What is the optimum temperature for the enzyme amylase?
Q. What is the optimum temperature for the enzyme amylase*? *Amylase- Amylase is an enzyme that converts starch by hydrolysis into sugars.
Asked by pupsgirly1023 - Sun Nov 30 19:16:30 2008 - - 1 Answers - 0 Comments
A. 40 degress
Answered by joe.tiplady - Sun Nov 30 19:24:20 2008
Q. What is the optimum temperature for the enzyme amylase*? *Amylase- Amylase is an enzyme that converts starch by hydrolysis into sugars.
Asked by pupsgirly1023 - Sun Nov 30 19:16:30 2008 - - 1 Answers - 0 Comments
A. 40 degress
Answered by joe.tiplady - Sun Nov 30 19:24:20 2008
What affect does amylase have on starch?
Q. I'm designing an experiment where I mix amylase and starch. I believe that maltose is produced. If I were to mix these two at a normal conditions, would the mass of the combination be lower than original because of the amylase? If I mixed them at a high temp, I would assume the enzyme would denature and the reaction would not continue. Is this true? Thanks I agree, doing an Iodine test would be perfect, but I am supposed to design a quantitative experiment.
Asked by t3harchit3ct - Wed Oct 22 20:59:59 2008 - - 1 Answers - 0 Comments
A. actually a much more visible way to do the experiment is to add startch to ater without enzyme and variuos amounts of enzyme ( and/or different incubation times ).The add a KI/I2 solution..the unreacted starch will react with the KI/I2 to produce a deep blue color...those reaction flasks having less starch or very little starch will produce much weaker color.
Answered by Merlin's Feline - Wed Oct 22 21:27:15 2008
Q. I'm designing an experiment where I mix amylase and starch. I believe that maltose is produced. If I were to mix these two at a normal conditions, would the mass of the combination be lower than original because of the amylase? If I mixed them at a high temp, I would assume the enzyme would denature and the reaction would not continue. Is this true? Thanks I agree, doing an Iodine test would be perfect, but I am supposed to design a quantitative experiment.
Asked by t3harchit3ct - Wed Oct 22 20:59:59 2008 - - 1 Answers - 0 Comments
A. actually a much more visible way to do the experiment is to add startch to ater without enzyme and variuos amounts of enzyme ( and/or different incubation times ).The add a KI/I2 solution..the unreacted starch will react with the KI/I2 to produce a deep blue color...those reaction flasks having less starch or very little starch will produce much weaker color.
Answered by Merlin's Feline - Wed Oct 22 21:27:15 2008
Why does amylase stop working in the acidic conditions in the stomach?
Q. Amylase is an enzyme which speeds up the digestion of starch. Amylase is produced by the salivary glands. Why does amylase stop working in the acidic conditions in the stomach? As food passes from the stomach into the small intestine, a different digestive juice is mixed with the food. What type of substance is this digestive juice?
Asked by Cassie Baker - Mon May 5 17:36:48 2008 - - 1 Answers - 0 Comments
A. Every enzyme has it own pH optimum. The amylase in the saliva has a pH optimum of 5.6. In the stomach, the pH is 1-2. So amylase stops working in the stomach. In the small intestine, a mixture of pancreatic enzymes work there: trypsin, chymotrypsin, lipase, amylase, etc.
Answered by OKIM IM - Mon May 5 17:44:08 2008
Q. Amylase is an enzyme which speeds up the digestion of starch. Amylase is produced by the salivary glands. Why does amylase stop working in the acidic conditions in the stomach? As food passes from the stomach into the small intestine, a different digestive juice is mixed with the food. What type of substance is this digestive juice?
Asked by Cassie Baker - Mon May 5 17:36:48 2008 - - 1 Answers - 0 Comments
A. Every enzyme has it own pH optimum. The amylase in the saliva has a pH optimum of 5.6. In the stomach, the pH is 1-2. So amylase stops working in the stomach. In the small intestine, a mixture of pancreatic enzymes work there: trypsin, chymotrypsin, lipase, amylase, etc.
