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Aspartic acid introduce the functional amine groups on the surface of superparamagnetic Fe(OH)3@Fe3O4 nanoparticles for efficient immobilization of Penaeus vannamei protease

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Abstract

In this study, we synthesized super magnetic Fe(OH)3@Fe3O4 nanoparticles (SPIONs) by the co-precipitation method and introduction of amine groups via chemisorption of l-aspartic acid (LAA) on the surface of SPIONs. Penaeus vannamei protease (PVP) was immobilized onto amine-functionalized supermagnetic nanoparticles (ASPIONs), and conditions affecting PVP immobilization were investigated. PVP immobilized onto ASPIONs exhibited shifts in both working optimum pH and temperature with an increase from pH 7 to pH 8, and increased optimum temperature by 10 °C compared to free enzyme. Similarly, the thermal, pH, and storage stabilities of the immobilized PVP were superior to those of free form of the enzyme. In comparison to the free enzyme, the immobilized enzyme was reusable for 15 cycles while retaining 73% of its initial activity. The Michaelis–Menten kinetic constant (Km) and maximum reaction velocity (Vmax) for free PVP were 2.3 µM and 88 µM min−1, respectively, whereas Km and Vmax values of immobilized enzyme were 2.5 µM and 85 µM min−1, respectively. These results indicated that immobilized PVP was efficient in terms of catalytic activity and can be applied to continuous casein processing applications in the different industries.

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References

  1. 1.

    Sharifian S, Homaei A, Kim SK, Satari M (2018) Production of newfound alkaline phosphatases from marine organisms with potential functions and industrial applications. Process Biochem 64:103–115. https://doi.org/10.1016/j.procbio.2017.10.005

  2. 2.

    Sharifian S, Homaei A, Hemmati R, Khajeh K (2017) Light emission miracle in the sea and preeminent applications of bioluminescence in recent new biotechnology. J Photochem Photobiol B Biol 172:115–128. https://doi.org/10.1016/j.jphotobiol.2017.05.021

  3. 3.

    Ding C, Sun H, Ren J, Qu X (2017) Immobilization of enzyme on chiral polyelectrolyte surface. Anal Chim Acta 952:88–95. https://doi.org/10.1016/j.aca.2016.11.047

  4. 4.

    Homaei A, Saberi D (2015) Immobilization of α-amylase on gold nanorods: an ideal system for starch processing. Process Biochem 50:1394–1399. https://doi.org/10.1016/j.procbio.2015.06.002

  5. 5.

    Homaei A, Etemadipour R (2015) Improving the activity and stability of actinidin by immobilization on gold nanorods. Int J Biol Macromol 72:1176–1181. https://doi.org/10.1016/j.ijbiomac.2014.10.029

  6. 6.

    Homaei AA, Sajedi RH, Sariri R et al (2010) Cysteine enhances activity and stability of immobilized papain. Amino Acids 38:937–942. https://doi.org/10.1007/s00726-009-0302-3

  7. 7.

    Homaei A (2015) Enhanced activity and stability of papain immobilized on CNBr-activated sepharose. Int J Biol Macromol 75:373–377. https://doi.org/10.1016/j.ijbiomac.2015.01.055

  8. 8.

    Homaei A (2015) Enzyme immobilization and its application in the food industry. In: Ravishankar, Rai (eds) Advances in food biotechnology, first. Wiley, Oxford, pp 145–164

  9. 9.

    Mohamed SA, Al-Harbi MH, Almulaiky YQ et al (2017) Immobilization of horseradish peroxidase on Fe3O4 magnetic nanoparticles. Electron J Biotechnol. https://doi.org/10.1016/j.ejbt.2017.03.010

  10. 10.

    Liu W, Wang L, Jiang R (2012) Specific enzyme immobilization approaches and their application with nanomaterials. Top Catal 55:1146–1156. https://doi.org/10.1007/s11244-012-9893-0

  11. 11.

    Shi L, Ma F, Han Y et al (2014) Removal of sulfonamide antibiotics by oriented immobilized laccase on Fe3O4 nanoparticles with natural mediators. J Hazard Mater 279:203–211. https://doi.org/10.1016/j.jhazmat.2014.06.070

  12. 12.

    Homaei A, Lavajoo F, Sariri R (2016) Development of marine biotechnology as a resource for novel proteases and their role in modern biotechnology. Int J Biol Macromol 88:542–552. https://doi.org/10.1016/j.ijbiomac.2016.04.023

  13. 13.

    Shojaei F, Homaei A, Taherizadeh MR, Kamrani E (2017) Characterization of biosynthesized chitosan nanoparticles from Penaeus vannamei for the immobilization of P. vannamei protease: an eco-friendly nanobiocatalyst. Int J Food Prop 20:S1413–S1423

  14. 14.

    Dadshahi Z, Homaei A, Zeinali F et al (2016) Extraction and purification of a highly thermostable alkaline caseinolytic protease from wastes Litopenaeus vannamei suitable for food and detergent industries. Food Chem 202:110–115. https://doi.org/10.1016/j.foodchem.2016.01.104

  15. 15.

    Arefi M, Saberi D, Karimi M, Heydari A (2015) Superparamagnetic Fe(OH)3@Fe3O4 nanoparticles: an efficient and recoverable catalyst for tandem oxidative amidation of alcohols with amine hydrochloride salts. ACS Comb Sci 17:341–347. https://doi.org/10.1021/co5001844

  16. 16.

