Buffer solution

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Acids and bases

Acid dissociation constant

Acid-base extraction
Acid-base reaction
Dissociation constant
Acidity function
Buffer solutions
pH
Proton affinity
Self-ionization of water

Acid types

Brønsted · Lewis · Mineral

Organic · Strong
Superacids · Weak

Base types

Brønsted · Lewis · Organic

Strong · Superbases
Non-nucleophilic · Weak

v·d·e

For an individual weak acid or weak base component, see Buffering agent. For uses not
related to acid-base chemistry, see Buffer (disambiguation).
A buffer solution is an aqueous solution consisting of a mixture of a weak acid and its conjugate
base or a weak base and its conjugate acid. It has the property that the pH of the solution changes
very little when a small amount of strong acid or base is added to it. Buffer solutions are used as
a means of keeping pH at a nearly constant value in a wide variety of chemical applications.
Many life forms thrive only in a relatively small pH range; an example of a buffer solution is
blood.
Contents
[hide]
• 1 Principles of Buffering
• 2 Buffer capacity
• 3 Calculating buffer pH (monoprotic acid)
• 4 Calculating buffer pH (polyprotic acid)
• 5 Applications
○ 5.1 Useful buffer mixtures
○ 5.2 "Universal" buffer mixtures
○ 5.3 Common buffer compounds used in biology
• 6 See also
• 7 References
• 8 External links

[edit] Principles of Buffering

Simulated titration of an acidified solution of a weak acid (pKa = 4.7) with alkali.
Buffer solutions achieve their resistance to pH change because of the presence of an equilibrium
between the acid HA and its conjugate base A-.

HA H+ + A-
When some strong acid is added to an equilibrium mixture of the weak acid and its conjugate
base, the equilibrium is shifted to the left, in accordance with Le Chatelier's principle. Because of
this, the hydrogen ion concentration increases by less than the amount expected for the quantity
of strong acid added. Similarly, if strong alkali is added to the mixture the hydrogen ion
concentration decreases by less than the amount expected for the quantity of alkali added.
The effect is illustrated by the simulated titration of a weak acid with pKa = 4.7. The relative
concentration of undissociated acid is shown in blue and of its conjugate base in red. The pH
changes relatively slowly in the buffer region, pH = pKa ± 1, centered at pH = 4.7 where [HA] =
[A-], but once the acid is more than 95% deprotonated the pH rises much more rapidly.
[edit] Buffer capacity

Buffer capacity for a 0.1 M solution of an acid with pKa of 7

Buffer capacity, β, is a quantitative measure of the resistance of a buffer solution to pH change
on addition of hydroxide ions. It can be defined as follows.

where dn is an infinitesimal amount of added base and d(p[H+]) is the resulting infinitesimal
change in the cologarithm of the hydrogen ion concentration. With this definition the buffer
capacity of a weak acid, with a dissociation constant Ka, can be expressed as

where CA is the analytical concentration of the acid.[1] pH is approximately equal to -log10[H+].

There are three regions of high buffer capacity.
• At very low p[H+] the first term predominates and β increases in proportion to the
hydrogen ion concentration. This is independent of the presence or absence of buffering
agents and applies to all solvents.
• In the region p[H+] = pKa ± 2 the second term becomes important and β rises to a
maximum at p[H+] = pKa. Buffer capacity is proportional to the concentration of the
buffering agent, CA, so dilute solutions have little buffer capacity. It is also proportional
to the acid dissociation constant, Ka (not pKa); the weaker the acid the greater its
buffering capacity.
• At very high p[H+] the third term predominates and β increases in proportion to the
hydroxide ion concentration. This is due to the self-ionization of water and is independent
of the presence or absence of buffering agents.
[edit] Calculating buffer pH (monoprotic acid)
First write down the equilibrium expression.
 HA A- + H+
The concentrations of the three species van be calculated in an ICE table. The columns of the
table correspond to the three species in equilibrium.
ICE table for monoprotic acid
[HA] [A-] [H+]
I C0 0 0
C -x x x
E C0-x x x
The first row, labelled I, has the Initial conditions: the concentration of acid is C0 and it is
initially undissociated so the concentrations of A- and H+ are zero. The second row, labelled C
for Change, specifies that when the acid dissociates, its concentration changes by an amount -x
and the concentrations of A- and H+ both change by an amount +x. This follows from the
equilibrium expression. The third row, labelled E for Equilibrium concentrations, is the sum of
the first two rows and shows the concentrations at equilibrium. It can be seen from the table that
at equilibrium [H+] = x.
To find x the equilibrium constant must be specified.

