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Stability studies of β-galactosidase immobilized on gluconic acid coated fullerenes

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Abstract

The present study demonstrates the coating of fullerenes with gluconic acid for the immobilization of Aspergillus oryzae β-galactosidase. The prepared nanomatrix provided 86% immobilization yield, and broadened the biocatalytic activity of immobilized enzyme at higher pH and temperature ranges. Immobilized β-galactosidase exhibited 60% activity even at 5.0% galactose concentration as compared to 23% enzyme activity obtained by soluble enzyme under similar experimental conditions. Reusability of the enzyme was improved considerably as a result of covalent immobilization. Immobilized β-galactosidase showed 89% activity even after sixth repeated use and could be recovered easily. The noticeable improvement in lactose hydrolysis was observed in batch reactors by immobilized enzyme in contrast to the soluble enzyme at high temperature ranges. At 50 °C, 89% lactose conversion was achieved by immobilized enzyme as compared to 77%, obtained by free β-galactosidase under similar incubation conditions. Hence, the developed immobilized enzyme preparation could be exploited for converting lactose into its monosaccharides in a convenient and cheaper way.

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Abbreviations

GACF:

Gluconic acid coated fullerene

IβG:

Immobilized β-galactosidase (β-galactosidase bound to GACF)

NPs:

Nanoparticles

SβG:

Soluble β-galactosidase

References

  • Alshanberi AM, Satar R, Ansari SA (2021) Stabilization of β-galactosidase on modified gold nanoparticles: a preliminary biochemical study to obtain lactose-free dairy products for lactose-intolerance individuals. Molecules 26(3):1226

    Article  CAS  Google Scholar 

  • Ansari SA, Husain Q (2010) Lactose hydrolysis by β galactosidase immobilized on concanavalin A-cellulose in batch and continuous mode. J Mol Catal B Enzym 63(1–2):68

    Article  CAS  Google Scholar 

  • Ansari SA, Husain Q (2012) Potential applications of enzymes immobilized on/in nanomaterials: a review. Biotechnol Adv 30(3):512

    Article  CAS  Google Scholar 

  • Ansari SA, Al-Shaeri M (2019) Biotechnological application of surface modified cerium oxide nanoparticles. Braz J Chem Eng 36(1):16

    Article  Google Scholar 

  • Ansari SA, Satar R, Zaidi SK, Naseer MI, Karim S, Alqahtani MH, Rasool M (2015a) Nanodiamonds as an effective and novel matrix for immobilizing β galactosidase. Food Bioprod Proc 95(4):298

    Article  CAS  Google Scholar 

  • Ansari SA, Satar R, Zaidi SK (2015b) Carboxylation of silver nanoparticles for the immobilization of β-galactosidase and its efficacy in galacto-oligosaccharides production. Quim Nova 38(3):58

    Google Scholar 

  • Bohme DK (2016) Fullerene ion chemistry: a journey of discovery and achievement. Philos Trans Royal Soc A 374(2):321

    Google Scholar 

  • Doane TL, Cheng Y, Babar A, Hill RJ, Burda C (2010) Electrophoretic mobilities of PEGylated gold NPs. J Am Chem Soc 132(44):15624

    Article  CAS  Google Scholar 

  • Guisan JM, Lopez-Gallego F, Bolivar JM, Rocha-Martin J, Fernandez-Lorente G (2020) The science of enzyme immobilization. Methods Mol Biol 2100(1):1

    CAS  PubMed  Google Scholar 

  • Guven RG, Kaplan A, Guven K, Matpan F, Dogru M (2011) Effects of various inhibitors on β-galactosidase purified from the thermoacidophilic Alicyclobacillus acidocaldarius subsp. Rittmannii isolated from Antarctica. Biotechnol Bioproc Eng 16(1):114

    Article  CAS  Google Scholar 

  • He H, Pham-Huy LA, Dramou P, Xiao D, Zuo P, Pham-Huy C (2013) Carbon nanotubes: applications in pharmacy and medicine. Biomed Res Internat 2013(5):578290