Answered by OKIM IM - Mon May 5 17:44:08 2008
Why is amylase important in the human bodey for it to break starch to maltose?
Q. What Temperature and pH do you believe that AMylase would worrk most effective in and why?
Asked by sunshine29 - Fri Feb 22 12:54:05 2008 - - 2 Answers - 0 Comments
A. We need amylase in order to break down starches into something we can make use of, ie maltose. Think about your question, where is amylase used? Our mouth! Body temp being 98.6F or 37C The pH f Saliva is between 6.5 - 7 Which is pretty much neutral. Those will be the optimal conditions for amylase to work. The site located below reaffirms my answer
Answered by breeder_18 - Fri Feb 22 13:00:49 2008
Q. What Temperature and pH do you believe that AMylase would worrk most effective in and why?
Asked by sunshine29 - Fri Feb 22 12:54:05 2008 - - 2 Answers - 0 Comments
A. We need amylase in order to break down starches into something we can make use of, ie maltose. Think about your question, where is amylase used? Our mouth! Body temp being 98.6F or 37C The pH f Saliva is between 6.5 - 7 Which is pretty much neutral. Those will be the optimal conditions for amylase to work. The site located below reaffirms my answer
Answered by breeder_18 - Fri Feb 22 13:00:49 2008
How does the absence of amylase not cause a disease?
Q. I do not understand that concept and have repeatedly read the sections on amylase from my textbook. Could anyone please explain? Thank you in advance.
Asked by Brandon - Sun Sep 13 21:23:40 2009 - - 1 Answers - 0 Comments
A. Amylase helps digest carbohydrates. Absolute absence can result in malabsorption syndromes.
Answered by finaldx - Sun Sep 13 21:51:54 2009
Q. I do not understand that concept and have repeatedly read the sections on amylase from my textbook. Could anyone please explain? Thank you in advance.
Asked by Brandon - Sun Sep 13 21:23:40 2009 - - 1 Answers - 0 Comments
A. Amylase helps digest carbohydrates. Absolute absence can result in malabsorption syndromes.
Answered by finaldx - Sun Sep 13 21:51:54 2009
How do i search for a primary article for my Amylase enzyme lab report?
Q. Hi-i need to write a lab report for the enzyme, amylase reacting with Starch to form maltose. I am searching for a primary article for this lab report but i am a little confused. What kind of article should i use and how can i search to find a good article?
Asked by Mgen - Tue Oct 13 02:15:54 2009 - - 2 Answers - 0 Comments
A. For this you will want to find some primary research, so the best place to look is your school or college library. They will probably have a periodical search engine where you can find the specific article you are looking for. You could try the American Chemical Society, or try looking online for some peer-reviewed journals and searching for your article that way...Good luck! Finding a good, reliable article is almost always the hardest part of the assignment!! :)
Answered by 08H - Tue Oct 13 02:25:36 2009
Q. Hi-i need to write a lab report for the enzyme, amylase reacting with Starch to form maltose. I am searching for a primary article for this lab report but i am a little confused. What kind of article should i use and how can i search to find a good article?
Asked by Mgen - Tue Oct 13 02:15:54 2009 - - 2 Answers - 0 Comments
A. For this you will want to find some primary research, so the best place to look is your school or college library. They will probably have a periodical search engine where you can find the specific article you are looking for. You could try the American Chemical Society, or try looking online for some peer-reviewed journals and searching for your article that way...Good luck! Finding a good, reliable article is almost always the hardest part of the assignment!! :)
Answered by 08H - Tue Oct 13 02:25:36 2009
What happens when you forget to add starch to amylase?
Q. After you treat amylase with heat or change its pH level, but forget to add starch to the solution before beginning the timing assay, what is the result?
Asked by hinata_hater h - Mon Mar 1 22:13:23 2010 - - 1 Answers - 0 Comments
A. a big fat nothing. without it's substrate, the amylase cannot do it's work. You might get some signal, but that is just "background noise" of the assay,
Answered by Robert - Mon Mar 1 22:17:56 2010
Q. After you treat amylase with heat or change its pH level, but forget to add starch to the solution before beginning the timing assay, what is the result?
