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Biology of Copper sulphate
Q. Hello. Please can you tell me whether copper sulphate ⇦ on eBay or Amazon [affil links] is an enzyme inhibitor, or indeed if it has any affect on the rate of enzyme reactions, in particular the enzyme, catalase? Thank you
h.chichger- UK
2000
Q. Is copper sulphate a competitive or non comp. inhibitor of catalase? I am a teacher and do you have any references on line to back this up? Thanks
Lucy McCreath- Cambridge, England
2001
Q. I want to know whether copper sulphate is an inhibitor (of catalase acting upon hydrogen peroxide) and what kind of an inhibitor, a competitive or non-competitive.
NARINDER Singh- Middlesbrough, England
A. I too am looking for information but I can tell you the answers to your question ... first of all look in any text book and you will find that copper ... or any other heavy metal disrupts the tertiary bonds in enzymes and therefore alters their active sites, therefore inhibiting the enzyme.
copper sulphate is a non-competitive inhibitor since it has no structural similarity to the substrate and does not bond at the active site.
Hope I have helped a bit .., if anyone else has any info regarding rate of inhibition, etc.
Sara Jaes-Brighton, UK
A. Copper (II) sulphate is an irreversible, non-competitive inhibitor of catalase. It is important to note that CuSO4, as most transition metal compounds, is non-competitive because it is so very different to the substrate (H2O2).
Andrew Nowacki- Jersey, Channel Islands
Q. I am currently doing a piece of course work on copper sulphate and how it acts on enzymes and I have found that it does not actually act as an inhibitor on the enzyme rennin - in fact it is an activator. I also have not been able to find any useful information on activators. Any help?
Lee O'Brian- England
2001
on eBayA. Don't blame me if this is wrong, but the theory I used for last year's course work ... the copper (2+) ions in the CuS04 solution combine with the thiol groups in enzymes, breaking the disulfide bonds that give the enzyme coil its shape. This results in ripples of distortion across the molecule to the active site, which is then altered so that the substrate no longer fits into it.
Helen Carey- England
2002
A. copper sulphate is a competitive inhibitor of the enzyme catalase. Catalase contains an iron haem group located in the center of a porphyrin ring which carries out the reaction. Adding copper sulphate displaces the iron from the center of the ring, as it has a higher stability constant (K stab). Thus, the iron which catalyses the overall reaction is removed and it cannot proceed.
Neil HarrisonStudent Studying biochemistry - Carlisle, UK
Q. I am a student and I am doing my AS biology course work. I have got a question about copper sulphate. When I did the experiment of enzyme-controlled reaction with starch and amylase, I did two set, one set by adding copper sulphate to the reaction and the other one didn't. Why the concentration of starch left is higher when I did not use copper sulphate than I use that? Suppose that copper sulphate is an inhibitor.
Michelle [last name deleted for privacy by Editor]- Madrid, Spain
2003
Q. I am an a-level student in the UK. For my biology course work this year I experimented with copper sulphate as an inhibitor on liver catalase. *cough* I had pretty bizarre results, though. I experimented using different conc.s of copper sulphate, soaked pieces of liver in them, chucked hydrogen peroxide all over them and measured the oxygen that came out the other end. You'd think that the lowest concentration of copper sulphate would have the least inhibition, and vice versa, eh? but no...it didn't play fair like that. I used concentrations 2%, 1%, .75%, .5% and .25% copper sulphate by volume: the first four concentrations followed the expected pattern but my .25% concentration always, always inhibited more than the .5%, usually more than the .75%, and in one case it even inhibited as much as the 1% did! I'm at a loss to explain this. Anyone with interesting ideas can reply to me.
