Asset Details
Do you wish to reserve the book?
Newly Synthesized Multifunctional Biopolymer Coated Magnetic Core/Shell Fe3O4@Au Nanoparticles for Evaluation of L-asparaginase Immobilization
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Newly Synthesized Multifunctional Biopolymer Coated Magnetic Core/Shell Fe3O4@Au Nanoparticles for Evaluation of L-asparaginase Immobilization
Do you wish to request the book?
Newly Synthesized Multifunctional Biopolymer Coated Magnetic Core/Shell Fe3O4@Au Nanoparticles for Evaluation of L-asparaginase Immobilization
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Newly Synthesized Multifunctional Biopolymer Coated Magnetic Core/Shell Fe3O4@Au Nanoparticles for Evaluation of L-asparaginase Immobilization
2023
Overview
The immobilization strategy can promote greater enzyme utilization in applications by improving the overall stability and reusability of the enzyme. In this work, the L-asparaginase (L-ASNase) obtained from
Escherichia coli
was chosen as a model enzyme and immobilized onto the Fe
3
O
4
@Au-carboxymethyl chitosan (CMC) magnetic nanoparticles (MNPs) through adsorption. TEM, SEM, FT-IR, XRD, EDS, and TGA analyses were performed to examine the structure with and without L-ASNase. The yield of immobilized L-ASNase on Fe
3
O
4
@Au-CMC was found to be 68%. The biochemical properties such as optimum pH, optimum temperature, reusability, and thermal stability of the Fe
3
O
4
@Au-CMC/L-ASNase were comprehensively investigated. For instance, Fe
3
O
4
@Au-CMC/L-ASNase reached maximum activity at pH 7.0 and the optimum temperature was found to be 50 °C. The noticeably lower Ea value of the Fe
3
O
4
@Au-CMC/L-ASNase revealed the enhanced catalytic activity of this enzyme after immobilization. The
Km
and
Vmax
values were 3.27 ± 0.48 mM, and 51.54 ± 0.51 μmol min
−1
for Fe
3
O
4
@Au-CMC/L-ASNase, respectively, which means good substrate affinity. The Fe
3
O
4
@Au-CMC/L-ASNase retained 65% of its initial activity even after 90 min at 60 °C. Moreover, it maintained more than 75% of its original activity after 10 cycles, indicating its excellent reusability. The results obtained suggested that this investigation highlights the use of MNPs as a support for the development of more economical and sustainable immobilized enzyme systems.
Publisher
Springer US,Springer Nature B.V
