Candida rugosa lipase covalently immobilized on facilely-synthesized carbon nitride nanosheets as a novel biocatalyst. Issue 26 (17th April 2018)
- Record Type:
- Journal Article
- Title:
- Candida rugosa lipase covalently immobilized on facilely-synthesized carbon nitride nanosheets as a novel biocatalyst. Issue 26 (17th April 2018)
- Main Title:
- Candida rugosa lipase covalently immobilized on facilely-synthesized carbon nitride nanosheets as a novel biocatalyst
- Authors:
- Li, Ya
Ruan, Zhijun
Zheng, Mingming
Deng, Qianchun
Zhang, Shan
Zheng, Chang
Tang, Hu
Huang, Fenghong
Shi, Jie - Abstract:
- Abstract : We report a rational design and fabrication of immobilized Candida rugosa lipase based on carbon nitride nanosheets (C3 N4 -NS) as the matrix. . Abstract : The immobilization of lipase on solid supports provides a significant improvement to the stability and reusability of lipase. During immobilization, the restricted surface area and inferior separation capacity of matrix materials are crucial for obtaining high-quality immobilized lipase. Carbon nitride nanosheets (C3 N4 -NS) as a type of two-dimensional nanomaterial have attracted various attentions for their prominent 2D planar nanostructure, characteristic surface area, thermostability and biocompatibility. Herein, we report a rational design and fabrication of immobilized Candida rugosa lipase based on carbon nitride nanosheets (C3 N4 -NS) as the matrix. The synthetic C3 N4 -NS are characterized by transmission electron microscopy, Brunauer–Emmett–Teller gas sorptometry measurement, X-ray powder diffraction, Fourier transform infrared spectroscopy and thermogravimetric analysis. These results show that C3 N4 -NS possess an as-expected two-dimensional nanostructure with a large surface area of 74.374 m 2 g −1 . In addition, we chose glutaraldehyde-assisted covalent attachment to combine C3 N4 -NS and Candida rugosa lipase (CRL) via amino groups at the margins of C3 N4 -NS. The as-constructed immobilized lipase (C3 N4 -NS@CRL) exhibits satisfactory enzyme-loading (44.76 mg g −1 ), pH-flexibility,Abstract : We report a rational design and fabrication of immobilized Candida rugosa lipase based on carbon nitride nanosheets (C3 N4 -NS) as the matrix. . Abstract : The immobilization of lipase on solid supports provides a significant improvement to the stability and reusability of lipase. During immobilization, the restricted surface area and inferior separation capacity of matrix materials are crucial for obtaining high-quality immobilized lipase. Carbon nitride nanosheets (C3 N4 -NS) as a type of two-dimensional nanomaterial have attracted various attentions for their prominent 2D planar nanostructure, characteristic surface area, thermostability and biocompatibility. Herein, we report a rational design and fabrication of immobilized Candida rugosa lipase based on carbon nitride nanosheets (C3 N4 -NS) as the matrix. The synthetic C3 N4 -NS are characterized by transmission electron microscopy, Brunauer–Emmett–Teller gas sorptometry measurement, X-ray powder diffraction, Fourier transform infrared spectroscopy and thermogravimetric analysis. These results show that C3 N4 -NS possess an as-expected two-dimensional nanostructure with a large surface area of 74.374 m 2 g −1 . In addition, we chose glutaraldehyde-assisted covalent attachment to combine C3 N4 -NS and Candida rugosa lipase (CRL) via amino groups at the margins of C3 N4 -NS. The as-constructed immobilized lipase (C3 N4 -NS@CRL) exhibits satisfactory enzyme-loading (44.76 mg g −1 ), pH-flexibility, thermostability (after 180 min at 50 °C, 67% of the initial activity remained) and recyclability (after 10 runs, 72% of the initial activity remained). When compared with the free CRL, all experimental data indicate that C3 N4 -NS@CRL exhibited improved stability and enhanced practicability. To our knowledge, this is the first report of the application of carbon nitride nanosheets to enzyme immobilization. … (more)
- Is Part Of:
- RSC advances. Volume 8:Issue 26(2018)
- Journal:
- RSC advances
- Issue:
- Volume 8:Issue 26(2018)
- Issue Display:
- Volume 8, Issue 26 (2018)
- Year:
- 2018
- Volume:
- 8
- Issue:
- 26
- Issue Sort Value:
- 2018-0008-0026-0000
- Page Start:
- 14229
- Page End:
- 14236
- Publication Date:
- 2018-04-17
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c8ra00536b ↗
- Languages:
- English
- ISSNs:
- 2046-2069
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 25869.xml