TY  - JOUR
AU  - Miletic, Nemanja
AU  - Nastasović, Aleksandra
AU  - Loos, Katja
PY  - 2012
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/968
AB  - Biotechnology also holds tremendous opportunities for realizing functional polymeric materials. Biocatalytic pathways to polymeric materials are an emerging research area with not only enormous scientific and technological promise, but also a tremendous impact on environmental issues. Many of the enzymatic polymerizations reported proceed in organic solvents. However, enzymes mostly show none of their profound characteristics in organic solvents and can easily denature under industrial conditions. Therefore, natural enzymes seldom have the features adequate to be used as industrial catalysts in organic synthesis. The productivity of enzymatic processes is often low due to substrate and/or product inhibition. An important route to improving enzyme performance in non-natural environments is to immobilize them. In this review we will first summarize some of the most prominent examples of enzymatic polymerizations and will subsequently review the most important immobilization routes that are used for the immobilization of biocatalysts relevant to the field of enzymatic polymerizations.
PB  - Elsevier Sci Ltd, Oxford
T2  - Bioresource Technology
T1  - Immobilization of biocatalysts for enzymatic polymerizations: Possibilities, advantages, applications
VL  - 115
SP  - 126
EP  - 135
DO  - 10.1016/j.biortech.2011.11.054
ER  - 

@article{
author = "Miletic, Nemanja and Nastasović, Aleksandra and Loos, Katja",
year = "2012",
abstract = "Biotechnology also holds tremendous opportunities for realizing functional polymeric materials. Biocatalytic pathways to polymeric materials are an emerging research area with not only enormous scientific and technological promise, but also a tremendous impact on environmental issues. Many of the enzymatic polymerizations reported proceed in organic solvents. However, enzymes mostly show none of their profound characteristics in organic solvents and can easily denature under industrial conditions. Therefore, natural enzymes seldom have the features adequate to be used as industrial catalysts in organic synthesis. The productivity of enzymatic processes is often low due to substrate and/or product inhibition. An important route to improving enzyme performance in non-natural environments is to immobilize them. In this review we will first summarize some of the most prominent examples of enzymatic polymerizations and will subsequently review the most important immobilization routes that are used for the immobilization of biocatalysts relevant to the field of enzymatic polymerizations.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Bioresource Technology",
title = "Immobilization of biocatalysts for enzymatic polymerizations: Possibilities, advantages, applications",
volume = "115",
pages = "126-135",
doi = "10.1016/j.biortech.2011.11.054"
}

Miletic, N., Nastasović, A.,& Loos, K.. (2012). Immobilization of biocatalysts for enzymatic polymerizations: Possibilities, advantages, applications. in Bioresource Technology
Elsevier Sci Ltd, Oxford., 115, 126-135.
https://doi.org/10.1016/j.biortech.2011.11.054

Miletic N, Nastasović A, Loos K. Immobilization of biocatalysts for enzymatic polymerizations: Possibilities, advantages, applications. in Bioresource Technology. 2012;115:126-135.
doi:10.1016/j.biortech.2011.11.054 .

Miletic, Nemanja, Nastasović, Aleksandra, Loos, Katja, "Immobilization of biocatalysts for enzymatic polymerizations: Possibilities, advantages, applications" in Bioresource Technology, 115 (2012):126-135,
https://doi.org/10.1016/j.biortech.2011.11.054 . .

TY  - JOUR
AU  - Miletic, Nemanja
AU  - Vuković, Zorica
AU  - Nastasović, Aleksandra
AU  - Loos, Katja
PY  - 2011
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/812
AB  - A series of poly(GMA-co-EGDMA) resins with identical composition but varying particle sizes, pore radii, specific surface areas and specific volumes are studied to assess how Candida antarctica lipase B immobilization affects the porosity of the copolymer particles. Mercury porosimetry reveals a significant change in the average pore size (up to 6.1-fold), the specific surface area (up to 3.2-fold) and the specific volume (up to 2.1-fold) of the epoxy resin. A similar behaviour is observed for glutaraldehyde-modified epoxy resins. The influences of the resin porosity properties on the loading of Candida antarctica lipase B during immobilization and on the hydrolytic activity (hydrolysis of p-nitrophenyl acetate) of the immobilized lipase are studied.
PB  - Wiley-V C H Verlag Gmbh, Weinheim
T2  - Macromolecular Bioscience
T1  - Effect of Candida antarctica Lipase B Immobilization on the Porous Structure of the Carrier
VL  - 11
IS  - 11
SP  - 1537
EP  - 1543
DO  - 10.1002/mabi.201100127
ER  - 

@article{
author = "Miletic, Nemanja and Vuković, Zorica and Nastasović, Aleksandra and Loos, Katja",
year = "2011",
abstract = "A series of poly(GMA-co-EGDMA) resins with identical composition but varying particle sizes, pore radii, specific surface areas and specific volumes are studied to assess how Candida antarctica lipase B immobilization affects the porosity of the copolymer particles. Mercury porosimetry reveals a significant change in the average pore size (up to 6.1-fold), the specific surface area (up to 3.2-fold) and the specific volume (up to 2.1-fold) of the epoxy resin. A similar behaviour is observed for glutaraldehyde-modified epoxy resins. The influences of the resin porosity properties on the loading of Candida antarctica lipase B during immobilization and on the hydrolytic activity (hydrolysis of p-nitrophenyl acetate) of the immobilized lipase are studied.",
publisher = "Wiley-V C H Verlag Gmbh, Weinheim",
journal = "Macromolecular Bioscience",
title = "Effect of Candida antarctica Lipase B Immobilization on the Porous Structure of the Carrier",
volume = "11",
number = "11",
pages = "1537-1543",
doi = "10.1002/mabi.201100127"
}

Miletic, N., Vuković, Z., Nastasović, A.,& Loos, K.. (2011). Effect of Candida antarctica Lipase B Immobilization on the Porous Structure of the Carrier. in Macromolecular Bioscience
Wiley-V C H Verlag Gmbh, Weinheim., 11(11), 1537-1543.
https://doi.org/10.1002/mabi.201100127

Miletic N, Vuković Z, Nastasović A, Loos K. Effect of Candida antarctica Lipase B Immobilization on the Porous Structure of the Carrier. in Macromolecular Bioscience. 2011;11(11):1537-1543.
doi:10.1002/mabi.201100127 .

Miletic, Nemanja, Vuković, Zorica, Nastasović, Aleksandra, Loos, Katja, "Effect of Candida antarctica Lipase B Immobilization on the Porous Structure of the Carrier" in Macromolecular Bioscience, 11, no. 11 (2011):1537-1543,
https://doi.org/10.1002/mabi.201100127 . .