Skip to main content
Log in

Metal–organic frameworks (MOFs): a novel support platform for ASNase immobilization

  • Materials for life sciences
  • Published:
Journal of Materials Science Aims and scope Submit manuscript

Abstract

Metal–organic frameworks (MOFs) have been recently studied for a variety of applications because of their huge surface area, large porosity, and tunable functionality. In this work, for the first time, the efficient immobilization of l-asparaginase (ASNase, EC 3.5.1.1) by using MOF as a simple and novel support is demonstrated. The functional groups, morphology, chemical composition, and crystal structure of the support and immobilized ASNase were investigated by using different methods, including Fourier transform infrared spectroscopy, scanning electron microscopy, energy-dispersive spectrometer, and X-ray diffraction. Afterward, the enzymatic activities and thermodynamic parameters of the immobilized l-ASNase (ASNase@ZIF-8) were compared with free one. After enzyme immobilization, the optimum temperature shifted from 50 to 60 °C, while the optimum pH remains unchanged at 9.0. However, the pH and thermal stability of the ASNase@ZIF-8 was significantly improved compared to the free one. The ASNase@ZIF-8 displayed an excellent long-term storage stability, which could protect more than 56% of the initial activity at 25 °C for 4 weeks. Besides, the ASNase@ZIF-8 had high reusability, which showed a high degree of activity (more than 45%) after 10 cycles. Km and Vmax values were 0.18 mM and 64.5 µmol/min for ASNase@ZIF-8 and those for free ASNase were 0.40 mM and 68.0 µmol/min, respectively. The proposed support based on ZIF-8 was superior in terms of high enzyme loading capacity (82.0%), high enzyme catalytic activity, and easy preparation process. Overall, newly developed support for ASNase may provide a new platform for its biotechnological applications.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
Figure 7
Figure 8
Figure 9
Figure 10
Figure 11

Similar content being viewed by others

References

  1. Xie T, Wang A, Huang L, Li H, Chen Z, Wang Q, Yin X (2009) Recent advance in the support and technology used in enzyme immobilization. Afr J Biotechnol 8:4724–4733

    CAS  Google Scholar 

  2. Brady D, Jordaan J (2009) Advances in enzyme immobilisation. Biotechnol Lett 31:1639–1650

    CAS  Google Scholar 

  3. Nadar SS, Rathod VK (2019) One pot synthesis of α-amylase metal organic framework (MOF)-sponge via dip-coating technique. Int J Biol Macromol 138:1035–1043

    CAS  Google Scholar 

  4. Sheldon RA, van Pelt S (2013) Enzyme immobilisation in biocatalysis: Why, What and How. Chem Soc Rev 42:6223–6235

    CAS  Google Scholar 

  5. Sheldon RA (2007) Enzyme immobilization: the quest for optimum performance. Adv Synth Catal 349:1289–1307

    CAS  Google Scholar 

  6. Datta S, Christena LR, Rajaram YR (2013) Enzyme immobilization: an overview on techniques and support materials. 3Biotech 3:1–9

    Google Scholar 

  7. Cui J, Feng Y, Jia S (2018) Silica encapsulated catalase@metal–organic framework composite: a highly stable and recyclable biocatalyst. Chem Eng J 351:506–514

    CAS  Google Scholar 

  8. Samui A, Kumar Sahu S (2018) One-pot synthesis of microporous nanoscale metal organic frameworks conjugated with laccase as a promising biocatalyst. New J Chem 42:4192–4200

    CAS  Google Scholar 

  9. Nadar SS, Rathod VK (2019) Immobilization of proline activated lipase within metal organic framework (MOF). Int J Biol Macromol. https://doi.org/10.1016/j.ijbiomac.2019.10.199

    Article  Google Scholar 

  10. Salgaonkar M, Nadar SS, Rathod VK (2019) Biomineralization of orange peel peroxidase within metal organic frameworks (OPP–MOFs) for dye degradation. J Environ Chem Eng 7:102969

    CAS  Google Scholar 

  11. Nadar SS, Vaidya L, Maurya S, Rathod VK (2019) Polysaccharide based metal organic frameworks (polysaccharide-MOF): a review. Coord Chem Rev 396:1–21

    CAS  Google Scholar 

  12. Tadepalli S, Yim J, Cao S, Wang Z, Naik RR, Singamaneni S (2018) Metal–organic framework encapsulation for the preservation and photothermal enhancement of enzyme activity. Small 14:1702382

    Google Scholar 

  13. Liu X, Chen W, Lian M, Chen X, Lu Y, Yang W (2019) Enzyme immobilization on ZIF-67/MWCNT composite engenders high sensitivity electrochemical sensing. J Electroanal Chem 833:505–511

