Development of Enzyme Loaded Polyion Complex Vesicle (PICsome): Thermal Stability of Enzyme in PICsome Compartment and Effect of Coencapsulation of Dextran on Enzyme Activity

Hengmin Tang, Yuki Sakamura, Takeshi Mori, Yoshiki Katayama, Akihiro Kishimura

研究成果: ジャーナルへの寄稿記事

4 引用 (Scopus)

抄録

Applications of enzymes are intensively studied, particularly for biomedical applications. However, encapsulation or immobilization of enzymes without deactivation and long-term use of enzymes are still at issue. This study focuses on the polymeric vesicles “PICsomes” for encapsulation of enzymes to develop a hecto-nanometer-scaled enzyme-loaded reactor. The catalytic activity of a PICsome-based enzyme nanoreactor is carefully examined to clarify the effect of compartmentalization by PICsome. Encapsulation by PICsome provides a stability enhancement of enzymes after 24 h incubation at 37 °C, which is particularly helpful for maintaining the high effective concentration of β-galactosidase. Moreover, to control the microenvironment inside the nanoreactor, a large amount of dextran, a neutral macromolecule, is encapsulated together with β-galactosidase in the PICsome. The resulting dextran-coloaded nanoreactor contributes to the enhancement of enzyme stability, even after exposure to 24 h incubation at −20 °C, mainly due to the antifreezing effect. (Figure presented.).

元の言語英語
記事番号1600542
ジャーナルMacromolecular Bioscience
17
発行部数8
DOI
出版物ステータス出版済み - 8 1 2017

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Enzyme Stability
Dextran
Enzyme activity
Dextrans
Thermodynamic stability
Enzymes
Hot Temperature
Nanoreactors
Galactosidases
Encapsulation
Immobilization
Macromolecules
Catalyst activity

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

これを引用

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AU - Kishimura, Akihiro

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