Asked by hinata_hater h - Mon Mar 1 22:13:23 2010 - - 1 Answers - 0 Comments
A. a big fat nothing. without it's substrate, the amylase cannot do it's work. You might get some signal, but that is just "background noise" of the assay,
Answered by Robert - Mon Mar 1 22:17:56 2010
What is the optimum temperature for amylase?
Q. What is the temperature optimum for amylase? What is the significance of this temperature? Does this temperature tell you anything about advantage of warm blooded mammals over "cold-blooded" lizards?
Asked by Th90 - Fri Oct 17 17:53:41 2008 - - 1 Answers - 0 Comments
A. Optimal temperatures of amylases range from 60 C. to 75 C., or about 140 F. to 177 F. These temperatures are much higher than the survivable body temperatures of any mammal or reptile. Nevertheless, such high optimums provide an advantage to homeothermic (warm-blooded) mammals, since they are able to digest food more rapidly than poikilothermic (cold-blooded) reptiles, and are thus able to maintain a higher rate of metabolic activity.
Answered by LAlawMedMBA - Thu Oct 23 09:36:54 2008
Q. What is the temperature optimum for amylase? What is the significance of this temperature? Does this temperature tell you anything about advantage of warm blooded mammals over "cold-blooded" lizards?
Asked by Th90 - Fri Oct 17 17:53:41 2008 - - 1 Answers - 0 Comments
A. Optimal temperatures of amylases range from 60 C. to 75 C., or about 140 F. to 177 F. These temperatures are much higher than the survivable body temperatures of any mammal or reptile. Nevertheless, such high optimums provide an advantage to homeothermic (warm-blooded) mammals, since they are able to digest food more rapidly than poikilothermic (cold-blooded) reptiles, and are thus able to maintain a higher rate of metabolic activity.
Answered by LAlawMedMBA - Thu Oct 23 09:36:54 2008
how can i investigate the effect of starch concentration on a fixed amylase concentration?
Q. Iw as thinking of using starch concentrations of 1C, 2C, 3C, 4C, 5C and testing it to 1C amylase. And using iodine to test the colour. But how do i collect the result sin order to make a graph. This mean collecting valid data to understand what is happening. Thanks you very much for this fantastic suggestion. I realy appreciate the help.
Asked by Ross - Sat Mar 28 14:58:28 2009 - - 1 Answers - 0 Comments
A. First of all, I don't know what you mean by a concentration of 1C. Concentrations are usually given in terms of molarity or percent by weight. If you mean molarity, it is unlikely you could get something like 5 M into solution. Why not do a series of dilutions by half... start with a 20 g per liter solution "Prepare a 20 g/l starch solution. Mix 20 g of soluble potato starch in approx. 50 ml of cold water. While stirring, add the slurry to approx. 900 ml of gently boiling water in a large beaker. Mix well and cool the gelatinized starch solution to room temperature. Add more water to bring the total volume to 1 liter. Put a few drops of the starch solution on a glass plate. Add 1 drop of the iodine reagent and see that a deep blue… [cont.]
Answered by kt - Sat Mar 28 15:10:06 2009
Q. Iw as thinking of using starch concentrations of 1C, 2C, 3C, 4C, 5C and testing it to 1C amylase. And using iodine to test the colour. But how do i collect the result sin order to make a graph. This mean collecting valid data to understand what is happening. Thanks you very much for this fantastic suggestion. I realy appreciate the help.
Asked by Ross - Sat Mar 28 14:58:28 2009 - - 1 Answers - 0 Comments
A. First of all, I don't know what you mean by a concentration of 1C. Concentrations are usually given in terms of molarity or percent by weight. If you mean molarity, it is unlikely you could get something like 5 M into solution. Why not do a series of dilutions by half... start with a 20 g per liter solution "Prepare a 20 g/l starch solution. Mix 20 g of soluble potato starch in approx. 50 ml of cold water. While stirring, add the slurry to approx. 900 ml of gently boiling water in a large beaker. Mix well and cool the gelatinized starch solution to room temperature. Add more water to bring the total volume to 1 liter. Put a few drops of the starch solution on a glass plate. Add 1 drop of the iodine reagent and see that a deep blue… [cont.]