Benjamin Denton- Warminster, Wilts, UK
A. Those of you doing A-level biology and asking questions: The explanation about iron given above seems to describe a non-competitive enzyme action despite the first sentence. a competitive enzyme somehow blocks the active site with a molecule of similar structure to the intended substrate. The action described on the heam group is a non-competitive action which actually changes the structure of the protein. This is not competition. Interesting side note for this experiment to further confuse you: Copper ions actually slightly catalyze the hydrogen peroxide reaction the CuS04 is supposed to inhibit. :)
Richard Marsh- Oxford, UK
Q. After conducting "An Investigation into the effect of varying concentrations of copper sulphate on the germination of cress seeds" I found that from using, 0.0002, 0.002, 0.02 and 0.2 concentrations, the mean length of radical produced after 3 days was progressively lower as concentration increased. All other relevant conditions kept constant.
This leads me to believe that copper sulphate is a noncompetitive inhibitor. I am interested to find out the chemistry behind this and have read the comments of Helen Darey above. Could anyone tell me why the positive copper ions are attracted to the thiol groups involved in disulfide bonds in the enzyme?
Barney HarrisStudent - Shropshire, UK
2003
Thank you to all of the above I am an a-level student studying AS biology and thanks to you all I am sure I will get full marks in my planning section.
is Cu2+ a permanent non-competitive inhibitor of catalase? Apparently need to know, though I don't know why ...
Kattie Lou [last name deleted for privacy by Editor]student - St Saviour, Jersey, UK
2004
A. Hydrogen peroxide is used as a substrate to catalyze, but, when H2O2 is entered and reacts with metal ions it can start to decompose under the pressure.
Adam Tomlinson- Northants, UK
Q. Would it be possible to answer my enquiry, I have scanned the internet and spent hours in the library with little answers. I am researching Enzymes and their particular effect in conjunction with inhibition. My investigation is to study the effect of CuSO4 on pectinase and the substrate of apples. I believe that CuSO4 in a reversible/competitive inhibitor to catalase, or amylase by studying your posted enquiries. Thank for your sharing of knowledge!
Emily Harrisartist/student - London, Essex, UK
2004
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Q. Hi there. I am doing a biology lab in which I am mixing hydrogen peroxide with catalase, and copper is being added. Our results showed that the reaction rate slowed down. Is that justified? Is copper acting as a competitive or non competitive inhibitor? And why I could not determine if I was right or wrong in my results? ASAP, thanks a lot.
nina [last name deleted for privacy by Editor]student - brampton, Ontario, Canada
Q. I am currently doing a piece of course work on the effect of CuSO4 on Catalase during the decomposition of H2O2. Qs. Is CuSO4 an inhibitor? Is it competitive or non-competitive? Is it reversible or irreversible? Why does it inhibit the reaction?
Syed Nadir Ahmed- London, UK
Q. I am doing course work into the effect of different concentrations of copper sulphate on the germination of cress seeds but we have to say something about copper tolerance can anyone help as I don't know anything about this?
Megan W.- Shresbury, Shropshire, UK
Q. Hi, I'm doing an A level chemistry investigation, and was just wondering if anyone can help! If the Cu2+ ions in copper sulphate inhibit catalase (I have found this to be true for many other d-block sulphates such as zinc sulphate, iron sulphate and nickel sulphate)why do the Cu2+ ions in copper oxide (CuO) not inhibit catalase?! Is it something to do with the fact they are bonded with sulphate? HELP!
Susan J.- London, UK
2005
Q. Hi I'm also a student and I'm doing AS biology, I just started the course work and I would like to know if copper sulphate can be used as an inhibitor on pectinase (breaking down pectins) its just I read it on a website and I'm not sure its true, any reply would be nice.
James W.- Telford
Q. I am an AS biology student doing my course work, and I have looked through previous questions, but as I have noticed, there has been none about the inhibition of yeast using Copper sulphate. I just wondered if anyone would mind giving me something, its just that I have a biological knowledge section of course work to complete and I can't find any information anywhere, I would appreciate it sooo much!
Roxanne H.Student - Bishops Stortford, Essex, UK
A. CuSO4 is indeed a non-competitive, irreversible inhibitor, because it is a heavy metal, the ions fit between the enzyme structure and alter the structure, preventing the enzyme from acting on any substrate.
Rox [last name deleted for privacy by Editor]- UK
Q. Hi everyone.
Are copper ions an inhibitor for amylase as well?
