TY - JOUR
T1 - Nano-assembly of manganese peroxidase and lignin peroxidase from P. chrysosporium for biocatalysis in aqueous and non-aqueous media
AU - Patel, Devendra S.
AU - Aithal, Rajendra K.
AU - Krishna, Gopal
AU - Lvov, Yuri M.
AU - Tien, Ming
AU - Kuila, Debasish
N1 - Funding Information:
We thank Dr. T. Mester and Mr. S. Singh for their help in this project. This work has been supported by the start-up grant of Louisiana Tech University.
PY - 2005/6/10
Y1 - 2005/6/10
N2 - Development, characterization, and activity studies of nano-assemblies of lignin peroxidase (LiP), and manganese peroxidase (MnP) from Phanerochaete chrysosporium on flat surfaces as well as colloidal particles have been investigated. These assemblies of LiP and MnP were fabricated with polyelectrolytes - poly(ethylenimine) (PEI), poly(dimethyldiallylammonium chloride) (PDDA), and poly(allylamine) (PAH) - using a layer-by-layer self-assembly technique (LbL). Characterization of these assemblies on flat surfaces was monitored using quartz crystal microbalance (QCM), while assemblies on microparticles such as melamine formaldehyde (MF) were carried out with zeta potential analyzer (ZPA). A unique dynamic adsorption-desorption of the enzyme layers is observed during the assembly. All the nano-assemblies of LiP and MnP can effectively oxidize veratryl alcohol (VA) to its aldehyde for an extended period of time. The effect of different polyions and the number of polyion layers on the activities of LiP and MnP nano-assembly was also examined. It is observed that drying of enzyme layer during the assembly and the use of non-aqueous media, such as acetone can significantly reduce the activity of the enzymes. Enzyme activity reaches a minimum when the concentration of acetone is increased to 30%; however, the activity can be restored to its original value by increasing the concentration of aqueous media. Preliminary studies using assemblies of LiP and MnP on MF microparticles further demonstrate the feasibility of developing potential systems for degradation of environmental pollutants.
AB - Development, characterization, and activity studies of nano-assemblies of lignin peroxidase (LiP), and manganese peroxidase (MnP) from Phanerochaete chrysosporium on flat surfaces as well as colloidal particles have been investigated. These assemblies of LiP and MnP were fabricated with polyelectrolytes - poly(ethylenimine) (PEI), poly(dimethyldiallylammonium chloride) (PDDA), and poly(allylamine) (PAH) - using a layer-by-layer self-assembly technique (LbL). Characterization of these assemblies on flat surfaces was monitored using quartz crystal microbalance (QCM), while assemblies on microparticles such as melamine formaldehyde (MF) were carried out with zeta potential analyzer (ZPA). A unique dynamic adsorption-desorption of the enzyme layers is observed during the assembly. All the nano-assemblies of LiP and MnP can effectively oxidize veratryl alcohol (VA) to its aldehyde for an extended period of time. The effect of different polyions and the number of polyion layers on the activities of LiP and MnP nano-assembly was also examined. It is observed that drying of enzyme layer during the assembly and the use of non-aqueous media, such as acetone can significantly reduce the activity of the enzymes. Enzyme activity reaches a minimum when the concentration of acetone is increased to 30%; however, the activity can be restored to its original value by increasing the concentration of aqueous media. Preliminary studies using assemblies of LiP and MnP on MF microparticles further demonstrate the feasibility of developing potential systems for degradation of environmental pollutants.
UR - http://www.scopus.com/inward/record.url?scp=20344368835&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=20344368835&partnerID=8YFLogxK
U2 - 10.1016/j.colsurfb.2005.03.007
DO - 10.1016/j.colsurfb.2005.03.007
M3 - Article
C2 - 15916887
AN - SCOPUS:20344368835
SN - 0927-7765
VL - 43
SP - 13
EP - 19
JO - Colloids and Surfaces B: Biointerfaces
JF - Colloids and Surfaces B: Biointerfaces
IS - 1
ER -