Answered by kt - Sat Mar 28 15:10:06 2009
Which cells of the human body is the genetic information for making salivary amylase?
Q. In which cells of the human body is the genetic information for making salivary amylase transcribed and translated?
Asked by Maggie Nemoy - Sun Jan 10 22:19:21 2010 - - 2 Answers - 0 Comments
A. Hmm. Maybe in the endothelial cells of your salivary glands? m
Answered by im - Mon Jan 11 00:14:20 2010
Q. In which cells of the human body is the genetic information for making salivary amylase transcribed and translated?
Asked by Maggie Nemoy - Sun Jan 10 22:19:21 2010 - - 2 Answers - 0 Comments
A. Hmm. Maybe in the endothelial cells of your salivary glands? m
Answered by im - Mon Jan 11 00:14:20 2010
time taken for amylase to denature under acidic conditions?
Q. My A2 Edexcel biology coursework is to investigate the time taken for amylase to denature under acidic conditions. I can't find much on the web so need some help as to what I put for my hypothesis/biological knowledge. Any help would be greatly appreciated. Thanks very much!
Asked by applejuice - Tue Sep 30 00:50:18 2008 - - 1 Answers - 0 Comments
A. One time in the lab i was amylaseing acidic acid in a flask on a bunsen burnner when the C4 kicked in out of nowhere..but luckily there was some H7C20 in the room and we quickly acidicity the acid problem like pros.
Answered by Tatties M - Tue Sep 30 00:54:01 2008
Q. My A2 Edexcel biology coursework is to investigate the time taken for amylase to denature under acidic conditions. I can't find much on the web so need some help as to what I put for my hypothesis/biological knowledge. Any help would be greatly appreciated. Thanks very much!
Asked by applejuice - Tue Sep 30 00:50:18 2008 - - 1 Answers - 0 Comments
A. One time in the lab i was amylaseing acidic acid in a flask on a bunsen burnner when the C4 kicked in out of nowhere..but luckily there was some H7C20 in the room and we quickly acidicity the acid problem like pros.
Answered by Tatties M - Tue Sep 30 00:54:01 2008
How do the two forms of amylase differ in their actions?
Q. alpha-amylase and beta-amylase how do they both differ from eachother in their actions?
Asked by Joyce - Wed Jan 24 14:52:14 2007 - - 2 Answers - 0 Comments
A. alpha-amylase hydrolyzes saccharide bonds, which are those pointed at by the arrows in the figure, above. So imagine, a bunch of alpha-amylases randomly bouncing around (Brownian motion!) in among some extremely long starch molecules. Whenever a "mouth" - the enzymatic or active site - bounces against a saccharide bond, "snip", and the bond is broken (hydrolyzed as a water molecule is added "across" the saccharide bond). With that bond broken, the whole starch molecule is now in two pieces. The more "bites," the more and smaller pieces. To help you "identify" with alpha-amylase, you will be happy to know that most of you have lots of it in your saliva. The beta-amylase PacMan is very picky and can only "chew" on the ends of a starch… [cont.]
Answered by Angel_89 - Wed Jan 24 15:18:02 2007
Q. alpha-amylase and beta-amylase how do they both differ from eachother in their actions?
Asked by Joyce - Wed Jan 24 14:52:14 2007 - - 2 Answers - 0 Comments
A. alpha-amylase hydrolyzes saccharide bonds, which are those pointed at by the arrows in the figure, above. So imagine, a bunch of alpha-amylases randomly bouncing around (Brownian motion!) in among some extremely long starch molecules. Whenever a "mouth" - the enzymatic or active site - bounces against a saccharide bond, "snip", and the bond is broken (hydrolyzed as a water molecule is added "across" the saccharide bond). With that bond broken, the whole starch molecule is now in two pieces. The more "bites," the more and smaller pieces. To help you "identify" with alpha-amylase, you will be happy to know that most of you have lots of it in your saliva. The beta-amylase PacMan is very picky and can only "chew" on the ends of a starch… [cont.]
