TY - JOUR
T1 - Impact of pluronic type on the physicochemical properties of lecithin liposome/pluronic particles
AU - Lee, Jihyo
AU - Choi, Seung Jun
N1 - Publisher Copyright:
© 2025 Elsevier Ltd
PY - 2025/7
Y1 - 2025/7
N2 - This study investigated how the ethylene oxide (EO) content in pluronic (70% for pluronic F127 and 80% for pluronic F108) affects the physicochemical attributes of lecithin liposome/pluronic particles characterized by a core/shell configuration. Additionally, their ability to encapsulate proteins was examined. Regardless of the EO content, the particles consistently exhibited a core/shell structure up to a lecithin/pluronic ratio of 0.2, with sizes ranging from 230 to 280 nm. Although liposome/pluronic particles maintained stability against pH alterations at 5 °C, storage above this temperature compromised their stability. This suggests that the EO content in pluronic does not significantly dictate the stability of these liposome/pluronic particles. Furthermore, these particles were able to encapsulate a model protein with a low isoelectric point (pI) with relative ease. However, attempts at modifying the liposome surface charge to a positive state for encapsulating proteins with higher pI values did not yield particles with a core/shell structure.
AB - This study investigated how the ethylene oxide (EO) content in pluronic (70% for pluronic F127 and 80% for pluronic F108) affects the physicochemical attributes of lecithin liposome/pluronic particles characterized by a core/shell configuration. Additionally, their ability to encapsulate proteins was examined. Regardless of the EO content, the particles consistently exhibited a core/shell structure up to a lecithin/pluronic ratio of 0.2, with sizes ranging from 230 to 280 nm. Although liposome/pluronic particles maintained stability against pH alterations at 5 °C, storage above this temperature compromised their stability. This suggests that the EO content in pluronic does not significantly dictate the stability of these liposome/pluronic particles. Furthermore, these particles were able to encapsulate a model protein with a low isoelectric point (pI) with relative ease. However, attempts at modifying the liposome surface charge to a positive state for encapsulating proteins with higher pI values did not yield particles with a core/shell structure.
KW - Core/shell-structured particles
KW - Lecithin
KW - Liposomes
KW - Pluronic
KW - Protein encapsulation
UR - http://www.scopus.com/inward/record.url?scp=85218418707&partnerID=8YFLogxK
U2 - 10.1016/j.jfoodeng.2025.112540
DO - 10.1016/j.jfoodeng.2025.112540
M3 - Article
AN - SCOPUS:85218418707
SN - 0260-8774
VL - 395
JO - Journal of Food Engineering
JF - Journal of Food Engineering
M1 - 112540
ER -