MadSci Network: Biochemistry |
Dear Dillon, Cool idea. Well, to start, none of those ingredients are enzymes. They are all smaller, organic molecules like detergents and some oils. There could be some minor component of the conditioner that is not listed. For example, a plant extract could be an ingredient. That would basically be some leaves ground up into liquid and added to the conditioner. If you grind up the leaves (or any plant or animal tissue) and then spin them in a centrifuge the large heavy parts, like the cell membranes and cell walls, settle to the bottom. The top will be all the enzymes and other proteins and molecules that are the water soluble fraction of the cells. If you keep this preparation under nice conditions (basically the same conditions it was used to in the cell: 150 mM salt, 25 degrees C ...) then the enzyme may stay "live." "Live" means that the enzyme still has activity. Every enzyme has a specific task in the cell. Enzymes catalyze reactions. "Catalyze" means the enzyme helps the reaction occur faster that it would normally. Like when you introduce two people at a party... those two people may have met without you, but by introducing them you have catalyzed their relationship. The past answers I've included below are about catalase. Catalase is an enzyme. It catalyzes the reaction of H2O2 to H2O + O2. Catalase will only catalyze that reaction, and no other enzyme will. Any enzyme that does cause H2O2 to become H2O will be called a catalase. This is because enzymes are named for their activity. To know if your enzyme is "alive" you need to know the enzyme's activity. Then you need an assay for that enzyme's activity. Then you need to show that when you add the enzyme to your test tube you see the activity and when you do not add the enzyme, you see no activity. For example. Catalase catalyses the H2O2 to H2O reaction. You could put H2O2 in two test tubes. (hydrogen peroxide = H2O2) You could add catalase to one tube, and nothing to the other. After a few minutes you could show that there is less hydrogen peroxide in the tube with the enzyme added. (Some chemicals have a colored reaction with H2O2 that would quantify the amnount of H202, for example. You should do a similar thing. Find out which enzymes the company claims to have in their conditioner. You should get the full name. You should also be able to get from them the assay they use to measure the activity of that enzyme. They should be able to tell you if the enzymes come from plants or animals... I would call the company. Here are some previous questions and answers to Mad Scientist that you might find helpful. You should getting a college level cell biology textbook. Look up enzyme in the index in the back. A first year biology book would be ideal for these kinds of questions. A great one I've read over and over again is The World of the Cell, by Wayne Becker. Remember when you read that book, when you read this answer and when you read any informative texts... read them over several times! I am giving you a lot of information, so does that college book. No one can get it all the first time. Read what you can and then go back and read it again. Good luck. Enzymes are cool and interesting things! They are not really "alive" but we would not be without them! See ya, Melanie Date: Sun Jul 19 17:46:05 1998 Posted By: Eric Maass, Operations Manager, semiconductors / communication products Area of science: Biochemistry ID: 898099328.Bc Message: Re: How does the concentration of hydrogen peroxide affect the reaction... Date: Sun Jul 19 17:46:05 1998 Posted By: Eric Maass, Operations Manager, semiconductors / communication products Area of science: Biochemistry ID: 898099328.Bc Message: Hello, Edgella -- your question took me back to my master's thesis (I worked on developing a glucose sensor, involving glucose oxidase and catalase)......anyway, to answer your question: The rate of the catalase reaction follows one of the general equations for enzyme-catalyzed reactions, the Michaelis-Menten equation. The rate of the catalase reaction with hydrogen peroxide would be: reaction rate V = Vmax x [Concentration of hydrogen peroxide] ------------------------------------------- Km + [Concentration of hydrogen peroxide] Vmax is the maximum reaction rate. Km is the Michaelis-Menten constant, and for catalase, Km = 25mM (25 millimoles/liter). Basically, the Michaelis-Menten equation reflects the fact that the reaction rates for enzymic reactions saturate -- that is, they reach a maximum reaction rate (Vmax), and stay at that maximum reaction rate regardless of how much additional hydrogen peroxide you add beyond that point. You should be able to plot what this graph should look like, for various amounts of hydrogen peroxide -- hopefully, the time that the disc takes to rise from the bottom of a beaker full of various concentrations of hydrogen peroxide should correspond to the reaction time, and therefore with the reaction rates. Good luck! And happy experimenting! Date: Wed Dec 2 17:20:23 1998 Posted By: Homero Rey, Sr. Application Scientist Area of science: General Biology ID: 912549344.Gb Message: The following paragraph is from an enzyme web site (http://www.facstaff.bucknell.edu/toner/gb/lab121/labs34.html) but it explains the relationship between enzyme activity and temperature very well: --------------------------------------------------------------------------- All chemical reactions speed up as temperature is raised. As the temperature increases, more molecules have enough kinetic energy to undergo the reaction. Since enzymes are catalysts for chemical reactions, enzyme reactions also tend to proceed faster with increasing temperature. However, if the temperature of an enzyme-catalyzed reaction is raised still further, an optimum is reached: above this point, the kinetic energy of the enzyme and water molecules is so great that the structure of the enzyme molecules starts to be disrupted. The positive effect of speeding up the reaction is now more than offset by the negative effect of denaturing more and more enzyme molecules. Many proteins are denatured by temperatures around 40-50deg.C, but some are still active at 70-80deg.C, and a few even withstand being boiled. --------------------------------------------------------------------------- Different enzymes have different optimum temperatures, depending on the organism and environment they have evolved in. The same enzyme can also have different optimum temperatures depending on it's source. As an example, I found the following reference for a plant catalase that has an optimum temperature of 40 deg. C and an operating range of 0-50 deg. C. --------------------------------------------------------------------------- TITLE: One-step purification and properties of catalase from leaves of Zantedeschia aethiopica. AUTHORS: Trindade H; Karmali A; Pais MS AUTHOR AFFILIATION: Falcudade de Ciencias de Lisboa, Departamento de Biologica Vegetal, Lisbon, Portugal. SOURCE: Biochimie 1988 Dec;70(12):1759-64 ABSTRACT: Catalase (E.C 1.11.1.6) was purified from leaves of Zandedeschia aethiopica to apparent hmogeneity by a one-step hydrophobic interaction chromatography on a phenyl Sepharose CL-4B column. The purified enzyme preparation was obtained with a final recovery of enzyme activity of about 61% and a specific activity of 146 U/mg protein. The purified enzyme ran as a single protein band when analyzed both by native PAGE and SDS-PAGE corresponding to an Mr of 220,000 Da, which consists of 4 subunits with identical Mr of 54,000 Da. The pI of purified enzyme was found to be 5.2 by isoelectric focusing on ultrathin polyacrylamide gels. The purified catalase has an optimum temperature of activity at 40 degrees C, whereas it is stable between 0 degrees and 50 degrees C. As regards pH, the enzyme has an optimum activity at pH 7.0 and it is stable in the range pH 6-8. The absorption spectrum of the purified enzyme exhibited 2 peaks at 280 nm and 405 nm. CAS REGISTRY NUMBERS: EC 1.11.1.6 (Catalase) --------------------------------------------------------------------------- So there is no single answer to your question! Depending on the particular catalase you're interested in, you will find different optimum temperatures. Hope this helps!
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