Activity Coefficient of Solution Components and Salts as Special Osmolyte from Kirkwood-Buff Theoretical Perspective

Main Article Content

Ikechukwu Iloh Udema
Abraham Olalere Onigbindec

Abstract

Background: There has been different interpretation of kosmotropes and chaotropes without concern for the physicochemical characteristics of the macromolecule and for the link between Hofmeister phenomena with solution structure. The objectives of this research are: 1) To investigate  different ways of determining activity coefficient and activity of ionic osmolyte 2), to present a common theoretical basis for the interaction between reaction mixture components and Hofmeister phenomena and 3) determine the preferential interaction parameters and the Kirkwood-Buff integrals.


Methods: A major theoretical research and partly experimental.


Results and Discussion: Some equations in literature gave different values of activity coefficient and activity of solution components. The preferential interaction by binding is positive with ethanol only and at its higher concentration in the presence of ideal solution of different concentration of calcium chloride. There was positive m-value with ethanol. It was negative m-value in the presence of preferentially binding species, calcium ion and ethanol as against the excluded chloride ion. There was negative and positive change of solvation preference and interaction parameter due respectively to ethanol only and a mixture of it and the salt.


Conclusion: Selected equations in literature may not give the same values of activity coefficient and activity of solution components. The presence of stabilising osmolyte, salt, and ethanol may not always yield positive m-values. The sign of the change of solvation preference with either binary or ternary mixture of osmolytes and, the cognate interaction parameter, may be a better indicator of the stability of a macromolecule. The kosmotropes and chaotropes may be cationic or anionic and their deficit or otherwise around the macromolecule and consequence, depend largely on net charge on the macromolecule at a given pH.

Keywords:
Porcine pancreatic alpha amylase, activity coefficient, preferential interaction parameter, change of solvation preference, m – value, ethanol, calcium chloride

Article Details

How to Cite
Udema, I., & Onigbindec, A. (2019). Activity Coefficient of Solution Components and Salts as Special Osmolyte from Kirkwood-Buff Theoretical Perspective. Asian Journal of Research in Biochemistry, 4(3), 1-20. Retrieved from http://journalajrb.com/index.php/AJRB/article/view/30068
Section
Original Research Article

References

Udema II, Onigbinde AO. Basic Kirkwood – Buff theory of solution structure and appropriate application of Wyman linkage equation to biochemical phenomena. Asian Journal of Physical and Chemical Sciences. 2019;7(1):1-14.

Sirotkin VA, Kuchierskaya AA. Alpha-Chymotrypsin in water-ethanol mixtures: Effect of preferential interactions. Chemical Physics Letters. 2017;689:156-161.

Cho Y, Zhang Y, Christensen T, Sagle LB, Chilkoti A, Crem er PS. Effects of Hofmeister anions on the phase transition temperature of elastin-like polypeptides. J Phys Chem B. 2008;112(44):13765–13771.

Evens TJ, Niedz RP. Are Hofmeister series relevant to modern ion-specific effects research? Scholarly Research Exchange. 2008;2008:1-9.

Harries D, Rösgen J. Use of macroscopic properties of solution to derive microscope structural information. Methods Cell Biol. 2008;84:680-730.

Rösgen JB, Pettitt M, Bolen DW. An analysis of the molecular origin of osmolyte-dependent protein stability. Protein Sci. 2007;16:733-743.

Ramasubbu N, Paloth V, Luo Y, Brayer GD, Levine MJ. Structure of human salivary alpha amylase at 1.6Å resolution: Implication for its role in the oral cavity. Acta Crysta. 1996;D52:435-446.

Yadav JK, Prakash V. Stabilization of α-amylase, the key enzyme in carbohydrates properties alterations, at low pH. Int. J. Food Prop. 2011;14:1182–1196.

Hertadi R, Widhyastuti H. Effects of calcium ion to the activity and stability of lipase isolated from Chromohalobacter japonicas BK-AB18. Procedia Chem. 2015;16:306-313.

Cipolla A, Delbrassine F, Da Lag J-C, Feller G. Temperature adaptations in psychrophilic, mesophilic and thermophilic chloride-dependent alpha amylase. Biochemie. 2012;94(9):1943-1950.

Lund M. Electrostatic interactions in and between biomolecules. Lund University. Ph.D Thesis.

Rösgen J, Pettit MB, Bolen DW. Protein folding, stability, and solvation structure in osmolyte solution. Biophys. J. 2005;89: 2988–2997.

Troller J. Methods to measure water activity. J. Food. Prot. 1983;46(2):129-134.

Saleh R, Khlystov A. Determination of activity coefficient of semi-volatile organic aerosols using the integrated volume method. J. Aerosol Sci. 2009;43(8):838-846.

Zhang L, Lu X, Wang Y, Shi J. Determination of activity coefficients using a flow EMF method. HCl in Methanol-water mixtures at 25, 35, 45C. J. Solution Chem. 1993;22(2):137-150.

Esteso MA, Fernandez-Merida L, Hernandez-Luis FF. Determination of activity coefficients in aqueous solutions of trichloroacetic acid from emf measurements at 25C. J. Electroanal. Chem. Interfacial Electrochem. 1987; 230(1-2):77-84.

