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Q&As since 1989
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Biology of Copper sulphate
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A. It doesn't seem to me that the effect of copper sulphate [on
eBay or
Amazon]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
2005
Q. What specific enzyme utilizes copper, iron, manganese and bromide?
Victoria Corazon Jordan- Cebu City, Philippines
2005
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
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
2005
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
2006
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
2006
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
2006
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
2006
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
2006
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
2006
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
2006
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.
2007
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
2007
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
2007
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.
2007
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. 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 copper and iron ions are positively charged, but 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
April 2014
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.
March 5, 2012
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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