Answered by Angel_89 - Wed Jan 24 15:18:02 2007
Is it possible to separate Amylase from Starch after mixing them, if so, how do you do it?
Q. After Amylase breaks apart the Starch molecules into Glucose molecules, how do you take Amylase out again and use it on another group of Starch? I need to design an experiment to see if enzymes are not used up after breaking apart a substrate, and to do this I believe I need to know how to take Amylase out of the glucose concentration. Thank you.
Asked by Please Help Me - Tue Jan 13 19:05:27 2009 - - 1 Answers - 0 Comments
A. It will be possible, but I'm not 100% sure on how (I'm a process chemist not biochemist). Three general ways to recover a reagent / product from a mixture: Distillation (impractical for this case). Precitation of the glucose (difficult) or enzyme by changing the temperature, pH, of solvent properties (add anti solvent or salt). Extraction one or the other into a non miscible solvent. I would probably go with precipitation and filtration as a first attempt. You just need to figure out how to make the Amylase insoluble in water. Regards N
Answered by lothian1234 - Tue Jan 13 19:21:16 2009
Q. After Amylase breaks apart the Starch molecules into Glucose molecules, how do you take Amylase out again and use it on another group of Starch? I need to design an experiment to see if enzymes are not used up after breaking apart a substrate, and to do this I believe I need to know how to take Amylase out of the glucose concentration. Thank you.
Asked by Please Help Me - Tue Jan 13 19:05:27 2009 - - 1 Answers - 0 Comments
A. It will be possible, but I'm not 100% sure on how (I'm a process chemist not biochemist). Three general ways to recover a reagent / product from a mixture: Distillation (impractical for this case). Precitation of the glucose (difficult) or enzyme by changing the temperature, pH, of solvent properties (add anti solvent or salt). Extraction one or the other into a non miscible solvent. I would probably go with precipitation and filtration as a first attempt. You just need to figure out how to make the Amylase insoluble in water. Regards N
Answered by lothian1234 - Tue Jan 13 19:21:16 2009
Why do people with pancreatitis have a different amylase concentration?
Q. Why is there a difference in amylase concentration in people with pancreatitis and healthy people ?
Asked by .. - Mon Nov 23 09:42:00 2009 - - 1 Answers - 0 Comments
A. usually the pancreas excretes its amylase into the intestine, but often with pancreatitis the outlet is plugged. This results in amylase and other digestive enzymes escaping internally (don't count the inside of the gut as the insides, its the outside). Eating fatty meals or drinking alcohol stimulates the pancreas to secrete digestive enzymes. There is chronic and accute pancreatitis conditions.
Answered by AbeLincolnParty - Mon Nov 23 09:52:17 2009
Q. Why is there a difference in amylase concentration in people with pancreatitis and healthy people ?
Asked by .. - Mon Nov 23 09:42:00 2009 - - 1 Answers - 0 Comments
A. usually the pancreas excretes its amylase into the intestine, but often with pancreatitis the outlet is plugged. This results in amylase and other digestive enzymes escaping internally (don't count the inside of the gut as the insides, its the outside). Eating fatty meals or drinking alcohol stimulates the pancreas to secrete digestive enzymes. There is chronic and accute pancreatitis conditions.
Answered by AbeLincolnParty - Mon Nov 23 09:52:17 2009
What does low amylase in lab results indicate?
Q. About a year ago I had some blood work done and a ct scan done to determine if I had an appendicitis. The ct scan came back negative all I had was an irritated ovarian cyst. My blood work however had one abnormality on it. My amylase level was below normal. My doctor never ordered any follow up testing. Should he have? And what would a low level amylase indicate?
