Design and characterization of self-assembled fish sarcoplasmic protein-alginate nanocomplexes
Authorized Users Only
2015
Authors
Stephansen, KarenMattebjerg, Maria
Wattjes, Jasper
Milivojević, Ana
Jessen, Flemming
Qvortrup, Klaus
Goycoolea, Francisco M.
Chronakis, Ioannis S.
Article (Published version)
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Show full item recordAbstract
Macrostructures based on natural polymers are subject to large attention, as the application range is wide within the food and pharmaceutical industries. In this study we present nanocomplexes (NCXs) made from electrostatic self-assembly between negatively charged alginate and positively charged fish sarcoplasmic proteins (FSP), prepared by bulk mixing. A concentration screening revealed that there was a range of alginate and FSP concentrations where stable NCXs with similar properties were formed, rather than two exact concentrations. The size of the NCXs was 293 +/- 3 nm, and the zeta potential was -42 +/- 0.3 mV. The NCXs were stable in water, gastric buffer, intestinal buffer and HEPES buffered glycose, and at all pH values from 2 to 9 except pH 3, where they aggregated. When proteolytic enzymes were present in the buffer, the NCXs were degraded. Only at high concentrations the NCXs caused a decreased viability in HeLa and U2OS cell lines. The simple processing procedure and the hi...gh stability of the NCXs, makes them excellent candidates for use in the food and pharmaceutical industry.
Keywords:
Alginate / Proteins / Particle / Nanocomplex / Drug deliverySource:
International Journal of Biological Macromolecules, 2015, 76, 146-152Publisher:
- Elsevier, Amsterdam
Funding / projects:
- Danish Strategic Research CouncilDanske Strategiske Forskningsrad (DSF) [DSF -10-93456]
- Danish Strategic Research Council (FENAMI Project)
DOI: 10.1016/j.ijbiomac.2015.02.018
ISSN: 0141-8130
PubMed: 25709012
WoS: 000353604000019
Scopus: 2-s2.0-84924551687
Institution/Community
Inovacioni centarTY - JOUR AU - Stephansen, Karen AU - Mattebjerg, Maria AU - Wattjes, Jasper AU - Milivojević, Ana AU - Jessen, Flemming AU - Qvortrup, Klaus AU - Goycoolea, Francisco M. AU - Chronakis, Ioannis S. PY - 2015 UR - http://TechnoRep.tmf.bg.ac.rs/handle/123456789/2996 AB - Macrostructures based on natural polymers are subject to large attention, as the application range is wide within the food and pharmaceutical industries. In this study we present nanocomplexes (NCXs) made from electrostatic self-assembly between negatively charged alginate and positively charged fish sarcoplasmic proteins (FSP), prepared by bulk mixing. A concentration screening revealed that there was a range of alginate and FSP concentrations where stable NCXs with similar properties were formed, rather than two exact concentrations. The size of the NCXs was 293 +/- 3 nm, and the zeta potential was -42 +/- 0.3 mV. The NCXs were stable in water, gastric buffer, intestinal buffer and HEPES buffered glycose, and at all pH values from 2 to 9 except pH 3, where they aggregated. When proteolytic enzymes were present in the buffer, the NCXs were degraded. Only at high concentrations the NCXs caused a decreased viability in HeLa and U2OS cell lines. The simple processing procedure and the high stability of the NCXs, makes them excellent candidates for use in the food and pharmaceutical industry. PB - Elsevier, Amsterdam T2 - International Journal of Biological Macromolecules T1 - Design and characterization of self-assembled fish sarcoplasmic protein-alginate nanocomplexes EP - 152 SP - 146 VL - 76 DO - 10.1016/j.ijbiomac.2015.02.018 ER -
@article{ author = "Stephansen, Karen and Mattebjerg, Maria and Wattjes, Jasper and Milivojević, Ana and Jessen, Flemming and Qvortrup, Klaus and Goycoolea, Francisco M. and Chronakis, Ioannis S.", year = "2015", abstract = "Macrostructures based on natural polymers are subject to large attention, as the application range is wide within the food and pharmaceutical industries. In this study we present nanocomplexes (NCXs) made from electrostatic self-assembly between negatively charged alginate and positively charged fish sarcoplasmic proteins (FSP), prepared by bulk mixing. A concentration screening revealed that there was a range of alginate and FSP concentrations where stable NCXs with similar properties were formed, rather than two exact concentrations. The size of the NCXs was 293 +/- 3 nm, and the zeta potential was -42 +/- 0.3 mV. The NCXs were stable in water, gastric buffer, intestinal buffer and HEPES buffered glycose, and at all pH values from 2 to 9 except pH 3, where they aggregated. When proteolytic enzymes were present in the buffer, the NCXs were degraded. Only at high concentrations the NCXs caused a decreased viability in HeLa and U2OS cell lines. The simple processing procedure and the high stability of the NCXs, makes them excellent candidates for use in the food and pharmaceutical industry.", publisher = "Elsevier, Amsterdam", journal = "International Journal of Biological Macromolecules", title = "Design and characterization of self-assembled fish sarcoplasmic protein-alginate nanocomplexes", pages = "152-146", volume = "76", doi = "10.1016/j.ijbiomac.2015.02.018" }
Stephansen, K., Mattebjerg, M., Wattjes, J., Milivojević, A., Jessen, F., Qvortrup, K., Goycoolea, F. M.,& Chronakis, I. S.. (2015). Design and characterization of self-assembled fish sarcoplasmic protein-alginate nanocomplexes. in International Journal of Biological Macromolecules Elsevier, Amsterdam., 76, 146-152. https://doi.org/10.1016/j.ijbiomac.2015.02.018
Stephansen K, Mattebjerg M, Wattjes J, Milivojević A, Jessen F, Qvortrup K, Goycoolea FM, Chronakis IS. Design and characterization of self-assembled fish sarcoplasmic protein-alginate nanocomplexes. in International Journal of Biological Macromolecules. 2015;76:146-152. doi:10.1016/j.ijbiomac.2015.02.018 .
Stephansen, Karen, Mattebjerg, Maria, Wattjes, Jasper, Milivojević, Ana, Jessen, Flemming, Qvortrup, Klaus, Goycoolea, Francisco M., Chronakis, Ioannis S., "Design and characterization of self-assembled fish sarcoplasmic protein-alginate nanocomplexes" in International Journal of Biological Macromolecules, 76 (2015):146-152, https://doi.org/10.1016/j.ijbiomac.2015.02.018 . .