0000000000615121
AUTHOR
Takeshi Furuta
showing 3 related works from this author
Encapsulation of Alcohol Dehydrogenase in Mannitol by Spray Drying
2014
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)…
Influence of emulsion and powder size on the stability of encapsulated d-limonene by spray drying
2005
Abstract The microencapsulation of d -limonene by spray drying was investigated with respect to the effects of emulsion droplet size, powder particle size, as well as to the effects of various kinds of matrices (gum arabic, maltodextrin, and modified starch) on its stability. It was realized by studying release characteristics and oxidative stability during storage. The release and the oxidation decreased deeply with an increase in powder and emulsion particle size for gum arabic and maltodextrin materials. Further, the distributions of emulsion size in the powder showed an increase in the fraction of large emulsion droplets and changed to a bimodal distribution. However, the modified starc…
Effects of protein on retention of ADH enzyme activity encapsulated in trehalose matrices by spray drying
2008
The retention of the enzymatic activity of alcohol dehydrogenase (ADH) on spray drying was examined under various drying conditions. Trehalose was used in the formulation of feed stocks for the spray drying. The retention of ADH activity was dependent on the concentration of ADH in the feed solution. The addition of other proteins, such as bovine serum albumin and β-lactoglobulin, exhibited an additional improvement of the retention of ADH activity. The inlet and outlet temperature of the drying air was another key factor for the enzyme activity on the spray drying. The surface morphology of the spray-dried particle was changed drastically with the addition of proteins.