Thanks.
Jaany Frixtol- UK
2005
A. Just a warning, that I'm only an A2 student and what I say may or may not be entirely accurate. You should definitely check up on anything I write here in case it's wrong.
After spending a few hours in the library, I've learned that copper inhibits enzymes by binding with their -SH (sulphydryl) groups. While these are not part of the active site, they are an integral part of the enzyme, and their disruption permanently puts the enzyme out of action. Amylase I THINK is affected by this mechanism. It is irreversible and non competitive inhibition.
Another mechanism seems to involve displacement of the Ca2+ ion in amylase by Cu2+. This again makes the enzyme useless as the calcium is important for the reaction. I think this would be reversible, if the Cu2+ was replaced again by the Ca2+.
This seems to be a remarkably complicated subject. I suspect all we're required to say, at AS and A2 level, is that it's an irreversible noncompetitive inhibitor that affects amylase.
Hope that helps.
Corinne J. [last name deleted for privacy by Editor]- Herts, UK
Q. Hello,
I am an AS student about to do my course work, my experiment is how CuSO4 acts as an inhibitor using H2O2 and yeast. I'm not sure how to go about this any suggestions would be great. ASAP
Stephanie [last name deleted for privacy by Editor]- London, UK
2005
Q. Does anyone know what CuSO4 solution does to the production of fruit juice production when using pectinase? I have tried experimentally, and it looks like a non-competitive inhibitor. but I don't know if it is reversible or irreversible. If anyone could tell me how I would go about finding out if it is reversible or irreversible, I would be very grateful.
Tony [last name deleted for privacy by Editor]- Surrey, UK
Q. I understand that copper sulphate in a non competitive irreversible inhibitor but can someone please state where I can find this information for myself --some references from sites on the net to back up these statements?
Thank you.
Lizzie [last name deleted for privacy by Editor]- Hertfordshire, UK
Q. I'm an A2 student, like most people on this page I have just attempted a course work on the inhibiting effect of copper sulphate on the decomposition of H2O2...its slightly overdue :S
Anyway, I was wondering why we would be told copper ions inhibit only to discover they catalyze...what if in fact they slightly inhibit BUT the leftover sulfur from the copper sulphate is a catalyst for the reaction? would this be a reasonable explanation?
Also, why would copper displace iron from the haem group if iron is more reactive than copper? simply because there is so much more copper in comparison with iron? I would appreciate any help or comments or any other explanation as to why the reaction was not inhibited!
Cheers,
- Milton Keyens, England
A. copper sulphate is an inhibitor, it acts efficiently on the enzyme alpha amylase and thus inhibiting the starch degradation by the enzyme.
Vinaykumar. I . Gurav- Belgaum, Karnataka, India
A. To Louise N, Milton Keynes,
I am guessing the copper would go in place of the iron because the iron would actually displace the copper from the sulphate group, not the other way around. This would also, I am guessing, take away the catalytic effect that sulphate groups produce.
Just an idea.
- London, England
2007
Q. I am an AS Biology student who is doing a course work on the effect of copper sulphate on an enzyme based reaction with catalase. It's not working out right because the copper sulphate seems to be acting as an activator instead of an inhibitor? Please help; am at my wits' end trying to figure out what I am doing wrong
Ebby Ayerume- Barking, Essex, United Kingdom
2005
Q. I have just finished a test of the effect of copper sulphate on amylase. Strangely, low levels of copper sulphate were seen to inhibit the break down of starch while high levels of copper sulphate didn't just fail to inhibit the reaction but actually proved faster than a reaction with no copper sulphate. This has baffled me, how has the increased levels of copper sulphate actually speeded up the reaction when everything suggests that it shouldn't?
James Miller- England
Q. I've listened to everyone's comments and theories, but does anyone know how you can demonstrate what type of inhibitor copper sulphate is experimentally?
