Affordable Access

Access to the full text

A fast and efficient stabilization of firefly luciferase on MIL-53(Al) via surface adsorption mechanism

Authors
  • Nowroozi-Nejad, Zohreh
  • Bahramian, Bahram
  • Hosseinkhani, Saman
Type
Published Article
Journal
Research on Chemical Intermediates
Publisher
Springer-Verlag
Publication Date
Jan 21, 2019
Volume
45
Issue
4
Pages
2489–2501
Identifiers
DOI: 10.1007/s11164-019-03748-w
Source
Springer Nature
Keywords
License
Yellow

Abstract

AbstractStabilization and immobilization on a proper support is essential in processing and production of enzymes. Luciferase is an unstable, thermally sensitive, and light-emitting enzyme that requires stabilization for efficiency and productivity in bio-luminescence reactions. In this work, a known and well-porous framework, MIL-53(Al), was used, for the first time, to support the immobilization of firefly luciferase. Interestingly, all the stability values were improved through the immobilization process, and the content of the loading enzyme on MIL-53(Al) was found to be significant. The results obtained indicated that the stabilization of firefly luciferase on MIL-53(Al) proceeded through the adsorption method. MIL-53(Al) was also characterized by the FT-IR, X-ray diffraction, FE-SEM, TEM, BET, and TGA techniques in order to determine the carboxylic groups and symmetric/asymmetric CO2, percentage of crystallinity and its purity, morphology, size, and shape of the MIL-53(Al) particles, and surface-to-area ratio and thermal gravimetry of support.Graphical abstract

Report this publication

Statistics

Seen <100 times