    Google Scholar 

  • Kalska-Szostko B, Rogowska M (2012) Preparation of magnetite-fullerene nanocomposite with enzyme immobilization. J Nanosci Nanotechnol 12(9):6907

    Article  CAS  Google Scholar 

  • Khalid K, Tan X, Zaid HFM, Tao Y, Chew CL, Chu DT, Lam MK, Ho YC, Lim JW, Wei LC (2020) Advanced in developmental organic and inorganic nanomaterial: a review. Bioengineered 11(1):328

    Article  CAS  Google Scholar 

  • Moreno C, Divins NJ, Gazquez J, Varela M, Angurelle I, Llorca J (2012) Improved thermal stability of oxide-supported naked gold nanoparticles by ligand-assisted pinning. Nanoscale 4(7):2278

    Article  CAS  Google Scholar 

  • Panesar PS, Kumari S, Panesar R (2010) Potential applications of immobilized β-galactosidase in food processing industries. Enzyme Res 2(2):473

    Google Scholar 

  • Pilehvar S, Wael KD (2015) Recent advances in electrochemical biosensors based on fullerene-C0 nano-structured platforms. Biosensors (basel) 5(4):712

    Article  CAS  Google Scholar 

  • Reis CLB, Sousa EYA, Serpa JF, Oliveira RC, Santos JCS (2019) Design of immobilized enzyme biocatalysts: drawbacks and opportunities. Quim Nova 42(7):13

    Google Scholar 

  • Sami S, Etesami N (2017) Improving thermal characteristics and stability of phase change material containing TiO2 nanoparticles after thermal cycles for energy storage. Appl Therm Eng 124(3):346

    Article  CAS  Google Scholar 

  • Saqib S, Akram A, Halim SA, Tassaduq R (2017) Sources of β-galactosidase and its applications in food industry. 3 Biotech 7(1):79

    Article  Google Scholar 

  • Sastre DE, Reis EA, Netto CGCM (2020) Strategies to rationalize enzyme immobilization procedures. Methods Enzymol 630(2):81

    Article  CAS  Google Scholar 

  • Sui Y, Cui Y, Nie Y, Xia GM, Sun GX, Han JT (2012) Surface modification of magnetite nanoparticles using gluconic acid and their application in immobilized lipase. Colloid Surface B Biointerface 93(1):24

    Article  CAS  Google Scholar 

  • Ureta MM, Martins GN, Figueira O, Pires PF, Castilho PC, Gomez-Zavaglia A (2020) Recent advances in β-galactosidase and fructosyltransferase immobilization technology. Crit Rev Food Sci Nutr 32(4):1040

    Google Scholar 

  • Wang EC, Wang AZ (2014) Nanoparticles and their applications in cell and molecular biology. Integrated Biology Cambridge 6(1):9

    Article  CAS  Google Scholar 

  • Wissing M, Niehues M, Ravoo BJ, Studer A (2020) Synthesis and immobilization of metal nanoparticles using photoactive polymer-decorated zeolite L crystals and their application in catalysis. Adv Synt Cataly 362(11):2245

    Article  CAS  Google Scholar 

  • Yang X, Ebrahimi A, Li J, Cui Q (2014) Fullerene-biomolecule conjugates and their biomedicinal applications. Int J Nanomed 9(1):77

    Article  Google Scholar 

  • Zhou QZK, Chen DC (2001) Effects of temperature and pH on the catalytic activity of the immobilized β-galactosidase from Kluyveromyces lactis. Biochem Eng J 9(1):33

    Article  CAS  Google Scholar 

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Acknowledgements

Mr. Jitendra Kumar of Department of Biotechnology (Chaudhary Charan Singh University, India) is gratefully acknowledged for providing the fullerene used in the study.

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Correspondence to Shakeel Ahmed Ansari.

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Ansari, S.A., Alshanberi, A.M. Stability studies of β-galactosidase immobilized on gluconic acid coated fullerenes. Braz. J. Chem. Eng. 39, 361–367 (2022). https://doi.org/10.1007/s43153-021-00146-x

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