Sian Jones- UK
A. Inhibition is a complicated process. It takes a lot of balancing factors for it to be able to work as planned. copper sulphate iS A non-competitive INHIBITOR but some experiments may go wrong or not as planned because sometimes copper ions, in some conditions such as say difference in temperature or the amounts you are using, starts acting like an activator. The point about equilibriums and balance of the reactions may come into this. Too much copper sulphate will not work. someone mentioned .5 %....that's lots of copper ions and probably relatively less amounts of substrate or enzyme. Think about it. A level should be covering all this right? I'm a GCSE student!
KANI V.- London, UK
Q. Hi, I'm am doing AS biology and my course work is based on copper sulphate inhibiting the rate of which lactase breaks down lactose. Does anyone know of any background information of copper sulphate and why it inhibits this reaction? thanks.
Andre M.- London, UK
2005
Q. Can anyone tell me about the inhibitory effect of copper sulphate on invertase.
Sindhu a- Chennai, TN, India
A. You may find all the answers you wish regarding copper and catalase here:
Orr, C.: Studies on Ascorbic Acid. II. Physical Changes in Catalase Following Incubation with Ascorbate and Copper, Biochem 6, 3000, 1967
Here is the abstract:
Incubation of catalase with either ascorbate or ascorbate and Cu2+ results in degradative changes in the catalase molecule. The effect of ascorbate alone appears to be qualitatively distinct from that of ascorbate in the presence of Cu2+. Electrophoretic and chromatographic analysis of catalase treated with CU~+ and ascorbate revealed that the molecule is extensively degraded with the majority of the resultant fragments being dialyzable. A similar analysis of the effect of ascorbate alone indicated that the degraded fragments were substantially larger and that a small fraction of aggregated or polymerized material occurred. By using [ 14C]ascorbate, significant nondialyzable radioactivity was found associated with the polymerized material suggesting that at least some ascorbate must be bound to catalase. After treatment with ascorbate, or ascorbate and Cu2+, the spectrum of catalase is changed. While there is obvious reduction in the Soret band at 408 mp the shift of this peak to longer wavelengths is almost undetectable. It is concluded that very little, if any, catalase complex I1 is formed under these conditions. Significant spectral changes occur at shorter wavelengths. These have been tentatively interpreted to represent oxidative changes in labile aromatic amino acids. The results strongly support previous data which indicated that the inhibition of catalase by ascorbate, or ascorbate and Cu2+, was the result of . OH or * OnH attack of the enzyme.
If you are going to use any of this, do quote the original Author.
- Zagreb, Croatia
A. It doesn't seem to me that the effect of copper sulphate
⇦ on
eBay or
Amazon [affil links] on the activity of catalase is that difficult to digest. Bearing in mind that copper sulphate is a non-active site directed inhibitor, which effects catalase.
It attaches itself onto a part of catalase (NOT it's active site), and alters the shape of the enzyme and therefore after a certain point does not only inhibit the effect of catalase but has the potential to stop it's activity altogether.
The effect of copper sulphate on catalase increases as you increase the concentration of copper sulphate whilst keeping a constant concentration of catalase and the substrate you are using (most probably hydrogen peroxide).
As you increase the number of copper sulphate molecules, there are more copper sulphate molecules in comparison to catalase. Use this analogy to help remember:
there are 100 guys (catalase), and a x number of girls (copper sulphate). If there are only 50 girls then 50 guys are still busy, whereas if there are 100 girls and 100 guys, they are all busy!
- London, Forest-Gate, England
A. Hursh... Do you do AS Biology? - Just a thought.
CUSO4
Copper (II) Sulphate is a metal ion. Some more well known heavy metal ions are mercury (Hg+), silver (Ag+) and arsenic (As+). Another ion is the extremely toxic substance cyanide (CN-).
All these substances are enzyme inhibitors and they permanently damage enzymes. Copper (II) Sulphate is non-competitive and therefore they are non active site directed (the inhibitor does not function on the active site.
CUSO4 ions attach away from the active site but still distorts the overall shape of the enzyme thus inhibiting the corresponding substrate.
Copper (II) Sulphate inhibits enzymes by irreversibly altering the tertiary molecular structure of a protein (all enzymes are proteins!) by breaking its disulfide bonds.