Asked by danie81 - Thu Dec 14 14:32:13 2006 - - 1 Answers - 0 Comments
A. An amylase test measures the amount of this enzyme in a sample of blood taken from a vein or in a sample of urine. Many conditions can change amylase levels. Your health professional will discuss any significant abnormal results with you in relation to your symptoms and medical history. If you have a lower than normal level, I would not be concerned. Higher than normal levels get attention. Normally, only low levels of amylase are found in the blood or urine. However, if the pancreas or salivary glands become damaged or blocked, more amylase is usually released into the blood and urine. In the blood, amylase levels rise for only a short time. In the urine, amylase may remain high for several days. If you want to be totally assured, call… [cont.]
Answered by Gino - Thu Dec 14 14:45:47 2006
Q. About a year ago I had some blood work done and a ct scan done to determine if I had an appendicitis. The ct scan came back negative all I had was an irritated ovarian cyst. My blood work however had one abnormality on it. My amylase level was below normal. My doctor never ordered any follow up testing. Should he have? And what would a low level amylase indicate?
Asked by danie81 - Thu Dec 14 14:32:13 2006 - - 1 Answers - 0 Comments
A. An amylase test measures the amount of this enzyme in a sample of blood taken from a vein or in a sample of urine. Many conditions can change amylase levels. Your health professional will discuss any significant abnormal results with you in relation to your symptoms and medical history. If you have a lower than normal level, I would not be concerned. Higher than normal levels get attention. Normally, only low levels of amylase are found in the blood or urine. However, if the pancreas or salivary glands become damaged or blocked, more amylase is usually released into the blood and urine. In the blood, amylase levels rise for only a short time. In the urine, amylase may remain high for several days. If you want to be totally assured, call… [cont.]
Answered by Gino - Thu Dec 14 14:45:47 2006
what would happen to the rate of amylase activity at 25 degrees celcius?
Q. amylase is an enzyme that aids in the digrestion of starches and has an ideal temperature range of 35 to 40 degrees celcius.
Asked by madison - Tue Oct 9 17:40:21 2007 - - 2 Answers - 0 Comments
A. The activity would slow down. When an enzyme works above its ideal temperature, it has a tendency of denaturing, at a lower temperatures, it slows down as there is less energy in the system.
Answered by Jenny H - Tue Oct 9 17:50:38 2007
Q. amylase is an enzyme that aids in the digrestion of starches and has an ideal temperature range of 35 to 40 degrees celcius.
Asked by madison - Tue Oct 9 17:40:21 2007 - - 2 Answers - 0 Comments
A. The activity would slow down. When an enzyme works above its ideal temperature, it has a tendency of denaturing, at a lower temperatures, it slows down as there is less energy in the system.
Answered by Jenny H - Tue Oct 9 17:50:38 2007
Why does the reaction catalysed by amylase occur quickly at the start and then slow down?
Q. Why does the reaction catalysed by amylase occur quickly at the start and then slow down?
Asked by Nick - Sun Jun 6 06:56:42 2010 - - 2 Answers - 0 Comments
A. reactants are being used up so less rate of reaction
Answered by hanan - Sun Jun 6 07:05:56 2010
Q. Why does the reaction catalysed by amylase occur quickly at the start and then slow down?
Asked by Nick - Sun Jun 6 06:56:42 2010 - - 2 Answers - 0 Comments
A. reactants are being used up so less rate of reaction
Answered by hanan - Sun Jun 6 07:05:56 2010
What is the difference between salivary amylase and pancreatic amylase?
Q. I don't want links from Wikipedia please... I don't understand Wikipedia... Thank you. =)
Asked by Denedy - Sat May 23 11:50:06 2009 - - 1 Answers - 0 Comments
A. Salivary amylase is secreted in the salivary gland while pancreatic amylase is secreted in the pancreas. Salivary amylase digests starch into maltose. Pancreatic amylase digests maltose into glucose.