Levine IN. Physical chemistry Peterson, K.A. and Oberbroeckling, S.R. (Eds) 5th Ed. McGraw-Hill Companies, Inc., 1221 Avenue of the Americas, New York, NY10020. 2002;299-303.

Miyawaki O, Saito A, Matsuo T, Nakamura K. Activity and activity coefficients of water in aqueous solutions and their relationships with solution structure parameters. Biosci. Biotech. Biochem. 1977;61(3):466-469.

Timasheff SN. Protein solvent preferential interaction, protein hydration, and the modulation of biochemical reactions by solvent components. Biochemistry. 2002;99(15):9721-9726.

Stadie WC, Sunderman FW. The osmotic coefficient of sodium in sodium hemoglobinate and of sodium chloride in hemoglobin solution. J. Biol. Chem. 1931;90(526):227-241.

Heitz MP, Rupp JW, Horn KW. Biocatalytic activity of mushroom tyrosinase in ionic liquids: Specific ion effects and the Hofmeister series. Insights Enzyme Res. 2018;2(1:1):1-9.

Sky-Peck HH, Thuvasethakul P. Human pancreatic alpha-amylase. II. Effects of pH, substrate and ions on the activity of the enzyme. Ann. Clin. Lab. Sci. 1977;7(4): 310-317.

Harano Y, Kinoshita M. Translational entropy gain of the solvent upon protein folding. Biophys. J. 2005;89:2701-2710.

Arakawa T, Timasheff SN. Mechanism of protein’s salting-in and salting-out by divalent salts: Balance between hydration and salt binding. Biochemistry. 1984;23(25):5912-5923.

Shimizu S. Estimating hydration changes upon bimolecular reactions from osmotic stress, high pressure, and preferential hydration experiments. Proc. Natl. Acad. Sci. U.S.A. 2004;101:1155–1199.

Parsegian VA, Rand RP, Rau DC. Osmotic stress, crowding, preferential hydration, and binding: A comparison of perspectives. 2000;97(8):3987-3992.

Sirotkin VA, Kuchierskaya AA. Lysozyme in water – acetonitrile mixtures: Preferential solvation at the inner edge of excess hydration. J. Chem. Phys. 2017;146:215101–215108.

Kirkwood JG, Buff FP. The statistical mechanical theory of solutions. J. Chem. Phys. 1951;19:774–777.

Pace CN. Measuring and increasing protein stability. Trends Biotechnol. 1990;8:93–98.

Baskakov I, Bolen DW. Forcing thermodynamically unfolded proteins to fold. J. Biol. Chem. 1998;273(9):4831-4834.

Bernfeld P. Amylases, alpha and beta. Methods. Enzymol. 1955;1:149–152.

Udema II. In vitro investigation into the effects of ethanol, aspirin, and stabilizers on mesophilic alpha amylase. Ambrose Alli University, Ekpoma; Thesis; 2013.

Stothart PH. Determination of partial specific volume and absolute concentration by densimetry. Biochem. J. 1984;219: 1049–1052.

Jeong-Bin Y, Choi SH, Lee T-H, Jan M-U, Park JM, Yi Ah-R, et al. Effects of calcium ion concentration on starch hydrolysis of barley α-Amylase isozymes. J. Microbial. Biotechnol. 2008;18(4):730-734.

Reddy SA, Sastry NG. Cation [M = H+, Li+, Na+, K+, Ca2+, Mg2+, NH4+, and NMe4+] Interactions with the aromatic motifs of naturally occurring amino acids: A theoretical study. J. Phys. Chem. A. 2005;109(39):8893-8903.

Bush DS, Sticher L, van Huystee R, Wagner D, Jones RL. The calcium requirement for stability and enzymatic activity of two isoforms of barley aleurone alpha-amylase. J. Biol. Chem. 1989; 264(32):19392-19398.

Baskakov I, Wang A, Bolen DW. Trimethlamine – N – oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: A test of the counteraction hypothesis. Biophys. J. 1998;74:2666-2673.

Kramer RM, Shende VR, Moti N, Pace NC, Scholtz MJ. Toward a molecular under-standing of protein solubility: Increased negative surface charge correlates with increased solubility. 2012;102:1907-1915.

Schurr JM, Rangel DP, Aragon SR. A contribution to the theory of preferential interaction coefficients. Proc. Natl. Acad. Sci. USA. 2005;89:2258–2276.

Danielewicz-Ferchmin, Banachowicz E, Ferchmin AR. Protein hydration and the huge electrostriction. Biophy. Chem. 2003;106:147-153.

Balos V, Boon M, Hunger J. Anionic and cationic Hofmeister effects are non-additive for guanidinium salts. Phys. Chem. Chem. Phys. 2017;19:9724-9728.

da Silva FLB, Lund M, Jönsson B, Åkesson T. On the complexation of proteins and polyelectrolytes. J. Phys. Chem. B. 2006;110:4459-4464.

Asciutto EK, General IT, Xiong K, Asher SA, Madura JD. Sodium perchlorate effects on the helical stability of a mainly alanine peptide. Biophy. J. 2010;186-196.

Davies CW. Ion association. Butterworths, London. 1962;37-53.