    CAS  Google Scholar 

  14. Cao SL, Yue DM, Li XH, Smith TJ, Li N, Zong MH, Wu H, Ma YZ, Lou WY (2016) Novel nano-/micro-biocatalyst: soybean epoxide hydrolase immobilized on UiO-66-NH2 MOF for efficient biosynthesis of enantiopure (R)-1, 2-octanediol in deep eutectic solvents. ACS Sustain Chem Eng 4:3586–3595

    CAS  Google Scholar 

  15. Ren S, Feng Y, Wen H, Li C, Sun B, Cui J, Jia S (2018) Immobilized carbonic anhydrase on mesoporous cruciate flower-like metal organic framework for promoting CO2 sequestration. Int J Biol Macromol 117:189–198

    CAS  Google Scholar 

  16. Wang Q, Zhang X, Huang L, Zhang Z, Dong S (2017) GOx@ZIF-8(NiPd) Nanoflower: an artificial enzyme system for tandem catalysis. Angew Chem Int Ed 56:16082–16085

    CAS  Google Scholar 

  17. Nadar SS, Rathod VK (2018) Encapsulation of lipase within metal–organic framework (MOF) with enhanced activity intensified under ultrasound. Enzyme Microb Technol 108:11–20

    CAS  Google Scholar 

  18. Patra S, Sene S, Mousty C, Serre C, Chaussé A, Legrand L, Steunou N (2016) Design of laccase-metal organic framework-based bioelectrodes for biocatalytic oxygen reduction reaction. ACS Appl Mater Interfaces 8:20012–20022

    CAS  Google Scholar 

  19. Ulu A, Koytepe S, Ates B (2016) Design of starch functionalized biodegradable P(MAA-co-MMA) as carrier matrix for l-asparaginase immobilization. Carbohydr Polym 153:559–572

    CAS  Google Scholar 

  20. Cachumba JJM, Antunes FAF, Peres GFD, Brumano LP, Santos JC, Da Silva SS (2016) Current applications and different approaches for microbial l-asparaginase production. Braz J Microbiol 47:77–85

    CAS  Google Scholar 

  21. Onishi Y, Prihanto AA, Yano S, Takagi K, Umekawa M, Wakayama M (2015) Effective treatment for suppression of acrylamide formation in fried potato chips using l-asparaginase from Bacillus subtilis. 3 Biotech 5:783–789

    Google Scholar 

  22. Ashok A, Doriya K, Rao JV, Qureshi A, Tiwari AK, Kumar DS (2019) Microbes producing l-asparaginase free of glutaminase and urease isolated from extreme locations of antarctic soil and moss. Sci Rep 9:1423

    Google Scholar 

  23. Asselin B, Rizzari C (2015) Asparaginase pharmacokinetics and implications of therapeutic drug monitoring. Leuk Lymphoma 56:2273–2280

    CAS  Google Scholar 

  24. Brumano LP, da Silva FVS, Costa-Silva TA, Apolinário AC, Santos JHPM, Kleingesinds EK, Monteiro G, Rangel-Yagui CO, Benyahia B, Junior AP (2019) Development of l-asparaginase biobetters: current research status and review of the desirable quality profiles. Front Bioeng Biotechnol 6:212

    Google Scholar 

  25. Ulu A, Ates B (2017) Immobilization of l-asparaginase on carrier materials: a comprehensive review. Bioconjug Chem 28:1598–1610

    CAS  Google Scholar 

  26. Cui J, Feng Y, Lin T, Tan Z, Zhong C, Jia S (2017) Mesoporous metal–organic framework with well-defined cruciate flower-like morphology for enzyme immobilization. ACS Appl Mater Interfaces 9:10587–10594

    CAS  Google Scholar 

  27. Wriston JC, Yellin TO (1973) l-asparaginase: a review. Adv Enzymol Relat Areas Mol Biol 39:185–248

    CAS  Google Scholar 

  28. Agrawal S, Kango N (2019) Development and catalytic characterization of l-asparaginase nano-bioconjugates. Int J Biol Macromol 135:1142–1150

    CAS  Google Scholar 

  29. Patil PD, Yadav GD (2018) Rapid in situ encapsulation of laccase into metal–organic framework support (ZIF-8) under biocompatible conditions. Chem Select 3:4669–4675

    CAS  Google Scholar 

  30. Dhiman S, Srivastava B, Singh G, Khatri M, Arya SK (2019) Immobilization of mannanase on sodium alginate-grafted-β-cyclodextrin: an easy and cost effective approach for the improvement of enzyme properties. Int J Biol Macromol. https://doi.org/10.1016/j.ijbiomac.2019.11.175