Answered by Glory2ManU - Sat May 23 12:34:51 2009
Q. I don't want links from Wikipedia please... I don't understand Wikipedia... Thank you. =)
Asked by Denedy - Sat May 23 11:50:06 2009 - - 1 Answers - 0 Comments
A. Salivary amylase is secreted in the salivary gland while pancreatic amylase is secreted in the pancreas. Salivary amylase digests starch into maltose. Pancreatic amylase digests maltose into glucose.
Answered by Glory2ManU - Sat May 23 12:34:51 2009
Why is salivary amylase catalysed better by alkalis than acids?
Q. Please could you go into detail? I am using the starch in an agar jelly plate to be broken down.
Asked by Vicky C - Sun Apr 6 10:47:46 2008 - - 1 Answers - 0 Comments
A. Enzymes are sensitive to changes in pH. There is usually an optimum pH at which the rate of reaction is greatest. Different enzymes have different optimum pH values. For example, enzymes in the mouth eg.amylase and small intestine work best in slightly alkaline conditions but those in the stomach work best in acidic conditions. At extreme pH's, something drastic can happen. Remember that the tertiary structure of the protein is in part held together by ionic bonds. At very high or very low pH's, these bonds within the enzyme can be disrupted, and it can lose its shape. If it loses its shape, the active site will probably be lost completely and so will its activity. This is essentially the same as denaturing the protein by heating it too… [cont.]
Answered by Peter S - Sun Apr 6 11:47:06 2008
Q. Please could you go into detail? I am using the starch in an agar jelly plate to be broken down.
Asked by Vicky C - Sun Apr 6 10:47:46 2008 - - 1 Answers - 0 Comments
A. Enzymes are sensitive to changes in pH. There is usually an optimum pH at which the rate of reaction is greatest. Different enzymes have different optimum pH values. For example, enzymes in the mouth eg.amylase and small intestine work best in slightly alkaline conditions but those in the stomach work best in acidic conditions. At extreme pH's, something drastic can happen. Remember that the tertiary structure of the protein is in part held together by ionic bonds. At very high or very low pH's, these bonds within the enzyme can be disrupted, and it can lose its shape. If it loses its shape, the active site will probably be lost completely and so will its activity. This is essentially the same as denaturing the protein by heating it too… [cont.]
Answered by Peter S - Sun Apr 6 11:47:06 2008
What is the purpose of adding Na2CO3 into a mixture of alpha amylase enzyme?
Q. during the experiment to determine the optimum pH and temperature of the alpha amylase, Na2CO3 was added into the mixture of enzymes at the end of the experiment before the absorbance was measured, what is the purpose of adding the Na2CO3?
Asked by jD - Sat Aug 15 00:52:56 2009 - - 1 Answers - 0 Comments
A. Presumably you measured amylase activity by determing the amount of reducing sugar produced using Benedict's solution. This test works in alkaline solution and so that is why Na2CO3 was added.
Answered by Peter S - Sat Aug 15 06:41:57 2009
Q. during the experiment to determine the optimum pH and temperature of the alpha amylase, Na2CO3 was added into the mixture of enzymes at the end of the experiment before the absorbance was measured, what is the purpose of adding the Na2CO3?
Asked by jD - Sat Aug 15 00:52:56 2009 - - 1 Answers - 0 Comments
A. Presumably you measured amylase activity by determing the amount of reducing sugar produced using Benedict's solution. This test works in alkaline solution and so that is why Na2CO3 was added.
Answered by Peter S - Sat Aug 15 06:41:57 2009
From Yahoo Answer Search: 'amylase'
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businessweek.com
Tue, 20 Jul 2010 14:41:23 GMT+00:00
BusinessWeek Novozymes, based in Bagsvaerd, Denmark, in May filed a complaint in the US that said Danisco infringed its patent on a so-called alpha amylase enzyme used ...
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Ian Lumsden
Wed, 09 Dec 2009 11:13:00 GM
Amylase. is set in a monochrome, flickering world of grey. Throughout one is conscious of the shadows as a paper man returns to lonely home, eats meagre meal, sleeps and loses his face in the night. He was in no great shape before this, ...
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