Encapsulation of Alcohol Dehydrogenase in Mannitol by Spray Drying

Hirokazu Shiga,Hidefumi Yoshii,Tze Neoh,Takeshi Furuta,Hiromi Joreau

doi:10.3390/pharmaceutics6010185

Hirokazu Shiga, Hidefumi Yoshii + Show 3 more

Open Access

https://doi.org/10.3390/pharmaceutics6010185

Copy DOI

Abstract

The retention of the enzyme activity of alcohol dehydrogenase (ADH) has been studied in various drying processes such as spray drying. The aim of this study is to encapsulate ADH in mannitol, either with or without additive in order to limit the thermal denaturation of the enzyme during the drying process. The retention of ADH activity was investigated at different drying temperatures. When mannitol was used, the encapsulated ADH was found inactive in all the dried powders. This is presumably due to the quick crystallization of mannitol during spray drying that resulted in the impairment of enzyme protection ability in comparison to its amorphous form. Maltodextin (dextrose equivalent = 11) was used to reduce the crystallization of mannitol. The addition of maltodextrin increased ADH activity and drastically changed the powder X-ray diffractogram of the spray-dried powders.

Highlights

In pharmaceutical formulation researches, the drying process is often used in order to stabilize and preserve biologically active molecules such as enzymes contained in solutions
Broadhead et al [5] studied the effect of drying temperature on the activity loss of β-galactosidase during spray drying
The retention of alcohol dehydrogenase (ADH) activity was investigated at inlet air temperature of 60, 80, 90, 100 and 120 °C

Summary

Introduction

In pharmaceutical formulation researches, the drying process is often used in order to stabilize and preserve biologically active molecules such as enzymes contained in solutions. Among the conventional drying processes that rely on evaporation, spray drying is a well-established method for processing liquids into powders. Spray drying utilizes heat from a hot gas stream to evaporate microdispersed droplets created by atomization of a continuous liquid feed, offering faster, less harsh, and cost-effective solvent evaporation, it is more adapted to produce enzyme powder [1]. Broadhead et al [5] studied the effect of drying temperature on the activity loss of β-galactosidase during spray drying. They found that higher outlet temperature of the drying air resulted in extensive enzyme denaturation. It is important to control the drying temperature in order to minimize the activity loss of enzymes

Objectives

Methods

Results

Conclusion