Effect of static magnetic field on α-amylase activity and enzymatic reaction

Abstract

The effect of magnetic field on α-amylase was studied. Under the experimental conditions, α-amylase solution was treated by 0.15 T, 0.30 T and 0.45 T static magnetic fields for a known period of time, then the activity, kinetic parameters, and the secondary conformation were investigated. The results showed that there was a considerable effect of the magnetic exposure on the α-amylase. The activity was increased by 27%, 34.1%, 37.8% compared with the control. It was also found that both kinetic parameters K _m and V _m could be decreased due to the increasing magnetic field, K _m decreased from 2.20×10⁻² to 0.87×10⁻², whereas V _m decreased from 2.0×10⁻³ g/min to 1.1×10⁻³ g/min. At the same time, there were some irregular changes in α-amylase secondary conformation.

Keywords

static magnetic field / α-amylase / activity / secondary conformation / Michaelis constant

References

[1] Chen S., Zhou R. Enzymology[M]. 2001, Shanghai: Fudan University Press.

[2] Watanabe Y., Nakagawa M., Miyakoshi Y. Enhancement of lipid peroxidation in the liver of mice exposed to magnetic fields[J]. Ind Health, 1997, 35 285-290.

[3] Beck B., Beck E., Polaniak R., et al. An effect of extremely low frequency magnetic field on alkaline phosphatase activity—in vivo and in vitro study[J]. Phys Medica, 2004, 1 28-30.

[4] Lewy H., Massot O., Touitou Y. Magnetic field (50 Hz) increases acetyltransferase hydroxy-indole-O-methyltransferase activity and melatonin release through an indirect pathway[J]. Int J Radiat Biol, 2003, 79(6): 431-435.

[5] Blank M., Soo L., Papstein V. Effects of low frequency magnetic fields on Na,K-ATPase activity[J]. Bioelectrochemistry and Bioenergetics, 1995, 38 267-273.

[6] Nazar A. S. M. I., Paul A., Dutta S. K. Frequency-dependent alteration of enolase activity by ELF fields[J]. Bioelectrochemistry and Bioenergetics, 1996, 39 259-262.

[7] Zhang Y., Tian Y., Hua Z., et al. The affection of the magnetization on the activity and stability of α-amylase[J]. Liquor Making, 2005, 132 34-36.

[8] Kalinin L. G., Boshkova I. L., Panchenko G. I., et al. The influence of a low- and high-frequency electromagnetic fields on seeds[J]. Biofizika, 2005, 50 361-366.

[9] Yan Liushui, Wei Qia, Shi Rongrong et al. Biological effect of constant magnetic field on α-amylase[J]. Journal of Nanchang Institute of Aeronautical Technology, 1996(1): 16–20(in Chinese).

[10] Bernfield P. Advances in Enzymology[M]. 1951, New York: Interscience Publication.

[11] Yankov D., Dobreva E., Beschkov V., et al. Study of optimum conditions and kinetics of starch hydrolysis by means of thermostable α-amylase[J]. Enzyme and Microbial Technology, 1986, 8(11): 665-667.

[12] Zhang J., Sun F., Chen D., et al. Studies on stability of magnetized catalase and an initial analysis of its mechanism[J]. Journal of Southwest Agricultural University, 2001, 23(3): 273-275.

[13] Vajda T. Investigation of magnetic field effect on trypsin activity[J]. Radiat Environ Biophys, 1980, 18 275-280.

[14] Luo Z., Yang J., Luo F. Properties and applications of α-amylase[J]. Food Research and Development, 2007, 28(8): 163-167.