Advertisement

3 Biotech

, 9:124 | Cite as

Inhibition assays of free and immobilized urease for detecting hexavalent chromium in water samples

  • Rushikesh Fopase
  • Suman Nayak
  • Monalisha Mohanta
  • Paresh Kale
  • Balasubramanian ParamasivanEmail author
Original Article
  • 47 Downloads

Abstract

The present work describes the inhibition studies of free as well as immobilized urease by different heavy metals. Porous silicon (PS) films prepared by electrochemical etching were used for urease immobilization by physical adsorption. The enzyme was subjected to varying concentrations of Cr6+, Cr3+, Cu2+, Fe2+, Cd2+ and Ni2+ and analyzed for the variation in the activity. To study the effect of other heavy metals on the interaction of urease and Cr6+, free as well as immobilized urease was subjected to the combination of each metal ion with Cr6+. Results proved the sensitivity of free as well as immobilized urease towards heavy metals by observed reduction in activity. Immobilized urease showed less degree of inhibition compared to free urease when tested for inhibition by individual metal ions and in combination with Cr6+. IC50 values were found higher for inhibition by the combination of metal ions with Cr6+. Interaction of heavy metal ions with functional groups in active site of urease and limitations of mass transfer are the two factors responsible for the variation in activity of urease. Relation between the variation of urease activity and amount of heavy metals can be applied in biosensor development for determining the concentration of Cr6+ present in the water samples.

Keywords

Urease Immobilization Porous silicon Chromium Heavy metals Urease inhibition 

Notes

Acknowledgements

The authors gratefully acknowledge the Department of Science and Technology (DST), India for funding the research under DST-WTI (Water Technology Initiative) (WTI/2015/113). The authors thank the Department of Biotechnology and Medical Engineering and the Department of Electrical Engineering of National Institute of Technology Rourkela, India for providing the research facility.

Compliance with ethical standards

Conflict of interest

The authors declare no conflict of interest to disclose.