Substitute the concentrations with the values found in the last row of the ICE table.

With specific values for C0 and Ka this equation can be solved for x. Assuming that pH =
-log10[H+] the pH can be calculated as pH = -log10x.
Note. When a pH meter is calibrated using known buffers, the reading gives the hydrogen ion
activity rather than its concentration. In this case the meter reading may differ from the value
calculated as above. For example, calculation of pH of phosphate-buffered saline would give the
value of 7.96, whereas the meter reading would be 7.4. The discepancy arises when the acid
dissociation constant value is specified as a concentration quotient and would not occur if Ka
were specified as a quotient of activities.
[edit] Calculating buffer pH (polyprotic acid)
% species formation calculated for a 10 millimolar solution of citric acid.
Polyprotic acids are acids that can lose more than one proton. The constant for dissociation of the
first proton may be denoted as Ka1 and the constants for dissociation of successive protons as Ka2,
etc. Citric acid, H3A, is an example of a polyprotic acid as it can lose three protons.
equilibrium pKa value
H3A H2A− + H+ pKa1 = 3.13

H2A− HA2− + H+ pKa2 = 4.76

HA2− A3− + H+ pKa3 = 6.40
When the difference between successive pK values is less than about three there is overlap
between the pH range of existence of the species in equilibrium. The smaller the difference, the
more the overlap. In the case of citric acid the overlap is extensive and solutions of citric acid are
buffered over the whole range of pH 2.5 to 7.5. Calculation of the pH of a particular mixture
requires a speciation calculation to be performed.
[edit] Applications
Buffer solutions are necessary to keep the correct pH for enzymes in many organisms to work.
Many enzymes work only under very precise conditions; if the pH moves outside of a narrow
range, the enzymes slow or stop working and can denature, thus permanently disabling their
catalytic activity.[2] A buffer of carbonic acid (H2CO3) and bicarbonate (HCO3−) is present in
blood plasma, to maintain a pH between 7.35 and 7.45.
Industrially, buffer solutions are used in fermentation processes and in setting the correct
conditions for dyes used in colouring fabrics. They are also used in chemical analysis[1] and
calibration of pH meters.
The majority of biological samples that are used in research are made in buffers, especially
phosphate buffered saline (PBS) at pH 7.4.
[edit] Useful buffer mixtures
Components pH range
HCl, Sodium citrate 1-5
Citric acid, Sodium citrate 2.5 - 5.6
 Acetic acid, Sodium acetate 3.7 - 5.6
K2HPO4, KH2PO4 5.8 - 8
Na2HPO4, NaH2PO4 6 - 7.5
CHES 8.6–10
Borax, Sodium hydroxide 9.2 - 11
[edit] "Universal" buffer mixtures
By combining substances with pKa values differing by only two or less and adjusting the pH a
wide-range of buffers can be obtained. Citric acid is a useful component of a buffer mixture
because it has three pKa values, separated by less than two. The buffer range can be extended by
adding other buffering agents. The following two-component mixtures (McIlvaine's buffer
solutions have a buffer range of pH 3 to 8.[3]
0.2M Na2HPO4 /mL 0.1M Citric Acid /mL pH...
20.55 79.45 3.0
38.55 61.45 4.0
51.50 48.50 5.0
63.15 36.85 6.0
82.35 17.65 7.0
97.25 2.75 8.0
A mixture containing citric acid, potassium dihydrogen phosphate, boric acid, and diethyl
barbituric acid can be made to cover the pH range 2.6 to 12.[4]
Other universal buffers are Carmody buffer and Britton-Robinson buffer, developed in 1931.
[edit] Common buffer compounds used in biology
Temp
pKa Effect
Common Buffer Mol.
at dpH/dT Full Compound Name
Name Range Weight
25°C in (1/K)
**
3-
7.7–
TAPS 8.43 −0.018 243.3 {[tris(hydroxymethyl)methyl]amino}propanesulfonic
9.1
acid
7.6–
Bicine 8.35 −0.018 163.2 N,N-bis(2-hydroxyethyl)glycine
9.0
7.5–
Tris 8.06 −0.028 121.14 tris(hydroxymethyl)methylamine
9.0
7.4–
Tricine 8.05 −0.021 179.2 N-tris(hydroxymethyl)methylglycine
8.8
3-[N-Tris(hydroxymethyl)methylamino]-2-
TAPSO 7.635 7.0-8.2 259.3
hydroxypropanesulfonic Acid
6.8–
HEPES 7.55 −0.014 238.3 4-2-hydroxyethyl-1-piperazineethanesulfonic acid
8.2
6.8– 2-{[tris(hydroxymethyl)methyl]amino}ethanesulfonic
TES 7.40 −0.020 229.20
8.2 acid
MOPS 7.20 6.5– −0.015 209.3 3-(N-morpholino)propanesulfonic acid
 7.9
6.1–
PIPES 6.76 −0.008 302.4 piperazine-N,N′-bis(2-ethanesulfonic acid)
7.5
5.0–
Cacodylate 6.27 138.0 dimethylarsinic acid
7.4
SSC 7.0 6.5-7.5 189.1 saline sodium citrate
5.5–
MES 6.15 −0.011 195.2
6.7

