Abstract
The influence of montmorillonite intercalated with representatives of three major classes of biological molecules-lysine (amino acid), α–glucose (carbohydrate) and rhamnolipid (lipid) on the catalytic activity of acid phosphatase was investigated. In comparison to pure clay, the presence of the organic intercalates preserves residual activity at extreme pH values of 3 and 11 and temperatures as low as 10 °C. Thermodynamic parameters of free energy, enthalpy and entropy, suggest that catalytic activity on the lysine and rhamnolipid intercalated surfaces is more spontaneous and favorable than that of pure clay. Michaelis-constants (K m values) and maximum reaction velocities (V max values) were determined and confirmed the enhancement of activity on the organo-mineral surfaces. The catalytic reaction product was measured as a function of time and the data fitted to equations describing the behavior of first and second order rates of reaction. All processes apart from the glucose-intercalated clay (second order) could be described by first order reactions. Catalytic activity was generally less on the glucose-mineral surface compared to the other organo-mineral surfaces and the pure clay. However, when all surfaces were saturated with acid phosphatase the glucose complex exhibited the highest level of catalytic activity.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Boyd S.A. and Mortland M.M. 1990. Enzyme interactions with clays and clay–organic matter complexes. In: Bollag J.M. and Stotzky G. (eds) Soil Biochemistry. Vol. 6. Marcel Dekker, New York, pp. 1–28.
Carter D.L., Mortland M.M. and Kemper W.D. 1986. In: Klute A. (ed) Physical and Mineralogical Methods. American Society of Agronomy Inc., Wisconsin,p. 419.
Cornish-Bowden A. 1979. Fundamentals of enzyme kinetics. Butterworths, London.
Dixon J.B. and White G.N. 1995. In: Soil mineralogy laboratory manual. Published by author, Soil and Crop Sciences Department, Texas A&M University.
Drapeau G. 1974. In: Lorand L. (ed) Protease from Staphylococcus aureus, Methods in Enzymology, XLVB, Wiley, New York, p. 469.
Ferris J.P. 2002. Montmorillonite catalysis of 30–50 Mer oligonucleotides: laboratory demonstration of potential steps in the origin of the RNA world. Origin. Life Evol. Bios. 32: 311–332.
Gianfreda L., Rao M.A. and Violante A. 1991. Invertase (β-Fructosidase): effects of Montmorillonite, Al-Hydroxide and Al(OH)x-Montmorillonite complex on activity and kinetic properties. Soil Biol. Biochem. 23: 581–587.
Huang P.M., Senesi N. and Buffle J. (eds), 1995. Structure and Surface Reactions of Soil Particles. Wiley, New York, pp. 449–479.
Katchalski E., Silman I. and Goldman R. 1971. Effect of the microenvironment on the mode of action of immobilized enzymes. Adv. Enzymol. 34: 445–536.
Kelleher B.P., Sutton D. and O'Dwyer T.F. 2002. The effect of kaolinite on the structural arrangements of N-Methylformamide and 1-Methyl-2-pyrrolidone. J. Colloid Interface Sci. 255: 219–224.
Khanna M., Yoder M., Calamai L. and Stotzky G. 1998. X-ray diffraction and electron microscopy of clay-DNA complexes. Sci. Soil. 3: 1–10.
Klein F., Bronsveld W., Norde W., Van Romunde L.K. and Singer J.M. 1979. A modified latex-fixation test for the detection of rheumatoid factors. J. Clin. Path. 32: 90–92.
Kobayashi Y. and Aomine S. 1967. Mechanism of inhibitory effect of allophane and montmorillonite on some enzymes. Soil Sci. Plant Nutr. 13: 180–194.
Laird D.A., Barak P., Nater E.A. and Dowdy R.H. 1991. Chemistry of smectitic and illitic phases in interstratified soil smectite. Soil Sci. Soc. Am. J. 55: 1499–1504.
Leprince F. and Quiquampoix H. 1996. Extracellular enzyme activity in soil: effect of pH and ionic strength on the interaction with montmorillonite of two acid phosphatases secreted by the ectomy-corrhizal fungus Hebeloma cylindrosporum. Eur. J. Soil Sci. 47: 511–522.
Makboul H.E. and Ottow J.C.G. 1979. Michaelis constant (Km ) of acid phosphatase as affected by montmorillonite, illite, and kaolinite clay minerals. Microb. Ecol. 5 (3): 207–213.
McLaren A.D. and Packer L. 1970. Some aspects of enzyme reactions in heterogeneous systems. Adv. Enzymol. 33: 245–308.
Nannipieri P. and Gianfreda L. 1998. Kinetics of enzyme reactions in soil environment. In: Huang P.M., Senesi N. and Buffle J. (eds), Structure and Surface Reactions of Soil Particles. Wiley, New York, pp. 449–479.
Segel I.K. 1975. Enzyme kinetics. John Wiley, New York.
Skujins J. 1976. Extracellular enzymes in soil. Crit. Rev. Microbial 4 John Wiley, New York, pp. 383–421.
Skujins J., Braal L. and McLaran A. 1962. Characterisation of phosphatase in a terrestrial soil sterilized with an electron beam. Enzymologia 25: 125–133.
Tabatabai M.A. 1982. Soil enzymes. In: Page A.L. (ed), Methods of Soils Analysis. Agronomy No. 9, Part II, 2nd edn. Soil Science Society of America, Madison, WI, pp. 903–947.
Tapp H. and Stotsky G. 1998. Persistence of the insecticidal toxins from Bacillus thuringiensis subsp. Kurstaki in soil. Soil Biol. Biochem. 30: 471–476.
Tarafdar J.C. and Marschner H. 1994. Phosphatase activity in the rhizosphere and hyphosphere of VA mycorrhizal wheat supplied with inorganic and organic phosphorus. Soil Biol. Biochem. 26: 387–395.
Theng B.K.G. 1979. Clay–organic interactions. Paper No. 5. Colloids Soils. Princ. Pract., Proc. Symp., 17 pp.
Verjee Z. 1969. Isolation of three acid phosphatases from wheat germ. Eur. J. Biochem. 9: 439–444.
Voet D. and Voet J.D. 1995. Thermodynamic Principles: A Review. In Biochemistry. 2nd edn. John Wiley & Sons, New York.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Kelleher, B.P., Willeford, K.O., Simpson, A.J. et al. Acid phosphatase interactions with organo-mineral complexes: influence on catalytic activity. Biogeochemistry 71, 285–297 (2004). https://doi.org/10.1023/B:BIOG.0000049348.53070.6f
Issue Date:
DOI: https://doi.org/10.1023/B:BIOG.0000049348.53070.6f