References

  1. Ali Khan A, Alzohairy MA (2010) Recent advances and applications of immobilized enzyme technologies: a review. Res J Biol Sci 5(8):565–575.  https://doi.org/10.3923/rjbsci.2010.565.575 CrossRefGoogle Scholar
  2. Attar A, Emilia Ghica M, Amine A, Brett CMA (2014) Poly(neutral red) based hydrogen peroxide biosensor for chromium determination by inhibition measurements. J Hazard Mater 279:348–355.  https://doi.org/10.1016/J.JHAZMAT.2014.07.019 CrossRefPubMedGoogle Scholar
  3. Behbehani GR, Barzegar L, Mohebbian M (2012) Strong inhibition of jack bean urease by chromium (III). Biosci Biotechnol Res Asia 9(2):2–6CrossRefGoogle Scholar
  4. Benkovic SJ, Hammes-Schiffer S, Karplus M, Truhlar DG (2003) A perspective on enzyme catalysis. Science 301(5637):1196–1202.  https://doi.org/10.1126/science.1085515 CrossRefPubMedGoogle Scholar
  5. Biswas P, Karn AK, Balasubramanian P, Kale PG (2017) Biosensor for detection of dissolved chromium in potable water: a review. Biosens Bioelectron 94:589–604.  https://doi.org/10.1016/j.bios.2017.03.043 CrossRefPubMedGoogle Scholar
  6. Chaudhari PS, Gokarna A, Kulkarni M, Karve MS, Bhoraskar SV (2005) Porous silicon as an entrapping matrix for the immobilization of urease. Sens Actuators B Chem 107:258–263.  https://doi.org/10.1016/j.snb.2004.10.009 CrossRefGoogle Scholar
  7. Chen L, Zhang J, Zhu Y, Zhang Y (2018) Interaction of chromium(III) or chromium(VI) with catalase and its effect on the structure and function of catalase: an in vitro study. Food Chem 244:378–385.  https://doi.org/10.1016/j.foodchem.2017.10.062 CrossRefPubMedGoogle Scholar
  8. Choi J-M, Han S-S, Kim H-S (2015) Industrial applications of enzyme biocatalysis: current status and future aspects. Biotechnol Adv 33:1443–1454.  https://doi.org/10.1016/J.BIOTECHADV.2015.02.014 CrossRefPubMedGoogle Scholar
  9. Daneshjou S, Dabirmanesh B, Rahimi F, Khajeh K (2017) Porous silicon nanoparticle as a stabilizing support for chondroitinase. Int J Biol Macromol 94:852–858.  https://doi.org/10.1016/j.ijbiomac.2016.10.077 CrossRefPubMedGoogle Scholar
  10. Dhanekar S, Jain S (2013) Porous silicon biosensor: Current status. Biosens Bioelectron 41:54–64.  https://doi.org/10.1016/j.bios.2012.09.045 CrossRefPubMedGoogle Scholar
  11. Do JS, Lin KH (2016) Kinetics of urease inhibition-based amperometric biosensors for mercury and lead ions detection. J Taiwan Inst Chem Eng 63:25–32.  https://doi.org/10.1016/j.jtice.2016.03.011 CrossRefGoogle Scholar
  12. Domínguez Renedo O, Lomillo A, Arcos Martinez MA, M.J (2004) Optimisation procedure for the inhibitive determination of chromium(III) using an amperometric tyrosinase biosensor. Anal Chim Acta 521:215–221.  https://doi.org/10.1016/J.ACA.2004.06.026 CrossRefGoogle Scholar
  13. Domínguez-Renedo O, Alonso-Lomillo MAA, Ferreira-Gonçalves L, Arcos-Martínez MJJ (2009) Development of urease based amperometric biosensors for the inhibitive determination of Hg (II). Talanta 79:1306–1310.  https://doi.org/10.1016/j.talanta.2009.05.043 CrossRefPubMedGoogle Scholar
  14. Erickson HP (2009) Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy. Biol Proced Online 11:32–51.  https://doi.org/10.1007/s12575-009-9008-x CrossRefPubMedPubMedCentralGoogle Scholar
  15. Fernandez RE, Bhattacharya E, Chadha A (2008) Covalent immobilization of Pseudomonas cepacia lipase on semiconducting materials. Appl Surf Sci 254:4512–4519.  https://doi.org/10.1016/j.apsusc.2008.01.099 CrossRefGoogle Scholar
