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Preparation and characterization of catalase‐loaded solid lipid nanoparticles based on soybean phosphatidylcholine
Author(s) -
Qi Ce,
Chen Yan,
Huang JianHua,
Jin QingZhe,
Wang XingGuo
Publication year - 2011
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.4646
Subject(s) - tripalmitin , chromatography , chemistry , catalase , solid lipid nanoparticle , zeta potential , acetone , solvent , nuclear chemistry , aqueous two phase system , aqueous solution , nanoparticle , organic chemistry , enzyme , drug delivery , materials science , nanotechnology
Abstract BACKGROUND: High‐purity soybean phosphatidylcholine (SPC) (94%) were prepared using macroporous resin adsorption chromatography previously. Catalase is a food enzyme for promoting health and protecting against many age‐related disease. Solid lipid nanoparticles (SLN) are safe immobilizing systems for efficient protein transportation to biomembranes while avoiding adverse degradation of protein. This study was aimed at developing and characterizing catalase‐loaded SLN using SPC as solubilizers and stabilizing agents, to protect catalase from proteolysis. RESULTS: Catalase‐loaded SLN were prepared by the double emulsification method and solvent evaporation techniques, using acetone–methylene chloride (1:1, v/v) as an organic solvent, SPC–tripalmitin as oil phase and Poloxamer 188 as a surfactant. The optimized SLN were prepared using an SPC:tripalmitin ratio of 5% (w/w), 20 s plus 30 s sonication, 20 g L −1 Poloxamer 188 and 1:2 (v/v) of oily phase:outer aqueous phase ratio. The mean particle size of SLN was 296.0 ± 7.0 nm, polydispersity index range and zeta potential were 0.322–0.354 and − 36.4 ± 0.6, respectively, and encapsulation efficiency reached its maximum of 77.9 ± 1.56%. Catalase, which was found to distribute between the solid lipid and inner aqueous phase, was gradually released from SLN up to 20% within 20 h. Catalase‐loaded SLN had stably retained 30% of H 2 O 2 ‐degrading activity for at least 24 h in a proteolytic environment, while free catalase lost its activity within 1 h. CONCLUSION: Catalase can indeed be loaded in tripalmitin‐based SLN using SPC as solubilizers and stabilizing agents, which protected it against proteolysis, suggesting the potential application of SPC in delivery and protection of functional food enzyme. Copyright © 2011 Society of Chemical Industry