5 Examples of Where Enzymes Are Used in Industry and Medicine ?

Uses Of Enzymes In Medicine

1. Will the sudden stopping of blood pressure meds cause the elevation of heart enzymes?

If you are having side effects from your blood pressure meds, call your doctor. If you can not afford the prescription, call your doctor. Do not just quit

2. what is the affect of ph in enzymes?

Enzymes can only work within a narrow range of temperature, pH, and salt concentration. For example, the enzyme peptase in the stomach only works in a pH around 2. When the pH of a solution goes beyond that of an enzyme's range, the enzyme can denature. When an enzyme denatures, its shape changes. It's hydrogen bonds (which hold the enzyme's shape together) break and the enzyme unfolds. Because of this change in the shape of the enzyme, the substrate is no longer able to bind to the enzyme. The shape of the active site of the enzyme and the shape of the substrate no longer correspond to each other. A denatured enzyme is no longer to catalyze the reaction. Your answer: pH of a solution must be within the enzyme's range in order for the enzyme to function.

3. Enzymes At Work! Please help!?

(a) Pepsin works best at pH 2. (b) pH 2 is acidic. Our stomach has an acidic environment Pepsin to work in; breaking proteins down to polypeptides. (c) Salivia is generally neutral, which is pH 7. This is why starch is broken down first in our mouths, which a neutral environment. Salivary amylase works well too in pH 8, a slightly alkaline environment, which is in a small intestine. Salivary amylase does not work well in an acidic environment, which is a stomach. Though salivary amylase can work well in pH 6, the gastric juices in the stomach has a very acidic pH 2. As shown in the graph, salivary amylase cannot work below pH 5.

4. Can a phospholipid form on its own from molecules at scratch with no help (such as enzymes or external influence)?

Very good question. Nobody knows but I guess that the answer is yes. In a pool of mixed chemicals including lipid (-like) compounds drying out on a phosphate-rich rock like apatite: yes, why not? highly likely

5. I'm a vegetarian and recently read about enzymes and rennet that are put it into cheese?

The definitions thus far are excellent. I've also noticed that many US made cheeses use animal rennet less often than imported cheeses. I purchase a ton of Horizon and Tillamook cheeses and always read labels before I buy anything different.

6. What to do with algae from fish ponds?

Well getting rid of algae is very hard to do when outside. There is product called Bio Restoration. here is how its used. Use a combination of liquid products called Bio-Restoration 1 and 2. This non-toxic duo rids ponds of all unwelcome growth, without harming fish. Pour Bio-Restoration 1 into the pond to stop the process of photosynthesis. All algae present in the pond will fall and die as the pond water turns a lilac color. 2 Add Bio-Restoration 2 to the pond and watch the microorganisms and enzymes break down the algae. The application of the second product also clears away the lilac color and restores the natural blue of the pond water. 3 Change the pond water regularly to inhibit nutrient production. If algae have nothing to feed on, they can not survive. A good filter works also, but not as well as changing the water. 4 Add 1 lb. of non-iodized salt to the pond every 12 hours up to three times. As the algae floats to the surface, it must be skimmed off. 5 Place an ultra sonic device into the pond to safely kill algae. The vibrations break down algae cells causing them to die without killing other plants or fish. Hope this helps. its a method i have heard of before and it works fairly well. as for the algae infested water i would say throw it out onto some gravel of the drive way or off into the woods. Dan B

7. Given the fact that many enzymes and blood proteins are conjugated proteins, what role might the prosthetic groups of such proteins play in the life of the cell?

From biological models, it appears that prosthetic groups of proteins often function in redox reactions (or oxidation-reduction reactions), where electrons transfer takes place.A common model is the heme group of hemoproteins. As a prosthetic group, heme contains an iron atom (Fe) which is the site of electron transfer. Analogously the photosynthetic molecule chlorophyll has a functional group classed as a chlorin with a magnesium atom (Mg) at its core of pyrrole-like subunits which are actually related to the porphyrin protein subunits of heme, found in both plants and animals.Heme and chlorophyll are considered metalloproteins, utilizing metal ion cofactors.The metal ion in heme and chlorophyll is centered within a structure consisting of multiple rings. The short lines inside the rings designate symbolically that the molecule is planar and aromatic and therefore, is a conjugated system.Image of benzene to illustrate aromaticity:In terms of the electronic nature of the molecule, aromaticity describes a conjugated system often made of alternating single and double bonds in a ring. This configuration allows for the electrons in the molecule's pi system to be delocalized around the ring, increasing the molecule's stability. The molecule cannot be represented by one structure, but rather a resonance hybrid of different structures, such as with the two resonance structures of benzene.The conjugated system surrounding the metal ion:stabilizes the molecule in such a way that a redox reaction (or O2 binding to heme) does not significantly change the reactivity of functional groups at other sites around the system.the ketone groups are actually part of the conjugation system of the molecule, and therefore to the stabilitystabilizes the molecule in such a way that the binding of oxygen does not lead to structural or geometric changes in the molecule. Prosthetic groups of proteins that do not involve metal ions can also function as cofactors, coenzymes, cytochromes, or by catalyzing reactions or by affecting the rate of enzyme kinetics. These cofactors include vitamins, like ascorbic acid and non-vitamin cofactors.Protein-derived cofactorsIn a number of enzymes, the moiety that acts as a cofactor is formed by post-translational modification of a part of the protein sequence. This often replaces the need for an external binding factor, such as a metal ion, for protein function. Potential modifications could be oxidation of aromatic residues, binding between residues, cleavage or ring-forming.These alterations are distinct from other post-translation protein modifications, such as phosphorylation, methylation, or glycosylation in that the amino acids typically acquire new functions. This increases the functionality of the protein; unmodified amino acids are typically limited to acid-base reactions, and the alteration of resides can give the protein electrophilic sites or the ability to stabilize free radicals.Examples of cofactor production include tryptophan tryptophylquinone (TTQ), derived from two tryptophan side chains,and 4-methylidene-imidazole-5-one (MIO), derived from an Ala-Ser-Gly motif.Characterization of protein-derived cofactors is conducted using X-ray crystallography and mass spectroscopy; structural data is necessary because sequencing does not readily identify the altered sites. Post-translational modification of the protein (after the polypeptide chain of the protein has been synthesized through translation) endows a protein with cofactor catalytic function but without the need for a metal ion binding factor such as Fe or Mg, in the case of metalloproteins.Thanks for readingGiven the fact that many enzymes and blood proteins are conjugated proteins, what role might the prosthetic groups of such proteins play in the life of the cell?

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