  16. Follmer C, Carlini CR (2005) Effect of chemical modification of histidines on the copper-induced oligomerization of jack bean urease (EC 3.5.1.5). Arch Biochem Biophys 435:15–20.  https://doi.org/10.1016/j.abb.2004.12.001 CrossRefPubMedGoogle Scholar
  17. Fopase R, Nayak S, Mohanta M, Kale P, Balasubramanian P (2019) Inhibition assays of urease for detecting trivalent chromium in drinking water. In: Green buildings and sustainable engineering. Springer, Singapore, pp 313–323CrossRefGoogle Scholar
  18. Gumpu MB, Sethuraman S, Krishnan UM, Rayappan JBB (2015) A review on detection of heavy metal ions in water—an electrochemical approach. Sens Actuators B Chem 213:515–533.  https://doi.org/10.1016/j.snb.2015.02.122 CrossRefGoogle Scholar
  19. Hartmann M, Jung D (2010) Biocatalysis with enzymes immobilized on mesoporous hosts: the status quo and future trends. J Mater Chem 20:844–857.  https://doi.org/10.1039/B907869J CrossRefGoogle Scholar
  20. Jesionowski T, Zdarta J, Krajewska B (2014) Enzyme immobilization by adsorption: a review. Adsorption 20:801–821.  https://doi.org/10.1007/s10450-014-9623-y CrossRefGoogle Scholar
  21. Jing C, Wang C, Yan K, Zhao K, Sheng G, Qu D, Niu F, Zhu H, You Z (2016) Synthesis, structures and urease inhibitory activity of cobalt(III) complexes with Schiff bases. Bioorganic Med Chem 24:270–276.  https://doi.org/10.1016/j.bmc.2015.12.013 CrossRefGoogle Scholar
  22. Khaldi K, Sam S, Lounas A, Yaddaden C, Gabouze NE (2017) Comparative investigation of two methods for acetylcholinesterase enzyme immobilization on modified porous silicon. Appl Surf Sci 421:148–154.  https://doi.org/10.1016/j.apsusc.2016.12.169 CrossRefGoogle Scholar
  23. Krajewska B (2008) Mono- (Ag, Hg) and di- (Cu, Hg) valent metal ions effects on the activity of jack bean urease. Probing the modes of metal binding to the enzyme. J Enzyme Inhib Med Chem 23:535–542.  https://doi.org/10.1080/14756360701743051 CrossRefPubMedGoogle Scholar
  24. Krajewska B, Brindell M (2016) Thermodynamic study of competitive inhibitors’ binding to urease. J Therm Anal Calorim 123:2427–2439.  https://doi.org/10.1007/s10973-015-5145-4 CrossRefGoogle Scholar
  25. Li HL, Zhu Y, Xu D, Wan Y, Xia L, Zhao XS (2009) Vapor-phase silanization of oxidized porous silicon for stabilizing composition and photoluminescence. J Appl Phys 105.  https://doi.org/10.1063/1.3133209 CrossRefGoogle Scholar
  26. Li G, Xiao F, Liao S, Chen Q, Zhou J, Wu Z, Yu R (2018) Label-free 2D colloidal photonic crystal hydrogel biosensor for urea and urease inhibitor. Sens Actuators B Chem 277:591–597.  https://doi.org/10.1016/j.snb.2018.09.059 CrossRefGoogle Scholar
  27. Liu D, Yin A, Chen K, Ge K, Lihua L, Nie N, Yao S (1995) Determination of trace levels of mercury(II) based on the inhibition of urease using a saw/impedance enzyme transducer. Anal Lett 28:vii–xiii.  https://doi.org/10.1080/00032719508006396 CrossRefGoogle Scholar
  28. Magomya A, Barminas J, Osemeahon S (2017) Assessment of metal-induced inhibition of soybean urease as a tool for measuring heavy metals in aqueous samples. IOSR J Appl Chem 10:61–70.  https://doi.org/10.9790/5736-1006026170 CrossRefGoogle Scholar
  29. Marchenko SV, Soldatkin OO, Kolomiets LA, Kornelyuk OI, Soldatkin AP (2018) Cyclodextrins application in urease-based biosensor for urea determination. Sens Lett 16:298–303.  https://doi.org/10.1166/sl.2018.3955 CrossRefGoogle Scholar
