NDC'01

ENZYME ENCAPSULATION WITH CRYSTAL TRANSFORMATION OF ANHYDROUS TREHALOSE

Hidefumi Yoshii¹, Hirokazu Shiga¹, Minoru Ishikawa¹, Takeshi Furuta¹, Pirkko Forssell², Kaisa Poutanen² and Pekka Linko³
1. Department of Biotechnology, Tottori University, Tottori 680-8552, Japan, E-mail: yoshii@bio.tottori-u.ac.jp
2. VTT Biotechnology, Tekniikantie 4C, Espoo, P.O.Box 15043, FIN-02044 VTT, Finland, E-mail: Pirkko.Forssell@vtt.fi
3. Department of Chemical Technology, Helsinki University of Technology, P.O. Box 6100, FIN-02015 HUT, Finland, E-mail: P.Linko@hut.fi

Keywords: trehalose, encapsulation, crystal transformation

ABSTRACT

Powdery encapsulation of enzyme in trehalose was studied on the basis of the crystal transformation from anhydrous trehalose to hydrous trehalose. This study investigated the effect of hydroxylpropyl- -cyclodextrin (HP- - CD) on protein stability of enzyme encapsulation with crystal transformation of anhydrous trehalose. The activity of the encapsulated enzyme depended on the molar mass of the enzyme owing to crystal transformation of trehalose from anhydrous to hydrous form. The remaining activity of the encapsulated alcohol dehydrogenase (ADH) increased with the use of amorphous anhydrous trehalose and the addition of HP- -CD into the enzyme solution. The activity of the encapsulated enzyme depended on the molar mass of the enzyme due to the crystal transformation of trehalose from anhydrous to hydrous form. The remaining activity of the encapsulated alcohol dehydrogenase (ADH) increased with the use of amorphous anhydrous trehalose and the addition of HP- -CD into the enzyme solution.