SnO2 hollow nanotubes

A novel and efficient support matrix for enzyme immobilization

Muhammad Zahid Anwar, Dong Jun Kim, Ashok Kumar, Sanjay K.S. Patel, Sachin Otari, Primata Mardina, Jae Hoon Jeong, Jung Hoon Sohn, Jong Hak Kim, Jung Tae Park, Jung Kul Lee

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

A major challenge in the industrial use of enzymes is maintaining their stability at elevated temperatures and in harsh organic solvents. In order to address this issue, we investigated the use of nanotubes as a support material for the immobilization and stabilization of enzymes in this work. SnO2 hollow nanotubes with a high surface area were synthesized by electrospinning the SnCl2 precursor and polyvinylpyrrolidone (dissolved in dimethyl formamide and ethanol). The electrospun product was used for the covalent immobilization of enzymes such as lipase, horseradish peroxidase, and glucose oxidase. The use of SnO2 hollow nanotubes as a support was promising for all immobilized enzymes, with lipase having the highest protein loading value of 217 mg/g, immobilization yield of 93%, and immobilization efficiency of 89%. The immobilized enzymes were fully characterized by various analytical methods. The covalently bonded lipase showed a half-life value of 4.5 h at 70 °C and retained ~91% of its original activity even after 10 repetitive cycles of use. Thus, the SnO2 hollow nanotubes with their high surface area are promising as a support material for the immobilization of enzymes, leading to improved thermal stability and a higher residual activity of the immobilized enzyme under harsh solvent conditions, as compared to the free enzyme.

Original languageEnglish
Article number15333
JournalScientific reports
Volume7
Issue number1
DOIs
Publication statusPublished - 2017 Dec 1

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Enzyme immobilization
Nanotubes
Immobilized Enzymes
Lipase
Enzymes
Povidone
Glucose Oxidase
Electrospinning
Dimethylformamide
Horseradish Peroxidase
Organic solvents
Thermodynamic stability
Ethanol
Stabilization
Proteins

All Science Journal Classification (ASJC) codes

  • General

Cite this

Anwar, M. Z., Kim, D. J., Kumar, A., Patel, S. K. S., Otari, S., Mardina, P., ... Lee, J. K. (2017). SnO2 hollow nanotubes: A novel and efficient support matrix for enzyme immobilization. Scientific reports, 7(1), [15333]. https://doi.org/10.1038/s41598-017-15550-y
Anwar, Muhammad Zahid ; Kim, Dong Jun ; Kumar, Ashok ; Patel, Sanjay K.S. ; Otari, Sachin ; Mardina, Primata ; Jeong, Jae Hoon ; Sohn, Jung Hoon ; Kim, Jong Hak ; Park, Jung Tae ; Lee, Jung Kul. / SnO2 hollow nanotubes : A novel and efficient support matrix for enzyme immobilization. In: Scientific reports. 2017 ; Vol. 7, No. 1.
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Anwar, MZ, Kim, DJ, Kumar, A, Patel, SKS, Otari, S, Mardina, P, Jeong, JH, Sohn, JH, Kim, JH, Park, JT & Lee, JK 2017, 'SnO2 hollow nanotubes: A novel and efficient support matrix for enzyme immobilization', Scientific reports, vol. 7, no. 1, 15333. https://doi.org/10.1038/s41598-017-15550-y

SnO2 hollow nanotubes : A novel and efficient support matrix for enzyme immobilization. / Anwar, Muhammad Zahid; Kim, Dong Jun; Kumar, Ashok; Patel, Sanjay K.S.; Otari, Sachin; Mardina, Primata; Jeong, Jae Hoon; Sohn, Jung Hoon; Kim, Jong Hak; Park, Jung Tae; Lee, Jung Kul.

In: Scientific reports, Vol. 7, No. 1, 15333, 01.12.2017.

Research output: Contribution to journalArticle

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AU - Anwar, Muhammad Zahid

AU - Kim, Dong Jun

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AU - Patel, Sanjay K.S.

AU - Otari, Sachin

AU - Mardina, Primata

AU - Jeong, Jae Hoon

AU - Sohn, Jung Hoon

AU - Kim, Jong Hak

AU - Park, Jung Tae

AU - Lee, Jung Kul

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AB - A major challenge in the industrial use of enzymes is maintaining their stability at elevated temperatures and in harsh organic solvents. In order to address this issue, we investigated the use of nanotubes as a support material for the immobilization and stabilization of enzymes in this work. SnO2 hollow nanotubes with a high surface area were synthesized by electrospinning the SnCl2 precursor and polyvinylpyrrolidone (dissolved in dimethyl formamide and ethanol). The electrospun product was used for the covalent immobilization of enzymes such as lipase, horseradish peroxidase, and glucose oxidase. The use of SnO2 hollow nanotubes as a support was promising for all immobilized enzymes, with lipase having the highest protein loading value of 217 mg/g, immobilization yield of 93%, and immobilization efficiency of 89%. The immobilized enzymes were fully characterized by various analytical methods. The covalently bonded lipase showed a half-life value of 4.5 h at 70 °C and retained ~91% of its original activity even after 10 repetitive cycles of use. Thus, the SnO2 hollow nanotubes with their high surface area are promising as a support material for the immobilization of enzymes, leading to improved thermal stability and a higher residual activity of the immobilized enzyme under harsh solvent conditions, as compared to the free enzyme.

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