In-situ activity of α-amylase in the presence of controlled-frequency moderate electric fields

LWT

Volumn 90, Issue , 2018, Pages 448-454

  Samaranayake, Chaminda P ^a   Sastry, Sudhir K ^a  

^a OHIO STATE UNIVERSITY   (United States)

Author keywords

Frequency; Moderate electric fields; Starch; amylase

Indexed keywords

AMYLASES; MOLECULAR DYNAMICS; STARCH;

ALPHA-AMYLASE ACTIVITY; DISPLACEMENT APPROACHES; EFFECTS OF ELECTRIC FIELDS; ELECTRIC FIELD FREQUENCY; FREQUENCY; INTERMOLECULAR SPACINGS; MOLECULAR DYNAMICS SIMULATIONS; OSCILLATORY BEHAVIORS;

ELECTRIC FIELDS;

EID: 85039928347     PISSN: 00236438     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lwt.2017.12.053     Document Type: Article

References (37)

1. Aibara, S., Esaki, K., Effects of high-voltage electric field treatment on bread starch. Bioscience Biotechnology & Biochemistry 62:11 (1998), 2194–2198.
2. Alikhajeh, J., Khajeh, K., Ranjbar, B., Naderi-Manesh, H., Lin, Y.H., Liu, M.Y., et al. High resolution crystal structure of Bacillus amyloliquifaciens alpha-amylase. RCSB Protein Data Bank, 2007, 10.2210/pdb3bh4/pdb.
3. Alikhajeh, J., Khajeh, K., Ranjbar, B., Naderi-Manesh, H., Lin, Y.H., Liu, E., et al. Structure of Bacillus amyloliquefaciens α-amylase at high resolution: Implications for thermal stability. Acta Crystallographica Section F 66:2 (2010), 121–129.
4. Anonymous, Nomenclature committee of the international union of biochemistry (NC-IUB). Units of enzyme activity: Recommendations 1978. European Journal of Biochemistry 97 (1979), 319–320.
5. Astrakas, L.G., Gousias, C., Tzaphlidou, M., Structural destabilization of chignolin under the influence of oscillating electric fields. Journal of Applied Physics, 111(074702), 2012.
6. BeMiller, J.N., Whistler, R.L., Carbohydrates. Fennema, O.R., (eds.) Food Chemistry, 1996, Marcel Dekker, Inc, New York, 157–223.
7. Castro, I., Macedo, B., Teixeira, J.A., Vicente, A.A., The effect of electric field on important food-processing enzymes: Comparison of inactivation kinetics under conventional and ohmic heating. Journal of Food Science 69:9 (2004), C696–C701.
8. Chopra, H.K., Panesar, P.S., Panesar, R., Marwaha, S.S., Dua, A., Kennedy, J.F., Immobilized enzymes in food processing. Panesar, P.S., Marwaha, A.S., Chopra, H.K., (eds.) Enzymes in food Processing: Fundamentals and potential applications, 2010, I. K. International Publishing House Pvt. Ltd, New Delhi, India, 259–290.
9. Durham, E.K., Moderate electric field treatment for saccharification of cellulose materials. (Ph. D. Dissertation), 2015, The Ohio State University, Columbus.
10. Fu, L., X-Ray study of the structure of liquid water. (Ph.D. Dissertation), 2008, Stanford University, Stanford.
11. Fuwa, H., A new method for microdetermination of amylase activity by the use of amylose as the substrate. The Journal of Biochemistry 41:5 (1954), 583–603.
12. Hill, T.L., Some possible biological effects of an electric field acting on nucleic acids or proteins. Journal of the American Chemical Society 80:9 (1958), 2142–2147.
13. Huggins, C., Russell, P., Colorimetric determination of amylase. Annals of Surgery 128:4 (1948), 668–678.
14. Jakob, A., Bryjak, J., Wojtowicz, H., Illeova, V., Annus, J., Polakovic, M., Inactivation kinetics of food enzymes during ohmic heating. Food Chemistry 123 (2010), 369–376.
15. Jalte, M., Lanoiselle, J.-L., Lebovka, N.I., Vorobiev, E., Freezing of potato tissue pre-treated by pulsed electric fields. LWT-Food Science and Technology 42 (2009), 576–580.
16. Janecek, S., Svensson, B., MacGregor, E.A., α-amylase: An enzyme specificity found in various families of glycoside hydrolases. Cellular and Molecular Life Sciences 71 (2014), 1149–1170.