@_@! Hope that helped some.
PS: Does Enzyme concentration have any effect on CUSO4? Does CUSO4 ultimately denature the enzyme?
- London, Clayhall, England
Q. What specific enzyme utilizes copper, iron, manganese and bromide?
Victoria Corazon Jordan- Cebu City, Philippines
2005
A. The enzyme concentration won't have any effect unless the ratio is greater for the enzyme. Because if it's true what you said that it is uncompetitive, then it doesn't have to compete for a place to attach, so it simply and calmly attaches to the enzyme...
So as long as the experimental yield isn't considered, NO enzyme concentration doesn't matter...
(I'm answering, hoping someone can correct me if I'm wrong because I'm simply a biology student...
- Uppsala, Sweden
Q. Hi
I have just carried out my AS investigation into the effect of changing the concentration of the inhibitor Copper Sulphate, on the enzyme catalase, in the decomposition of Hydrogen Peroxide. I predicted that the larger the concentration of copper sulphate, the less oxygen would be produced, therefore the rate of reaction would be slower. HOWEVER, after spending hours trying various different methods, my results were fairly inconclusive, as apart from the negative control, the ones with more copper sulphate produced more oxygen! In the first minute, each of the different concentrations (0.05, 0.1, 0.2, 0.3, 0.4 and 0.5 M) all produced 0.5 cm3. Does anyone have any idea why it would do this? Does the copper sulphate wash off after a minute? Should I have left the potato in the inhibitor for longer than 2 minutes? I am so confused! Please reply
- London, Middlesex, England
2006
Q. Just starting my cw on the effects of copper sulphate on amylase. Struggling to find scientific knowledge to back up my hypothesis, any ideas?
I know it is an inhibitor but am reading lots of conflicting info about whether it is competitive/ non-competitive or reversible/irreversible, my understanding is that it is a non-competitive reversible but not 100% sure about this.
Any help offered would be greatly appreciated.
- London, England
Q. I have been looking into the effects of copper sulphate on catalase. I am now in the process of planning my experiment, however I am unable to work out the specific volumes or concentrations of copper sulphate and potato pulp (catalase) to use.
William Gaille- London, England
Q. Does anybody know of any websites for any information on this subject? I am now doing course work on it for A-level and I need a 'reliable' evidence source, any website names someone could give?
Thanks
- Leiston, Suffolk, England
Q. Hi, I'm an A-level biology student preparing to study the various parameters that affect the kinetics of alpha-amylase catalyzed hydrolysis of starch. I will be testing varying concentrations of the enzyme amylase to catalyze the hydrolysis of starch.
Amylase should break down the polymer to smaller sugars and eventually convert them to the individual basic glucose units.
If anyone has any prior experience of planning this practical or knows of a reliable information source id be extremely grateful. I know in my head what to do and what to expect but my teacher insists I plan it out properly to the exams board requirements ... anyone know of any tips?
- Bromley, London, England
I'm writing up my AS biology course work, investigating the effect of Copper (II) Sulphate solution on the inhibition of amylase. Thanks to everyone who has posted information relating directly to this subject or just to Copper (II) sulphate. It has been very useful. (Don't worry I will reference you!)
Thanks
- Oxford, UK
2006
A. I've just finished my potato/catalase experiment and found that the following volumes/concentrations worked:
10 cc Copper Sulphate
5 g Potato (blended)
5 cc Hydrogen Peroxide
I used 2%, 1%, 0.75%, 0.5%, 0.25% and 0.1% concentrations of copper sulphate and did one with water as my control.
Hope this helps!
- London, UK
A. I've been doing AS course work on the effect of copper sulphate on rennin in the coagulation of milk. I found that instead of inhibiting the enzyme, rennin, it speeds the reaction up. This is because copper is a heavy metal so inhibits proteins, and milk consists of mainly protein so the milk forms a precipitate and clots. Rennin is also inhibited but is not required to coagulate the milk so does not affect the rate of the reaction.
