TY - JOUR
T1 - Design and characterization of self-assembled fish sarcoplasmic protein-alginate nanocomplexes
AU - Stephansen, Karen
AU - Mattebjerg, Maria
AU - Wattjes, Jasper
AU - Milisavljevic, Ana
AU - Jessen, Flemming
AU - Qvortrup, Klaus
AU - Goycoolea, Francisco M
AU - Chronakis, Ioannis S
N1 - Copyright © 2015 Elsevier B.V. All rights reserved.
PY - 2015/5/1
Y1 - 2015/5/1
N2 - 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±3nm, and the zeta potential was -42±0.3mV. 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.
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±3nm, and the zeta potential was -42±0.3mV. 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.
U2 - 10.1016/j.ijbiomac.2015.02.018
DO - 10.1016/j.ijbiomac.2015.02.018
M3 - Journal article
C2 - 25709012
SN - 0141-8130
VL - 76
SP - 146
EP - 152
JO - International Journal of Biological Macromolecules
JF - International Journal of Biological Macromolecules
ER -