  30. Moyo M, Okonkwo JO, Agyei NM (2014) An amperometric biosensor based on horseradish peroxidase immobilized onto maize tassel-multi-walled carbon nanotubes modified glassy carbon electrode for determination of heavy metal ions in aqueous solution. Enzyme Microb Technol 56:28–34.  https://doi.org/10.1016/J.ENZMICTEC.2013.12.014 CrossRefPubMedGoogle Scholar
  31. Nepomuscene NJ, Daniel D, Krastanov A (2007) Biosensor to detect chromium in wastewater. Biotechnol Biotechnol Equip 21:377–381.  https://doi.org/10.1080/13102818.2007.10817477 CrossRefGoogle Scholar
  32. Oehlschläger K, Hüttl R, Wolf G (1998) Calorimetric investigations of urease inhibition by heavy metal ions. Thermochim Acta 310:185–189.  https://doi.org/10.1016/S0040-6031(97)00395-X CrossRefGoogle Scholar
  33. Pan L, Wang C, Yan K, Zhao K, Sheng G, Zhu H, Zhao X, Qu D, Niu F, You Z (2016) Synthesis, structures and Helicobacter pylori urease inhibitory activity of copper(II) complexes with tridentate aroylhydrazone ligands. J Inorg Biochem 159:22–28.  https://doi.org/10.1016/j.jinorgbio.2016.02.017 CrossRefPubMedGoogle Scholar
  34. Pearson RG (1968) Hard and soft acids and bases, HSAB, Part I fundamental principles. J Chem Educ 45:581–587CrossRefGoogle Scholar
  35. Preininger C, Wolfbeis OS (1996) Disposable cuvette test with integrated sensor layer for enzymatic determination of heavy metals. Biosens Bioelectron 11:981–990.  https://doi.org/10.1016/0956-5663(96)87657-3 CrossRefGoogle Scholar
  36. Saleem M, Rafiq M, Seo S-Y, Lee KH (2016) Acetylcholinesterase immobilization and characterization, and comparison of the activity of the porous silicon-immobilized enzyme with its free counterpart. Biosci Rep 36:e00311–e00311.  https://doi.org/10.1042/BSR20150154 CrossRefPubMedPubMedCentralGoogle Scholar
  37. Sang LC, Vinu A, Coppens MO (2011) General description of the adsorption of proteins at their iso-electric point in nanoporous materials. Langmuir 27:13828–13837.  https://doi.org/10.1021/la202907f CrossRefPubMedGoogle Scholar
  38. Shaw WHR, Raval DN (1961) The inhibition of urease by metal ions at pH 8.9. J Am Chem Soc 83:3184–3187CrossRefGoogle Scholar
  39. Smith RG, D’Souza N, Nicklin S (2008) A review of biosensors and biologically-inspired systems for explosives detection. Analyst 133:571.  https://doi.org/10.1039/b717933m CrossRefPubMedGoogle Scholar
  40. Soni A, Surana RK, Jha SK (2018) Smartphone based optical biosensor for the detection of urea in saliva. Sens Actuators B Chem 269:346–353.  https://doi.org/10.1016/j.snb.2018.04.108 CrossRefGoogle Scholar
  41. Syshchyk O, Skryshevsky VA, Soldatkin OO, Soldatkin AP (2015) Enzyme biosensor systems based on porous silicon photoluminescence for detection of glucose, urea and heavy metals. Biosens Bioelectron 66:89–94.  https://doi.org/10.1016/j.bios.2014.10.075 CrossRefPubMedGoogle Scholar
  42. Thust M, Schöning MJ, Frohnhoff S, Arens-Fischer R, Kordos P, Lüth H (1996) Porous silicon as a substrate material for potentiometric biosensors. Meas Sci Technol 7:26–29.  https://doi.org/10.1088/0957-0233/7/1/003 CrossRefGoogle Scholar
  43. Toren EC, Burger FJ (1968) Trace determination of metal ion inhibitors of the glucose-glucose oxidase system. Mikrochim Acta 56:1049–1058.  https://doi.org/10.1007/BF01224060 CrossRefGoogle Scholar
  44. Vaghela C, Kulkarni M, Haram S, Aiyer R, Karve M (2018) A novel inhibition based biosensor using urease nanoconjugate entrapped biocomposite membrane for potentiometric glyphosate detection. Int J Biol Macromol 108:32–40.  https://doi.org/10.1016/J.IJBIOMAC.2017.11.136 CrossRefPubMedGoogle Scholar