What is the principle involved in the isolation of

casein from milk?
It is about isoelectric precipitation. This involves the principle on isoelectric pH of a
certain solution. Casein has its isoelectric pH at 4.6. Therefore, it is insoluble in
solutions with pH lower than 4.6. The pH of milk is around 6.6 which gives casein
the negative charge and makes it a soluble salt. Once you add an acid to the
solution, the negative charge of casein becomes neutral, precipitating the neutral
protein (casein).

Sorry,the answer is not so good. Try to do some research too. :)

Isotope separation

Other centrifuges, the first being the Zippe-type centrifuge, separate isotopes, and
these kinds of centrifuges are in use in nuclear power and nuclear weapon
programs.

Gas centrifuges are used in uranium enrichment. The heavier isotope of uranium
(uranium-238) in the uranium hexafluoride gas tends to concentrate at the walls of
the centrifuge as it spins, while the desired uranium-235 isotope is extracted and
concentrated with a scoop selectively placed inside the centrifuge. It takes many
thousands of centrifuges to enrich uranium enough for use in a nuclear reactor
(around 3.5% enrichment), and many thousands more to enrich it to weapons-grade
(above 90% enrichment) for use in nuclear weapons.

Explain the solubility of ovoglobulin in egg

white knowing that globulins are not soluble
in water?
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The ovoglobulin forms a sol in dilute salt solutions, but not in pure water
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Other Answers (1)

• Mr Hex Vision
It just well could be that the egg white is like an organic solvent due to the amount of
proteins and fat in it. With this in mind the ionic properties are changed to a non-polar
environment causing the globulins to be dissolved in the egg white.
Description
This section is from the book "Experimental Cookery From The Chemical And Physical
Standpoint", by Belle Lowe. Also available from Amazon: Experimental cookery.

