Open Access Peer-reviewed Research Article

Biosensor for maltose quantification and estimation of maltase activity

Main Article Content

Elena V. Emelyanova corresponding author

Abstract

The aim of this study was to create a laboratory model of an amperometric microbial biosensor for maltose quantification in the presence and absence of starch and to estimate the use of the model in the study of maltase activity of the culture-receptor. The biosensor for maltose was developed on the basis of a Clark-type oxygen electrode, coupled with a bioreceptor, which contained bacterial cells immobilized on the membrane. The determination of maltose concentration was based on measuring the rate of electrode current change in response to addition of the analyte. The detection limit of the biosensor was 1 µM maltose, a linear interval of standard curve was observed from 14 µM up to 1.9 mM of maltose. The microbial biosensor demonstrated good sensitivity to maltose, 36.02 nА (M·s)-1. Combination of bioreceptors on the basis of fungus and bacterium allowed of using the biosensor for quantification of maltose in the presence of starch. Changes in metabolism of the culture-receptor had an effect on the biosensor response. It indicated that the developed model was a tool of simple construction and easy-to-use in the study of maltase activity of the immobilized culture-receptor.

Keywords
Amperometric microbial biosensor, Clark-type oxygen electrode, maltose determination, maltase, starch

Article Details

How to Cite
Emelyanova, E. V. (2019). Biosensor for maltose quantification and estimation of maltase activity. Advances in Biochips, 1(1), 2-11. https://doi.org/10.25082/AB.2019.01.001