Ian NewhamStudent - London, England
Q. Hey, Louise N's message was posted a while back and is very relevant to my course work write up, however I could not find a response to this post, could anyone help please, many thanks! Are Louise's theories correct? They seem very likely?
Alice W.- Reading, Berkshire, England
2006
Q. copper sulphate inhibits the germination of mustard seeds - but what effect, if any does sulphate alone have?
I have found many references to show the effect of copper but was wondering if anyone knew if sulphate would effect results and in what way.
Does it in fact have any role other than to allow solubility of copper?
- Welwyn, Garden City, UK
Q. How does copper sulphate amylase; as in what effects does it have on the structure?
Josh Jackson- Nantwich, Cheshire, England
2007
Hi I just want to say thank you to all of you because you have helped me so much, you have enabled me to fully understand my course work so that I am able to give an adequate answer to the question, I am very grateful, and just want to say thank you again to all of you!
- Wolverhampton, U.K.
A. I am a AS-level student of biology. If you are looking for a known inhibitor of catalase, I would suggest silver nitrate (AgNO3) solution. This is a non-competitive, non-reversible inhibition, as the silver (1+) ions react with the sulphydryl (-SH) groups of catalase, hence rendering catalase unable to catalyze the decomposition of hydrogen peroxide. I would further suggest you to begin with 1.0 M silver nitrate solution for a wide range of results.
Charles Brown- London, UK
2007
Q. Dear Readers,
I am a teacher in a very small school in a poor country, trying to teach my students enzyme inhibition. I am looking for a procedure to show the effect of lead nitrate on alpha amylase activity. If you have a simple procedure to show this, I would appreciate it very much.
teacher - Madanapalle, Andhra Pradesh, India
2007
A. The explanation about iron given above seems to describe a non-competitive enzyme action despite the first sentence. a competitive enzyme somehow blocks the active site with a molecule of similar structure to the intended substrate. The action described on the heam group is a non-competitive action which actually changes the structure of the protein.
Kabir [last name deleted for privacy by Editor]Bsix - London
Q. Hi I am trying to complete my course work on the effect of copper sulphate to amylase and starch. I found in my practical that the copper sulphate acted as a catalyst and am baffled by this as it is meant to be an inhibitor. I used 0.1 M copper sulphate and did it for temps 0 degrees to 70. Why did I get these results?
Danielle T.- Accrington, Lancashure, U.K.
2007
Q. Hi I've been using the non competitive inhibitor copper sulphate on the enzyme trypsin -- does this still have the same effect on the enzyme as catalase/amylase and attach by disulfide bonds or ionic bonds as I've been told?
Laura G.Student - Durham, UK
A. Hi, I think this is right, copper sulphate is a non competitive inhibitor. The copper sulphate attaches itself on to the catalase (away from the active site) distorting the enzymes shape therefore preventing the hydrogen peroxide being able to "lock" into the active site as it doesn't fit anymore. Hope it helps x
Emily Thorpe- Leeds, U.K.
Q. Okay, I'm doing as biology c/w and I'm using fruit to get the catalase enzyme from, however I have no idea how to extract the catalase from the fruit or even if that's what I'm supposed to be doing? Any advice would be much appreciated.
Carmen D. [last name deleted for privacy by Editor]- Redbridge, London, UK
February 3, 2008
Q. Hey
Another AS biology student... thanks so much to everyone who has already contributed. I just wanted to check if this is alright:
copper sulphate acts as an inhibitor of catalase because the copper
2+ ions that are released when copper sulphate is in solution displaces the iron haem group which helps to catalase the overall reaction.
- Kent, England
February 3, 2008
Q. I'm doing AS Biology at the moment, and my course work is "the effect of copper sulphate on the enzyme amylase". And (after a week of conducting the experiment with the WRONG enzyme!) I'm a little bit confused. This is gonna seem like a really thick question, but what actually is amylase? I know it's an enzyme with a tertiary structure of amino acids and all that, but I was reading through what everyone else has said, and there was something about calcium ?! What does copper sulphate do/bind to/deactivate/bugger up in the amylase to permanently inhibit it?