Properties Of Egg Proteins

The extensive use of eggs in cookery is made possible by their protein content. The protein
coagulates during heating, thus bringing about thickening as in custards or the binding of pieces
of food together as in croquettes. The proteins of the egg are good emulsifying agents. The
proteins form elastic films when beaten, thus incorporating air, which is used as leavening in
such products as angel cakes and souffles. The elasticity of the egg protein is also important in
products such as popovers where the egg stretches with expansion of steam, and later coagulates
to aid in forming the framework of the popover.
The proteins of the egg. The proteins of the white are ovoalbumin, ovoglobulin, and ovomucin.
There may be small amounts of other proteins and it is also possible that each protein is made up
of component fractions. Hughes and Scott give the relative proportions of the proteins in the
three portions of the white as shown in Table 41.
The principal protein of the yolk is ovovitellin. Sell, Olsen, and Kremers separated salted egg
yolk into a soluble lipoid fraction and an insoluble residue. The latter consisted of sodium
chloride and the protein-like material of the yolk. This residue they called lecitho-protein. It
composed about 32.5 per cent of the yolk. This protein fraction contained nearly one-half the
total lecithin of the yolk.
Percentage Of The Total Nitrogen Contributed By Each Of
The Three Protein Fractions (Hughes And Scott)
Outer thin layer of egg Thick layer of Inner layer of thin
white white white

