1. Liposomal Microcapsulation of Enzymes by Proliposome Method with Chitosan-Coating
- Author
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Kiyoshi Matsumoro, Yoshihiro Shimoda, and Hiroya Ishikawa
- Subjects
chemistry.chemical_classification ,Liposome ,Chromatography ,Chitosan coating ,Chitosan ,chemistry.chemical_compound ,Enzyme ,Biochemistry ,chemistry ,Soybean Lecithin ,Residual activity ,Alkaline phosphatase ,Agronomy and Crop Science ,Biotechnology - Abstract
Liposomal microcapsules containing enzymes were prepared by proliposome method to improve a stability of enzymes under acidic conditions. Two model enzymes, ~-galactosidase and alkaline phosphatase, were encapsulated by the method wlth soybean lecithins, and their encapsulation behaviors were investigated. The highest encapsulation efficiency was obtained by using 25mg of the enzyme and 250mg of soybean lecithin (fi-galactosidase; 57.30/0, alkaline phosphatase; 53.0010). However, the microcapsules did ' not exhibit the stabilizing effect for ~-galactosidase at pH 3. Chitosan-coating was made for proliposome-capsules to keep enzymatic activity under acidic conditions. The microcapsules coated with >0.50/0 of chitosan 10 showed high stability at pH 3, and encapsulated ~Lgalactosidase was retained 80.70/0 of its activity. Similarly, alkaline phosphatase was highly stabilized by the encapsulation with chitosan-coating. No decrease in the residual activity of encapsulated alkaline phosphatase was observed at pH 5 for 60min, while uncapsulated one lost 53.30/0 of its activity. The activity of encapsulated alkaline phosphatase was kept 20.1 and 59.20/0 for 60min at pH 3 and 4, respectively, while uncapsulated alkaline phosphatase was completely inactivated at these pHs.
- Published
- 2005
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