I'm sure this is a stupid question, but please could someone intelligent explain it to me!
cheers! XD
- London, England
February 13, 2008
Q. Hey, thanks for all those comments they have helped me in my AS human bio cwk, however, could anyone explain a little better the part about how copper displaces iron ions in the enzyme catalase, my teacher said I needed to research this and I can't find ANYTHING!
Cheers.
- UK
March 12, 2008
A. Hi Anna. I'm from the metal finishing industry and know nothing about enzymes, but we do know that copper displaces iron in simple salts (an iron nail placed in a solution of copper sulphate will spontaneously grow a copper plating). The reason for this is that although both copper and iron ions are positively charged,copper is more noble -- it has more affinity for any available electrons, more attractive power, so positively charged copper ions will steal electrons from neutral (metallic) iron, letting the copper come out of solution and causing the iron to go into solution.
Regards,
Ted Mooney, P.E.
Striving to live Aloha
finishing.com - Pine Beach, New Jersey
Q. Hi, please can calcium inhibit amylase? If it can, how does it inhibits amylase and is it a competitive or non competitive inhibition?
INABOYA STANLEYSTUDENT - BENIN, EDO, NIGERIA
September 16, 2008
Q. Hi, my name is Sita ram, I am carrying out the effect of copper on amylase activity and I want to know about its interactions, also about its effects on amylase activity.
Sita ram Pottumuttu- Visakhapatnam, Andhra Pradesh, India
October 22, 2008
Q. Hi everyone,
I wanted to know whether copper sulphate acts as a Fungal Inhibitor or not. Please help me answer this question?
- Delhi , India
December 30, 2008
Q. We are starting to use copper sulphate in our wort agar to isolate colonies of yeasts. We are told that copper sulphate will inhibit ab yeast (Anheuser Busch yeast) but will not affect other wild type yeasts. We do not buy this theory. Tell us how copper sulphate inhibits yeast growth and also why it will inhibit all yeasts just not ab yeast. Thanks.
dave passarellianalysis qa - rydal georgia
August 2, 2009
Q. What evidence is there that it isn't the sulphate group that causing the inhibition / effects the reaction is any way? I'm aware that it is the metal ion which inhibits but for the purpose of my investigation it would help to explain why this is so.
Andy B. [last name deleted for privacy by Editor]Student - Southampton, U.K.
March 12, 2011
A. I'm an A2 chemistry student doing my individual investigation. Having done an experiment on the effect of copper(II) sulphate inhibition on both the effect catalase and an inorganic catalyst (Manganese(IV) oxide) on the decomposition of hydrogen peroxide, I found that in both cases the results showed significant variation from my volume control. This would suggest to me that the mechanism of inhibition stems more from interaction with the hydrogen peroxide (perhaps the formation of ligand complexes) which prevent the decomposition. That's not to say that the copper ions do not inhibit the enzyme, but from my results I would submit that the much more significant factor would be copper-substrate interaction.
Angus Bonnett- Isle of Man, U.K.
Q. Hey guys,
I've been reading a lot of these posts and I think one big thing to consider is that using a liver cell or potato cell or yeast cell (which is what I regrettably did for my coursework) is actually very different from using pure catalase since cells can die or the copper can't get past the cell membrane or the copper has a higher affinity for some other enzyme inside the cell than for catalase.
Basically lots of problems if you don't use pure catalase so that might be why a lot of people's results are weird because mine definitely were. Basically I added 10 ml of CuSO4 solution to my yeast solution each time and increased the concentration from 0.0 mol/dm3 to 0.1 mol/dm3 etc up to 0.5 mol/dm3 and my rate of oxygen production started low at 0.0 mol/dm3 , increased until a peak at 0.3 mol/dm3 and then sharply dropped again. This was not expected; the rate of reaction was supposed to keep dropping as concentration increased and I don't quite know why. The reason I talked about before is one possible answer but there might be others. Any ideas anybody has would be great, and thank you to everyone who contributed to this thread already- it was really helpful
- Hong Kong, China
April 23, 2014
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