Ovomucin....................................... 1. 91 5. 11 1. 10

Ovoglobulin................. 3. 66 5. 59 9. 89

Ovoalbumin.................................... 94 .43 89. 18 89. 29

Solubility of the proteins. The albumin of egg forms a sol with water and dilute salt solutions.
The globulin forms a sol in dilute salt solutions, but not in pure water. The globulin composes
about 6.5 per cent of the total proteins of the egg.
Egg-white proteins belong to the group of hydrophilic colloids. Egg white and water are
mutually soluble. Usually the addition of 1 tablespoon of water to an egg white, unless it is very
watery, increases its extensibility, and when the egg white is whipped a larger volume is
obtained. But with increasing quantities of water a stage is reached at which the egg white loses
too much of its rigidity and will no longer retain air in small bubbles, the bubbles being large and
floating on the more liquid part.
The ovovitellin of the egg yolk is combined with phosphorus and belongs to the phosphoprotein
group. It is insoluble in water but is soluble in dilute salt solutions and in dilute alkalies.
Isoelectric point of egg proteins. Loeb has reported the isoelectric point of egg albumin as pH
4.8. Some investigators give pH 4.7 as the isoelectric point. Above the isoelectric point the
albumin combines with bases to form salts like sodium albuminate; below the isoelectric point it
combines with acids to form salts like albumin acetate, citrate, or tartrate. Above the isoelectric
point the protein is negatively charged; below, it is positively charged. Since the reaction of the
egg white is about pH 7.6 to 9, there will probably be few combinations of egg white with
alkalies or alkaline salts in food preparation that will increase its alkalinity. Many combinations
are made that increase its acidity. For example, the addition of a teaspoon of cream of tartar, a
salt with an acid reaction, to a cup of egg whites, proportions often used in angel food cakes,
increases the acidity and lowers the pH, often to about 7.5 or 7.0. As the proportion of cream of
tartar is increased, the pH is lowered to a greater extent. The addition of fruit juices and fruit pulp
to egg whites to make fruit whip, souffles, or similar desserts, increases the acidity. When 1 to 2
teaspoons of lemon juice are added to an egg white the pH is lower than 4.8.
No record could be found in the literature of the isoelectric point of ovovitellin. When lemon
juice is added to egg yolk, the mixture is thickest at a pH between 4 and 5, as if the greatest
tendency to curdle is at this point. This might indicate that the isoelectric point of the egg yolk
proteins is between pH 4 and 5. This greatest thickening occurs with about 5 cc. of lemon juice
to an egg yolk.
The addition of an acid like vinegar or fruit juice to the white and yolk beaten together tends to
curdle the mixture. This occurs when the acidity is in the vicinity of the isoelectric point. When
sufficient acid is added to lower the pH below the isolectric point of the egg proteins, and if the
salt formed, such as protein citrate, is soluble, the coagulum dissolves and the mixture becomes
smooth. With the exception of salad dressings and a few sauces, there are probably not many
instances in which enough acid is added to lower the pH of the food mixture below the
isoelectric point of the egg protein.
Peptization of egg proteins. Peptization of egg proteins increases the tenderness of some
products. Freundlich states that peptization of proteins is frequently brought about by low
concentrations of electrolytes, though to accomplish this the electrolyte must be intimately mixed
with the substance to be peptized. The hydroxyl, citrate, acetate, and tartrate ions are effective
for peptizing egg proteins. For example, when tomato or lemon juice is added to egg in amounts
to bring the pH of the egg slightly above or about the isoelectric point of egg albumin, the
tenderness of omelets is definitely increased. In some instances peptization of the egg proteins is
detrimental. An example of this is the thinning of salad dressings, thickened with only egg yolk,
when heated above the temperature at which optimum coagulation occurs.
Sugars (sucrose, dextrose, and levulose) through peptization tend to prevent coagulation of egg
protein.
Denaturation. Denaturation, by which soluble proteins are rendered insoluble, of egg proteins is
brought about in a variety of ways, including the action of acids, salts, heat, mechanical
agitation, and radiation. Mechanical agitation or beating of egg white, as well as the tendency of
proteins in surfaces to form films, causes partial denaturation of the egg proteins. Sugar tends to
prevent this denaturation.
Genetics of Bitter Taste Perception
Scientists have found bitter taste perception is connected to human populations that share
common genes. For example, the percentage of people who do not taste bitterness ranges from 3
percent in West Africa; 6 to 23 percent in China; 40 percent in India and approximately 30
percent in people of European decent.
Differences in bitter taste perception among people are believed to be about 20 percent gene-
based. The most common gene cited as having an impact on bitter taste perception is the
TAS2R38 gene on chromosome 7. People who are more sensitive to bitterness carry the C allele
of the SNP rs1726866, while those who carry the T allele of this SNP on both copies of
chromosome 7 are more likely to be less sensitive. There are other gene variants that may
explain bitter taste perception, but not near to the degree as the TAS2R38 gene.
Interpreting Your Genetic Test Results
There is a way for people to find out if they are a bitterness non-taster, taster, or super-taster. It is
difficult to make firm judgments based on the test results, but studies have found that the non-
taster genotype can be a predictor of increased alcohol consumption in adults and lower
preference for sweets in children. If you are a super-taster, you may not enjoy some foods such
as grapefruit, cabbage, or coffee.
Frequently Asked Questions About Bitter Taste Perception
Q: If I taste a food that is new to me and it is bitter, should I leave it alone?
A: Not necessarily. There are many foods that have a bitter taste that are fine to eat. However, if
you are trying something new and have no information on whether it is safe to eat or not,
bitterness can possibly be an indication that you should not eat it.
Q: Why is the study of bitter taste perception important to researchers?
A: Research into bitter taste perception can be very useful because it provides information about
the foods people may want to eat, depending on their sensitivity to bitterness. Over time, this
research may be helpful in predicting how people respond to new food products and aid in the
development of dietetic interventions.
Q: Do I need to be concerned if I am a non-taster or super-taster for bitterness?
A: Information that suggests that a person is prone to being a non-taster or super-taster of
bitterness does not require any particular intervention, although it can be useful information in
relation to why he or she likes certain foods. There is evidence that harmful chemicals often taste
bitter, which could be an issue with non-tasters of bitterness. However, at this point, science has
not evolved to the point of easily altering genes to enhance sensitivity to bitterness.
Recent News on Bitter Taste Perception
Researchers are looking at factors that contribute to children being overly sensitive to bitterness.
Evidence shows that parents who are sensitive to bitterness have children who are often much
more sensitive, suggesting that ability to accept bitterness may improve with age.
Scientists at the Monell Chemical Senses Center have discovered that bitter taste perception of
vegetables is influenced by a combination of taste genes and the presence of naturally-occurring
toxins in a given vegetable. It is believed that taste receptors are capable of detecting toxins in
fruit and vegetable plants.