Stable Dried Catalase Particles Prepared by Electrospraying
Therapeutic proteins and peptides are clinically important, offering potency while reducing the potential for off-target effects. Research interest in developing therapeutic polypeptides has grown significantly during the last four decades. However, despite the growing research effort, maintaining t...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-07-01
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| Series: | Nanomaterials |
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| Online Access: | https://www.mdpi.com/2079-4991/12/14/2484 |
| _version_ | 1797444733896753152 |
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| author | Corinna S. Schlosser Steve Brocchini Gareth R. Williams |
| author_facet | Corinna S. Schlosser Steve Brocchini Gareth R. Williams |
| author_sort | Corinna S. Schlosser |
| collection | DOAJ |
| description | Therapeutic proteins and peptides are clinically important, offering potency while reducing the potential for off-target effects. Research interest in developing therapeutic polypeptides has grown significantly during the last four decades. However, despite the growing research effort, maintaining the stability of polypeptides throughout their life cycle remains a challenge. Electrohydrodynamic (EHD) techniques have been widely explored for encapsulation and delivery of many biopharmaceuticals. In this work, we explored monoaxial electrospraying for encapsulation of bovine liver catalase, investigating the effects of the different components of the electrospraying solution on the integrity and bioactivity of the enzyme. The catalase was successfully encapsulated within polymeric particles made of polyvinylpyrrolidone (PVP), dextran, and polysucrose. The polysorbate 20 content within the electrospraying solution (50 mM citrate buffer, pH 5.4) affected the catalase loading—increasing the polysorbate 20 concentration to 500 μg/mL resulted in full protein encapsulation but did not prevent loss in activity. The addition of ethanol (20% <i>v/v</i>) to a fully aqueous solution improves the electrospraying process by reducing surface tension, without loss of catalase activity. The polymer type was shown to have the greatest impact on preserving catalase activity within the electrosprayed particles. When PVP was the carrier there was no loss in activity compared with fresh aqueous solutions of catalase. The optimum particles were obtained from a 20% <i>w/v</i> PVP or 30% <i>w/v</i> PVP-trehalose (1:1 <i>w/w</i>) solution. The addition of trehalose confers stability advantages to the catalase particles. When trehalose-PVP particles were stored at 5 °C, enzymatic activity was maintained over 3 months, whereas for the PVP-only analogue a 50% reduction in activity was seen. This demonstrates that processing catalase by monoaxial electrospraying can, under optimised conditions, result in stable polymeric particles with no loss of activity. |
| first_indexed | 2024-03-09T13:15:49Z |
| format | Article |
| id | doaj.art-bf5ff524d9c441b4aa8246c0a71acb81 |
| institution | Directory Open Access Journal |
| issn | 2079-4991 |
| language | English |
| last_indexed | 2024-03-09T13:15:49Z |
| publishDate | 2022-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Nanomaterials |
| spelling | doaj.art-bf5ff524d9c441b4aa8246c0a71acb812023-11-30T21:36:25ZengMDPI AGNanomaterials2079-49912022-07-011214248410.3390/nano12142484Stable Dried Catalase Particles Prepared by ElectrosprayingCorinna S. Schlosser0Steve Brocchini1Gareth R. Williams2UCL School of Pharmacy, University College London, 29-39 Brunswick Square, London WC1N 1AX, UKUCL School of Pharmacy, University College London, 29-39 Brunswick Square, London WC1N 1AX, UKUCL School of Pharmacy, University College London, 29-39 Brunswick Square, London WC1N 1AX, UKTherapeutic proteins and peptides are clinically important, offering potency while reducing the potential for off-target effects. Research interest in developing therapeutic polypeptides has grown significantly during the last four decades. However, despite the growing research effort, maintaining the stability of polypeptides throughout their life cycle remains a challenge. Electrohydrodynamic (EHD) techniques have been widely explored for encapsulation and delivery of many biopharmaceuticals. In this work, we explored monoaxial electrospraying for encapsulation of bovine liver catalase, investigating the effects of the different components of the electrospraying solution on the integrity and bioactivity of the enzyme. The catalase was successfully encapsulated within polymeric particles made of polyvinylpyrrolidone (PVP), dextran, and polysucrose. The polysorbate 20 content within the electrospraying solution (50 mM citrate buffer, pH 5.4) affected the catalase loading—increasing the polysorbate 20 concentration to 500 μg/mL resulted in full protein encapsulation but did not prevent loss in activity. The addition of ethanol (20% <i>v/v</i>) to a fully aqueous solution improves the electrospraying process by reducing surface tension, without loss of catalase activity. The polymer type was shown to have the greatest impact on preserving catalase activity within the electrosprayed particles. When PVP was the carrier there was no loss in activity compared with fresh aqueous solutions of catalase. The optimum particles were obtained from a 20% <i>w/v</i> PVP or 30% <i>w/v</i> PVP-trehalose (1:1 <i>w/w</i>) solution. The addition of trehalose confers stability advantages to the catalase particles. When trehalose-PVP particles were stored at 5 °C, enzymatic activity was maintained over 3 months, whereas for the PVP-only analogue a 50% reduction in activity was seen. This demonstrates that processing catalase by monoaxial electrospraying can, under optimised conditions, result in stable polymeric particles with no loss of activity.https://www.mdpi.com/2079-4991/12/14/2484electrosprayingproteinsbovine liver catalasesolid-state protein formulationprotein stability |
| spellingShingle | Corinna S. Schlosser Steve Brocchini Gareth R. Williams Stable Dried Catalase Particles Prepared by Electrospraying Nanomaterials electrospraying proteins bovine liver catalase solid-state protein formulation protein stability |
| title | Stable Dried Catalase Particles Prepared by Electrospraying |
| title_full | Stable Dried Catalase Particles Prepared by Electrospraying |
| title_fullStr | Stable Dried Catalase Particles Prepared by Electrospraying |
| title_full_unstemmed | Stable Dried Catalase Particles Prepared by Electrospraying |
| title_short | Stable Dried Catalase Particles Prepared by Electrospraying |
| title_sort | stable dried catalase particles prepared by electrospraying |
| topic | electrospraying proteins bovine liver catalase solid-state protein formulation protein stability |
| url | https://www.mdpi.com/2079-4991/12/14/2484 |
| work_keys_str_mv | AT corinnasschlosser stabledriedcatalaseparticlespreparedbyelectrospraying AT stevebrocchini stabledriedcatalaseparticlespreparedbyelectrospraying AT garethrwilliams stabledriedcatalaseparticlespreparedbyelectrospraying |