    Mikhaylova M, Kim DK, Berry CC et al (2004) BSA immobilization on amine functionalized superparamagnetic iron oxide nanoparticles. Chem Mater 16:2344–2354

  17. 17.

    Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein–dye binding. Anal Biochem 72:248–254. https://doi.org/10.1016/0003-2697(76)90527-3

  18. 18.

    Homaei A, Barkheh H, Sariri R, Stevanato R (2014) Immobilized papain on gold nanorods as heterogeneous biocatalysts. Amino Acids 46:1649–1657. https://doi.org/10.1007/s00726-014-1724-0

  19. 19.

    Homaei A, Samari F (2017) Investigation of activity and stability of papain by adsorption on multi-wall carbon nanotubes. Int J Biol Macromol 105:1630–1635. https://doi.org/10.1016/j.ijbiomac.2017.02.038

  20. 20.

    Homaei A (2017) Immobilization of Penaeus merguiensis alkaline phosphatase on gold nanorods for heavy metal detection. Ecotoxicol Environ Saf 136:1–7. https://doi.org/10.1016/j.ecoenv.2016.10.023

  21. 21.

    Fortes CCS, Daniel-da-Silva AL, Xavier AMRB., Tavares APM (2017) Optimization of enzyme immobilization on functionalized magnetic nanoparticles for laccase biocatalytic reactions. Chem Eng Process Process Intensif. https://doi.org/10.1016/j.cep.2017.03.009

  22. 22.

    Al-Dhrub AHA, Sahin S, Ozmen I et al (2017) Immobilization and characterization of human carbonic anhydrase I on amine functionalized magnetic nanoparticles. Process Biochem. https://doi.org/10.1016/j.procbio.2017.03.025

  23. 23.

    Das A, Singh J, Yogalakshmi KN (2017) International biodeterioration and biodegradation laccase immobilized magnetic iron nanoparticles: fabrication and its performance evaluation in chlorpyrifos degradation. Int Biodeterior Biodegrad 117:183–189. https://doi.org/10.1016/j.ibiod.2017.01.007

  24. 24.

    Wanjari S, Prabhu C, Yadav R et al (2011) Immobilization of carbonic anhydrase on chitosan beads for enhanced carbonation reaction. Process Biochem 46:1010–1018. https://doi.org/10.1016/j.procbio.2011.01.023

  25. 25.

    Arrhenius S (1889) Uber die Reaktionsgeschwindigkeit bei der Inversion von Rohrzucker durch Säuren. Z Phys Chem 4:226

  26. 26.

    Homaei AA, Sariri R, Vianello F, Stevanato R (2013) Enzyme immobilization: an update. J Chem Biol 6:185–205. https://doi.org/10.1007/s12154-013-0102-9

  27. 27.

    Brena B, González-Pombo P, Batista-Viera F (2013) Immobilization of enzymes: a literature survey. Immobil Enzym Cells 1051:15–31. https://doi.org/10.1007/978-1-62703-550-7_2

  28. 28.

    Kim BJ, Kang BK, Bahk YY et al (2009) Immobilization of horseradish peroxidase on multi-walled carbon nanotubes and its enzymatic stability. Curr Appl Phys 9:e263–e265. https://doi.org/10.1016/j.cap.2009.06.050

  29. 29.

    Chen C, Xie Q, Yang D et al (2013) Recent advances in electrochemical glucose biosensors: a review. RSC Adv 3:4473. https://doi.org/10.1039/c2ra22351a

  30. 30.

    Tischer W, Kasche V (1999) Immobilized enzymes: crystals or carriers? 17:326–335

  31. 31.

    Copeland RA (2000) Enzymes: a practical introduction to structure, mechanism, and data analysis. Wiley, Oxford

  32. 32.

    Palmer T (1995) Understanding enzymes. Prentice Hall/Ellis Horwood, Upper Saddle River

  33. 33.

    Jafary F, Panjehpour M, Varshosaz J, Yaghmaei P (2016) Stability improvement of immobilized alkaline phosphate using chitosan nanoparticles. Braz J Chem Eng 33:243–250. https://doi.org/10.1590/0104-6632.20160332s20140074

  34. 34.

    Samani NB, Nayeri H, Amiri G (2016) Effects of cadmium chloride as inhibitor on stability and kinetics of immobilized Lactoperoxidase (LPO) on silica-coated magnetite nanoparticles versus free LPO. 3:pp 230–239

  35. 35.

    Patel SKS, Otari SV, Chan Kang Y, Lee J-K (2017) Protein–inorganic hybrid system for efficient his-tagged enzymes immobilization and its application in l-xylulose production. RSC Adv 7:3488–3494. https://doi.org/10.1039/C6RA24404A

  36. 36.

    Contesini FJ, Figueira J, de A, Kawaguti HY, et al (2013) Potential applications of carbohydrases immobilization in the food industry. Int J Mol Sci 14:1335–1369. https://doi.org/10.3390/ijms14011335

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Acknowledgements

Authors are grateful to the University of Hormozgan for the financial support to this research.

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Correspondence to Ahmad Homaei.

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Moslemi, M., Homaei, A. & Toiserkani, H. Aspartic acid introduce the functional amine groups on the surface of superparamagnetic Fe(OH)3@Fe3O4 nanoparticles for efficient immobilization of Penaeus vannamei protease. Bioprocess Biosyst Eng 41, 749–756 (2018). https://doi.org/10.1007/s00449-018-1908-1

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Keywords

  • Superparamagnetic Fe(OH)3@Fe3O4 nanoparticles
  • Aspartic acid
  • Functional amine groups
  • Penaeus vannamei protease