Investigation of the Impact of Saccharides on the Relative Activity of Trypsin and Catalase after Droplet and Spray Drying DOI Creative Commons

Johanna Dieplinger,

Christina Möser,

Gerhard König

и другие.

Pharmaceutics, Год журнала: 2023, Номер 15(10), С. 2504 - 2504

Опубликована: Окт. 21, 2023

While using saccharides as stabilizers for therapeutic protein drying is common, the mechanisms underlying stabilization during remain largely unexplored. Herein, we investigated effect of different saccharides, trehalose dihydrate (TD), dextran (DEX), and hydroxypropyl β-cyclodextrins (low substitution-HP high substitution-HPB), on relative activities enzymes trypsin catalase miniaturized (MD) or spray (SD). For trypsin, presence especially HP, was beneficial, it significantly improved enzyme activity following MD. The HPB preserved trypsin's MD SD. Adding did not show a notable improvement in activities. Increasing TD beneficial SD catalase, indicated by increased activity. Molecular docking molecular dynamics simulations oftrypsin with HP revealed influence their substitution binding affinity enzyme. A higher to bind itself observed simulations. Experimentally, reduction mainly MD, attributable droplet temperature than from experiments aggregation propensity modeling helped elucidate impact size preserving drying.

Язык: Английский

Investigation of the Impact of Saccharides on the Relative Activity of Trypsin and Catalase after Droplet and Spray Drying DOI Creative Commons

Johanna Dieplinger,

Christina Möser,

Gerhard König

и другие.

Pharmaceutics, Год журнала: 2023, Номер 15(10), С. 2504 - 2504

Опубликована: Окт. 21, 2023

While using saccharides as stabilizers for therapeutic protein drying is common, the mechanisms underlying stabilization during remain largely unexplored. Herein, we investigated effect of different saccharides, trehalose dihydrate (TD), dextran (DEX), and hydroxypropyl β-cyclodextrins (low substitution-HP high substitution-HPB), on relative activities enzymes trypsin catalase miniaturized (MD) or spray (SD). For trypsin, presence especially HP, was beneficial, it significantly improved enzyme activity following MD. The HPB preserved trypsin's MD SD. Adding did not show a notable improvement in activities. Increasing TD beneficial SD catalase, indicated by increased activity. Molecular docking molecular dynamics simulations oftrypsin with HP revealed influence their substitution binding affinity enzyme. A higher to bind itself observed simulations. Experimentally, reduction mainly MD, attributable droplet temperature than from experiments aggregation propensity modeling helped elucidate impact size preserving drying.

Язык: Английский

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