    Article  Google Scholar 

  31. Li X, Gao X, Ai L, Jiang J (2015) Mechanistic insight into the interaction and adsorption of Cr(VI) with zeolitic imidazolate framework-67 microcrystals from aqueous solution. Chem Eng J 274:238–246

    CAS  Google Scholar 

  32. Shen Y, Li W, Wu J, Li S, Luo H, Dai S, Wu W (2014) Solvent extraction of lanthanides and yttrium from aqueous solution with methylimidazole in an ionic liquid. Dalt Trans 43:10023–10032

    CAS  Google Scholar 

  33. Esfahanian M, Ghasemzadeh MA, Razavian SMH (2019) Synthesis, identification and application of the novel metal–organic framework Fe3O4@PAA@ZIF-8 for the drug delivery of ciprofloxacin and investigation of antibacterial activity. Artif Cells Nanomed Biotechnol 47:2024–2030

    CAS  Google Scholar 

  34. Adnan M, Li K, Xu L, Yan Y (2018) X-shaped ZIF-8 for immobilization rhizomucor miehei lipase via encapsulation and its application toward biodiesel production. Catalysts 8:96

    Google Scholar 

  35. Cao SL, Xu H, Lai LH, Gu WM, Xu P, Xiong J, Yin H, Li XH, Ma YZ, Zhou J, Zong MH, Lou WY (2017) Magnetic ZIF-8/cellulose/Fe3O4 nanocomposite: preparation, characterization, and enzyme immobilization. Bioresour Bioprocess 4:56

    Google Scholar 

  36. Trivedi MK, Branton A, Trivedi D, Nayak G, Saikia G, Jana S (2015) Physical and structural characterization of biofield treated imidazole derivatives. Nat Prod Chem Res 3:5

    Google Scholar 

  37. Wu X, Ge J, Yang C, Hou M, Liu Z (2015) Facile synthesis of multiple enzyme-containing metal–organic frameworks in a biomolecule-friendly environment. Chem Commun 51:13408–13411

    CAS  Google Scholar 

  38. Wang J, Zhao G, Yu F (2016) Facile preparation of Fe3O4@MOF core-shell microspheres for lipase immobilization. J Taiwan Inst Chem Eng 69:139–145

    CAS  Google Scholar 

  39. Yan J, Pan G, Ding C, Quan G (2010) Kinetic and thermodynamic parameters of β-glucosidase immobilized on various colloidal particles from a paddy soil. Colloids Surfaces B Biointerfaces 79:298–303

    CAS  Google Scholar 

  40. El-Refai HA, Shafei MS, Mostafa H, El-Refai AM, Araby EM, El-Beih FM, Easa SM, Gomaa SK (2016) Comparison of free and immobilized l-asparaginase synthesized by gamma-irradiated penicillium cyclopium. Polish J Microbiol 65:43–50

    Google Scholar 

  41. Gupta G, Sahai V, Gupta RK (2014) Thermal stability and thermodynamics of xylanase from Melanocarpus albomyces in presence of polyols and salts. BioResources 9:5801–5816

    Google Scholar 

  42. Ahmed SA, Saleh SAA, Abdel-Hameed SAM, Fayad AM (2019) Catalytic, kinetic and thermodynamic properties of free and immobilized caseinase on mica glass-ceramics. Heliyon 5:e01674

    Google Scholar 

  43. Vaidya L, Nadar SS, Rathod VK (2019) Entrapment of surfactant modified lipase within zeolitic imidazolate framework (ZIF)-8. Int J Biol Macromol 146:678–686

    Google Scholar 

  44. Tarhan T, Ulu A, Sariçam M et al (2020) Maltose functionalized magnetic core/shell Fe3O4@Au nanoparticles for an efficient l-asparaginase immobilization. Int J Biol Macromol 142:443–451

    Google Scholar 

  45. Ulu A, Noma SAA, Koytepe S, Ates B (2018) Magnetic Fe3O4@MCM-41 core-shell nanoparticles functionalized with thiol silane for efficient l-asparaginase immobilization. Artif Cells Nanomed Biotechnol 46:1035–1045

    CAS  Google Scholar 

Download references

Acknowledgements

The author would like to thank Dr. Burhan Ates for his helpful advice on various technical issues in this article.

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Ahmet Ulu.

Ethics declarations

Conflict of interest

The author declared no conflict of interest.

Additional information

Publisher's Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Ulu, A. Metal–organic frameworks (MOFs): a novel support platform for ASNase immobilization. J Mater Sci 55, 6130–6144 (2020). https://doi.org/10.1007/s10853-020-04452-6

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10853-020-04452-6

Navigation