  45. Vaidya AM, Annapure US (2019) Enzymes in biosensors for food quality assessment. Enzym Food Biotechnol 32:659–674.  https://doi.org/10.1016/B978-0-12-813280-7.00038-4 CrossRefGoogle Scholar
  46. Vemulachedu H, Fernandez RE, Bhattacharya E, Chadha A (2009) Miniaturization of EISCAP sensor for triglyceride detection. J Mater Sci Mater Med 20:S229–S234.  https://doi.org/10.1007/s10856-008-3534-y CrossRefPubMedGoogle Scholar
  47. Volotovsky V, Kim N (1997) Urease-based biosensor for mercuric ions determination. Sens Actuators B Chem 42:233–237.  https://doi.org/10.1016/S0925-4005(97)80340-1 CrossRefGoogle Scholar
  48. Wieczorek K, Wyszkowska J, Kucharski J (2015) Sensitivity of soil urease to soil contamination by zinc, copper, nickel, cadmium and lead. Fresenius Environ Bull 24:2496–2504Google Scholar
  49. Yue L-M, Lee J, Lü Z-R, Yang J-M, Ye Z-M, Park Y-D (2017) Effect of Cd2+ on tyrosinase: Integration of inhibition kinetics with computational simulation. Int J Biol Macromol 94:836–844.  https://doi.org/10.1016/J.IJBIOMAC.2016.09.001 CrossRefPubMedGoogle Scholar
  50. Yun D, Song MJ, Hwang S, Hong SI (2012) Fabrication and electrochemical characterization of nanoporous silicon electrode for Amperometric urea biosensor. Jpn J Appl Phys 51:06FG02.  https://doi.org/10.1143/JJAP.51.06FG02 CrossRefGoogle Scholar
  51. Zaborska WX, Krajewska B, Leszko M, Olech Z (2001) Inhibition of urease by Ni2+ ions. Analysis of reaction progress curves. J Mol Catal B Enzym 13:103–108.  https://doi.org/10.1016/S1381-1177(00)00234-4 CrossRefGoogle Scholar
  52. Zhang HM, Zhang GC, Wang YQ (2011) The interaction of chromium(VI) with urease in solution. Biol Trace Elem Res 141:53–64.  https://doi.org/10.1007/s12011-010-8718-x CrossRefPubMedGoogle Scholar
  53. Zheng M, Mao L, Huang F, Xiang X, Deng Q, Feng Y (2015a) A mixed-function-grafted magnetic mesoporous hollow silica microsphere immobilized lipase strategy for ultrafast transesterification in a solvent-free system. RSC Adv 5:43074–43080.  https://doi.org/10.1039/C5RA05611J CrossRefGoogle Scholar
  54. Zheng M, Zhu J, Huang F, Xiang X, Shi J, Deng Q, Ma F, Feng Y (2015b) Enzymatic deacidification of the rice bran oil and simultaneous preparation of phytosterol esters-enriched functional oil catalyzed by immobilized lipase arrays. RSC Adv 5:70073–70079.  https://doi.org/10.1039/C5RA11533G CrossRefGoogle Scholar
  55. Zheng M, Xiang X, Wang S, Shi J, Deng Q, Huang F, Cong R (2017) Lipase immobilized in ordered mesoporous silica: a powerful biocatalyst for ultrafast kinetic resolution of racemic secondary alcohols. Process Biochem 53:102–108.  https://doi.org/10.1016/J.PROCBIO.2016.12.005 CrossRefGoogle Scholar
  56. Zhou Z, Hartmann M (2013) Progress in enzyme immobilization in ordered mesoporous materials and related applications. Chem Soc Rev 42:3894–3912.  https://doi.org/10.1039/c3cs60059a CrossRefPubMedGoogle Scholar
  57. Zhou Y, Li Y-S, Tian X-L, Zhang Y-Y, Yang L, Zhang J-H, Wang X-R, Lu S-Y, Ren H-L, Liu Z-S (2012) Enhanced ultrasensitive detection of Cr(III) using 5-thio-2-nitrobenzoic acid (TNBA) and horseradish peroxidase (HRP) dually modified gold nanoparticles (AuNPs). Sens Actuators B Chem 161:1108–1113.  https://doi.org/10.1016/J.SNB.2011.12.035 CrossRefGoogle Scholar

Copyright information

© King Abdulaziz City for Science and Technology 2019

Authors and Affiliations

  1. 1.Department of Biotechnology and Medical EngineeringNational Institute of Technology RourkelaOdishaIndia
  2. 2.Department of Electrical EngineeringNational Institute of Technology RourkelaOdishaIndia

Personalised recommendations