflammation. The poison cyanide inhibits cytochrome c oxidase, which effectively blocks cellular respiration.\n\nWhile all enzymes have a biological role, some enzymes are used commercially for other purposes. Many household cleaners use enzymes to speed up chemical reactions ( e.g., breaking down protein or starch stains in clothes).\n\nMore than 5,000 enzymes are known. Typically the suffix -ase is added to the name of the substrate (e.g., lactase is the enzyme that catalyzes the cleavage of lactose) or the type of reaction (e.g., DNA polymerase catalyzes the formation of DNA polymers). However, this is not always the case, especially when enzymes modify multiple substrates. For this reason Enzyme Commission or EC numbers are used to classify enzymes based on the reactions they catalyze. Even this is not a perfect solution, as enzymes from different species or even very similar enzymes in the same species may have identical EC numbers.\nIn enzymes, as with other proteins, function is determined by structure. An enzyme can be:\n\n    * A monomeric protein, i.e., containing only one polypeptide chain, typically one hundred or more amino acids; or\n    * an oligomeric protein consisting of several polypeptide chains, different or identical, that act together as a unit.\n\nAs with any protein, each monomer is actually produced as a long, linear chain of amino acids, which folds in a particular fashion to produce a three-dimensional product. Individual monomers may then combine via non-covalent interactions to form a multimeric protein. Many enzymes can be unfolded or inactivated by heating, which destroys the three-dimensional structure of the protein.\n\nhttp://en.wikipedia.org/wiki/Enzyme#3D_Structure