References

  1. Skryabin G and Golovleva L. Microorganisms in organic chemistry, "Nauka", Moscow (in Russian), 1976.
  2. Mfomber PM and Senwo ZN. Soil maltase activity by a glucose oxidase-perioxidase system. Biotech, 2012, 2: 225-231. https://doi.org/10.1007/s13205-012-0050-z
  3. Thirunavukkarasu M and Priest FG. Purification and characterization of an extracellular and a cellular α-glucosidase from Bacillus licheniformis. Journal of General Microbiology, 1984, 130: 3135-3141. https://doi.org/10.1099/00221287-130-12-3135
  4. Aoki K, Uchida H, Katsube T, et al. Integration of bienzymatic disaccharide sensors for simultaneous determination of disaccharides by means of light addressable potentiometric sensor. Analytica Chimica. Acta, 2002, 471: 3-12. https://doi.org/10.1016/S0003-2670(02)00921-2
  5. Gondo S, Kim C, Hirata, et al. Studies on dynamic behavior of the biosensor based on immobilized glucoamylase-glucose oxidase membrane. Biosensors and Bioelectronics, 1997, 12: 395-401. https://doi.org/S0956-5663(96)00082-6
  6. Kullick T, Bock U, Schubert J, et al. Application of enzyme-field effect transistor sensor arrays as detectors in a flow-injection analysis system for simultaneous monitoring of medium components. Part II. Monitoring of cultivation processes. Analytica Chi mica. Act a, 1995, 300: 25-31. https://doi.org/10.1016/0003-2670(94)00376-W
  7. Menzel C, Lerch T, Scheper T, et al. Development of biosensors based on an electrolyte isolator semiconductor (EIS)-capacitor structure and their application for process monitoring part i. development of the biosensors and their characterization. Analytica Chimica. Acta, 1995, 317: 259-264. https://doi.org/10.1016/0003-2670(95)00419-X
  8. Mori T, Motonaga T and Okahata Y. Cast films of lipid-coated enzymes as selective sensors for disaccharides. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 1999, 146: 387-395. https://doi.org/10.1016/S0927-7757(98)00808-5
  9. Pyeshkova V, Saiapina O, Soldatkin O, et al. Enzyme conductometric biosensor for maltose determination. Biopolymers and Cell, 2009, 25: 272-278. https://doi.org/10.7124/bc.0007E6
  10. Sun C, Zhang X, Jiang D, et al. Electrocatalytic oxidation of carbohydrates at a molecular deposition film electrode based on water-soluble cobalt phthalocyanine and its application to flow-through detection. Journal of Electroanalytical Chemistry, 1996, 411: 73-78. https://doi.org/10.1016/0022-0728(96)04563-9
  11. Tessema M, Ruzgas T, Gorton L, et al. Flow injection amperometric determination of glucose and some other low molecular weight saccharides based on oligosaccharide dehydrogenase mediated by benzoquinone systems. Analytica Chimica. Acta, 1995, 310: 161-171. https://doi.org/10.1016/0003-2670(95)00111-C
  12. Filipiak M, Fludra K and Gosciminska E. Enzymatic membranes for determination of some disaccharides by means of an oxygen electrode. Biosensors and Bioelectronics, 1996, 11: 355-364. https://doi.org/10.1016/0956-5663(96)82731-X
  13. Ge F, Zhang X E, Zhang P, et al. Simultaneous determination of maltose and glucose using a screen-printed electrode system. Biosensors and Bioelectronics, 1998, 13: 333-339. https://doi.org/10.1016/S0956-5663(97)00122-X
  14. Varadi M, Àdanyi N, Nagy G, et al. Studying the bienzyme reaction with amperometric detection for measuring maltose. Biosensors and Bioelectronics, 1993, 8: 339-345. https://doi.org/10.1016/0956-5663(93)85015-G
  15. Zajoncova L, Jilek M, Beranova V, et al. A biosensor for the determination of amylase activity. Biosensors and Bioelectronics, 2004, 20: 240-245. https://doi.org/10.1016/j.bios.2004.01.006
  16. Riedel K, Lehmann M, Adler K, et al. Physiological characterization of a microbial sensor containing the yeast Arxula adeninivorans LS3. Antonie Van Leeuwenhoek, 1997, 71: 345-351. https://doi.org/10.1023/A:1000231111592
  17. Khan AA and Eaton NR. Purification and characterization of maltase and α-methil glucosidase from yeast. Biochimica et Biophysica Acta, 1967, 146: 173-180. https://doi.org/10.1016/0005-2744(67)90084-8
  18. Emelyanova E. Aerobic microorganisms are the bases for biosensors for starch and maltose detection, Proceedings of XIII Congress of S.N.Vinogradskyj society of microbiologists of Ukraine, Yalta, Russia, 2013: 378.
  19. Riedel K, Renneberg R, Wollenberger U, et al. Microbial sensors: fundamentals and application for process control. Journal of Chemical Technology and Biotechnology, 1989, 44: 85-106. https://doi.org/10.1002/jctb.280440202
  20. Baronas R, Ivanauskas F and Kulys J. The influence of the enzyme membrane thickness on the response of amperometric biosensors. Sensors, 2003, 3: 248-262. https://doi.org/10.3390/s30700248
  21. Berezin I and Klesov A. Practical course of chemical and enzyme kinetics, Moscow University Press, Moscow, Russian, 1976.
  22. Emelyanova E and Reshetilov A. Estimation of diffusion for different receptor elements of a microbial biosensor, Physics and Radioelectronics in Medicine and Ecology PHRЕME 2016, Proc. XII International Scientific Conference, Vladimir-Suzdal, Russia. Book II, 2016: 166-169.
  23. Turner APF, Karube I and Wilson GS. Biosensors: Fundamentals and applications, Oxford University Press, New York, US, 1987.
  24. Solyanikova I, Borzova O and Emelyanova E. Kinetics of interaction between substrates/substrate analogs and benzoate 1,2-dioxygenase from benzoate-degrading Rhodococcus opacus 1CP. Folia Microbiology, 2017, 62: 355-362. https://doi.org/10.1007/s12223-017-0505-z
  25. Wang LH and Hartman PA. Purification and some properties of an extracellular maltase from Bacillus subtilis. Applied and Environmental Microbiology, 1976, 31: 108-118.
  26. Olusanya O and Olutiola PO. Characterisation of maltase from enteropathogenic Escherichia coli. FEMS Microbiology Letters, 1986, 36: 239-244. https://doi.org/10.1111/j.1574-6968.1986.tb01702.x
  27. Needleman RB, Federoff HJ, Eccleshall TR, et al. Purification and characterization of an α-glucosidase from Saccharomyces carlsbergensis. Biochemistry, 1978, 17: 4657-4661. https://doi.org/10.1021/bi00615a011
  28. McWethy SJ and Hartman PA. Extracellular maltase of Bacillus brevis. Applied and Environmental Microbiology, 1979: 1096-1102.
  29. Guffanti AA and Corpe WA. Partial purification and characterization of alfa-glucosidase from Pseudomonas fluorescens W. Archives of Microbiology, 1976, 107: 269-276. PMID: 818970.
  30. Dawson R, Elliot D, Elliot W, et al. Data for biochemical research, Clarendon Press, Oxford, 1986.
  31. Sugimoto T, Amemura A and Harada Y. Formations of extracellular isoamylase and intracellular α-glucosidase and amylase(s) by Pseudomonas SB15 and a mutant strain. Applied Microbiology, 1974, 28: 336-339.
  32. Shuman HA and Beckwith J. Escherichia coli K-12 mutants that allow transport of maltose via the β-galactoside transport system. Journal of Bacteriology, 1979, 137: 365-373.
  33. Braitsch M, Kählig H, Kontaxis G, et al. Synthesis of fluorinated maltose derivatives for monitoring protein interaction by 19F NMR. Beilstein Journal of Organic Chemistry, 2012: 448-455. https://doi.org/10.3762/bjoc.8.51
  34. Bao H and Duong F. Discovery of an auto-regulation mechanism for the maltose ABC transporter MaIFGK2. PLOS ONE, 2012, 7(4): e34836. https://doi.org/10.1371/journal.pone.0034836
  35. Guffanti AA and Corpe WA. Maltose metabolism of Pseudomonas fluorescens. Journal of Bacteriology, 1975, 124: 262-268.
  36. Yoshigi N, Chikano T and Kamimura M. Purification and properties of an amylase from Bacillus cereus NY-14. Agricultural and Biological Chemistry, 1985, 49: 3369-3376. https://doi.org/10.1271/bbb1961.49.3369