17. Janositz, A., Noack, A.-K., Knorr, D., Pulsed electric fields and their impact on the diffusion characteristics of potato slices. LWT-Food Science and Technology 44 (2011), 1939–1945.
18. Kouzaev, G.A., Applications of advanced Electromagnetics: Components and systems. 2013, Springer, New York.
19. Kulp, K., Carbohydrases. Reed, G., (eds.) Enzymes in food processing, 1975, Academic Press, New York, 54–117.
20. th ed., 2003-2004, CRC Press LLC, Boca Raton.
21. Liu, H.-L., Chen, W.-J., Chou, S.-N., Mechanisms of aggregation of alpha- and beta-amylases in aqueous dispersions. Colloids and Surfaces B: Biointerfaces 28 (2003), 215–225.
22. Liu, D., Wu, Q., Chen, H., Chang, P.R., Transitional properties of starch colloid with particle size reduction from micro- to nanometer. Journal of Colloid and Interface Science 339 (2009), 117–124.
23. Li, D., Yang, N., Zhou, X., Jin, Y., Guo, L., Xie, Z., et al. Characterization of acid hydrolysis of granular potato starch under induced electric field. Food Hydrocolloids 71 (2017), 198–206.
24. van der Maarel, M.J.E.C., van der Veen, B., Uitdehaag, J.C.M., Leemhuis, H., Dijkhuizen, L., Properties and applications of starch-converting enzymes of the α-amylase family. Journal of Biotechnology 94 (2002), 137–155.
25. Neumann, E., Elementary analysis of chemical electric field effects in biological macromolecules: II. Kinetic aspects of electro-optic and conductometric relaxations. Gutmann, F., Keyzer, H., (eds.) Modern bioelectrochemistry, 1986, Plenum Press, New York, 133–174.
26. Ohshima, T., Tamura, T., Sato, M., Influence of pulsed electric field on various enzyme activities. Journal of Electrostatics 65 (2007), 156–161.
27. Pereira, R.N., Teixeira, J.A., Vicente, A.A., Exploring the denaturation of whey proteins upon application of moderate electric fields: A kinetic and thermodynamic study. Journal of Agricultural and Food Chemistry 59 (2011), 11589–11597.
28. Russell, P.J., Hertz, P.E., McMillan, B., Biology: The dynamic science. 4th ed., 2017, Cengage Learning, Boston (Chapter 3).
29. Samaranayake, C.P., Sastry, S.K., Electrode and pH effects on electrochemical reactions during ohmic heating. Journal of Electroanalytical Chemistry 577 (2005), 125–135.
30. Samaranayake, C.P., Sastry, S.K., Effects of controlled-frequency moderate electric fields on pectin methylesterase and polygalacturonase activities in tomato homogenate. Food Chemistry 199 (2016), 265–272.
31. Samaranayake, C.P., Sastry, S.K., Effect of moderate electric fields on inactivation kinetics of pectin methylesterase in tomatoes: The roles of electric field strength and temperature. Journal of Food Engineering 186 (2016), 17–26.
32. Schwan, H.P., Alternating current spectroscopy of biological substances. Proceedings of the IRE 47:11 (1959), 1841–1855.
33. Singh, A., Orsat, V., Raghavan, V., Soybean hydrophobic protein response to external electric field: A molecular modeling approach. Biomolecules 3 (2013), 168–179.
34. Sundarram, A., Murthy, T.P.K., α-amylase production and applications: A review. Journal of Applied & Enveronmental Microbiology 2:4 (2014), 166–175.
35. Teixeira, J., Luzar, A., Physics of liquid Water: Structure and dynamics. Bellissent-Funel, M.-C., (eds.) Hydration processes in Biology: Theoretical and experimental approaches, 1999, IOS Press, Amsterdam, 35–63.
36. Tian, M., Fang, T., Du, M., Zhang, F., Effects of pulsed electric field (PEF) treatment on enhancing activity and conformation of α-amylase. The Protein Journal 35 (2016), 154–162.
37. Xiao, Z., Storms, R., Tsang, A., A quantitative starch-iodine method for measuring alpha-amylase and glucoamylase activities. Analytical Biochemistry 351 (2006), 146–148.