TY - JOUR
T1 - Preparation of cobalt nanoparticles from polymorphic bacterial templates
T2 - A novel platform for biocatalysis
AU - Jang, Eunjin
AU - Shim, Hyun Woo
AU - Ryu, Bum Han
AU - An, Deu Rae
AU - Yoo, Wan Ki
AU - Kim, Kyeong Kyu
AU - Kim, Dong Wan
AU - Kim, T. Doohun
N1 - Funding Information:
This work was supported by the National Research Foundation of Korea (NRF-2012S1A2A1A01028907), and Sookmyung Women's University Research Grant (1-1503-0020) to T.D.K. We are grateful for the help of Dr. John Carver (University of Adelaide, Australia) for this project.
Publisher Copyright:
© 2015 Elsevier B.V.
PY - 2015/11/1
Y1 - 2015/11/1
N2 - Nanoparticles have gathered significant research attention as materials for enzyme immobilization due to their advantageous properties such as low diffusion rates, ease of manipulation, and large surface areas. Here, polymorphic cobalt nanoparticles of varied sizes and shapes were prepared using Micrococcus lylae, Bacillus subtilis, Escherichia coli, Paracoccus sp., and Haloarcula vallismortis as bacterial templates. Furthermore, nine lipases/carboxylesterases were successfully immobilized on these cobalt nanoparticles. Especially, immobilized forms of Est-Y29, LmH, and Sm23 were characterized in more detail for potential industrial applications. Immobilization of enzymes onto cobalt oxide nanoparticles prepared from polymorphic bacterial templates may have potential for efficient hydrolysis on an industrial-scale, with several advantages such as high retention of enzymatic activity, increased stability, and strong reusability.
AB - Nanoparticles have gathered significant research attention as materials for enzyme immobilization due to their advantageous properties such as low diffusion rates, ease of manipulation, and large surface areas. Here, polymorphic cobalt nanoparticles of varied sizes and shapes were prepared using Micrococcus lylae, Bacillus subtilis, Escherichia coli, Paracoccus sp., and Haloarcula vallismortis as bacterial templates. Furthermore, nine lipases/carboxylesterases were successfully immobilized on these cobalt nanoparticles. Especially, immobilized forms of Est-Y29, LmH, and Sm23 were characterized in more detail for potential industrial applications. Immobilization of enzymes onto cobalt oxide nanoparticles prepared from polymorphic bacterial templates may have potential for efficient hydrolysis on an industrial-scale, with several advantages such as high retention of enzymatic activity, increased stability, and strong reusability.
KW - Biocatalysts
KW - Cobalt oxide nanoparticles
KW - Enzyme immobilization
UR - http://www.scopus.com/inward/record.url?scp=84941627892&partnerID=8YFLogxK
U2 - 10.1016/j.ijbiomac.2015.09.009
DO - 10.1016/j.ijbiomac.2015.09.009
M3 - Article
C2 - 26358553
AN - SCOPUS:84941627892
SN - 0141-8130
VL - 81
SP - 747
EP - 753
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
ER -