CH 48 School of Science and Engineering, ATENEO DE MANILA UNIVERSITY

Experiment 2: Potentiometric Acid-Base Titrations

1. Introduction
The ionization constant of weak acids and bases may be measured from the titration curves wherein each inflection point essentially gives the pK value corresponding to an ionization equilibrium. The titration curve may be determined through potentiometric titration. For a hypothetical, univalent acid ionization:

HA ====== A- + H+
the equilibrium is written as:

(1)

Ka = aH+ aA- / aHA Ka = aH+ CA A / (CHA HA)

(2) (3)

where the as are the activities of the species in solution, C is the concentration, and is the activity coefficient. Taking the negative logarithms of both sides of the equation yields: pKa = - log aH+ - log (CA/CHA) - log (A / HA) pKa + log (A / HA) = - log aH+ - log (CA/CHA) pK = pH - log (CA/CHA) (4)

In equation (4), the term for the activity coefficients is lumped with the true pKa value giving a redefinition of Ka as K. During titration, the pH or the cell potential E, is measured and plotted against the volume of titrant added. The potential of the solution is usually measured using a glass electrode against a reference electrode (usually Ag/Agcl); this potential is directly proportional to the pH as follows: E = constant + 2.303 (RT/F) pH (5) where the constant is obtained from the calibration of the electrode against standard buffer solutions. Measurement of pKa values is based on the assumption that the process is a reversible one. If a voltmeter is used to measure the potential, it draws a small current thereby making the process for generating the titration curve irreversible. To circumvent this, a potentiometer is used in measuring cell electromotive force. For weak acids, when the concentration of the conjugate base becomes significant, the solution exhibits a buffering effect, that is, it is able to resist drastic changes in pH on addition of a small amount of acid or base. The buffer capacity may be calculated as follows: dB / d(pH) = (2.303 CA-CHA) / (CA- + CHA) (6)

where B is the number of equivalents of base (or titrant) added per liter of solution. A plot of dB/d(pH) against pH shows the point in the titration curve at which there is maximum buffering capacity.

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CH 48 School of Science and Engineering, ATENEO DE MANILA UNIVERSITY

II. Procedure
1. Prepare standardized 0.1 M NaOH and 0.1 M HCl solutions. Use deionized water in preparing the NaOH solution, and standardize it against standard potassium acid phthalate using a phenolphthalein endpoint. The HCl solution may then be standardized using the standardized NaOH solution. Follow the instructions for calibration, use, and proper care of the pH meter and pH probe. Titration of acetic acid. Titrate 25 mL of 0.1 M acetic acid with 0.1 M NaOH. Take pH readings after every 5 mL addition of the titrant, but take more readings near the inflection points. To see this, you will need to roughly plot the curve on a graphing paper as you titrate. Titration of an amino acid. Weigh out about 250-mg portions of the amino acid and dissolve in 30mL deionized water. Titrate one portion with the standard 0.1 M NaOH, and the other with the 0.1 M HCl solution. Record the pH at every 5-mL interval and with increasing frequency near the inflection points.

2. 3.

4.

In addition, measure the pH range of phenolphthalein by adding a few drops to the amino acid solution being titrated. Note the pH at which the color changes are observed.

III. Data analysis

Plot the equivalents of base added per L of solution against pH, and dB/d(pH) against pH. Determine from these the point at which maximum buffering capacity is observed for acetic acid. Discuss your results. The titration curve for the amino acid may be generated by plotting pH versus volume HCl to the left of the origin, and the pH against volume of base to the right. Re-plot this curve against equivalents H+ added that reacted per mole of amino acid. Equivalents H+ is determined from the pH and the volume of titrant added. On a separate graph, plot the buffer capacity curve. Determine the pK values of the amino acid. Will it be possible to determine the form (whether pure, a sodium salt or chloride salt) of the amino acid at the start of the experiment? Include in your discussion the effect of pH on indicator used.

IV. References
PW Atkins. 1994. Physical Chemistry, 5/e. Oxford: ELBS FD Daniels, RA Alberty, JW Williams, CD Cornwell, P Bender, & JE Harriman. 1970. Experimental Physical Chemistry, 7/e. New York: McGraw-Hill. DC Harris. 1987. Quantitative Chemical Analysis, 2/e. New York: WH Freeman. DR Patrick. 1992. Electronic Instruments: Instrumentation Training Course, 4/e. New Jersey: Prentice-Hall.

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