Transformation of cyclodextrin glucanotransferase (CGTase) from aqueous suspension to fine solid particles via electrospraying
In this study, the potential of electrohydrodynamic atomization or electrospraying to produce nanometer-order CGTase particles from aqueous suspension was demonstrated. CGTase enzyme was prepared in acetate buffer solution (1% v/v), followed by electrospraying in stable Taylor cone-jet mode. The dep...
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Elsevier Inc.
2014
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2-s2.0-84905391050 Saallah S.; Naim M.N.; Mokhtar M.N.; Abu Bakar N.F.; Gen M.; Lenggoro I.W. Transformation of cyclodextrin glucanotransferase (CGTase) from aqueous suspension to fine solid particles via electrospraying 2014 Enzyme and Microbial Technology 64-65 10.1016/j.enzmictec.2014.06.002 https://www.scopus.com/inward/record.uri?eid=2-s2.0-84905391050&doi=10.1016%2fj.enzmictec.2014.06.002&partnerID=40&md5=4b17df68e307aff0a4f9ce6d1db577a9 In this study, the potential of electrohydrodynamic atomization or electrospraying to produce nanometer-order CGTase particles from aqueous suspension was demonstrated. CGTase enzyme was prepared in acetate buffer solution (1% v/v), followed by electrospraying in stable Taylor cone-jet mode. The deposits were collected on aluminium foil (collector) at variable distances from the tip of spraying needle, ranging from 10 to 25 cm. The Coulomb fission that occurs during electrospraying process successfully transformed the enzyme to the solid state without any functional group deterioration. The functional group verification was conducted by FTIR analysis. Comparison between the deposit and the as-received enzyme in dry state indicates almost identical spectra. By increasing the distance of the collector from the needle tip, the average particle size of the solidified enzyme was reduced from 200 ± 117 nm to 75 ± 34 nm. The average particle sizes produced from the droplet fission were in agreement with the scaling law models. Enzyme activity analysis showed that the enzyme retained its initial activity after the electrospraying process. The enzyme particles collected at the longest distance (25 cm) demonstrated the highest enzyme activity, which indicates that the activity was controlled by the enzyme particle size. © 2014 Elsevier Inc.. Elsevier Inc. 1410229 English Article All Open Access; Green Open Access |
author |
Saallah S.; Naim M.N.; Mokhtar M.N.; Abu Bakar N.F.; Gen M.; Lenggoro I.W. |
spellingShingle |
Saallah S.; Naim M.N.; Mokhtar M.N.; Abu Bakar N.F.; Gen M.; Lenggoro I.W. Transformation of cyclodextrin glucanotransferase (CGTase) from aqueous suspension to fine solid particles via electrospraying |
author_facet |
Saallah S.; Naim M.N.; Mokhtar M.N.; Abu Bakar N.F.; Gen M.; Lenggoro I.W. |
author_sort |
Saallah S.; Naim M.N.; Mokhtar M.N.; Abu Bakar N.F.; Gen M.; Lenggoro I.W. |
title |
Transformation of cyclodextrin glucanotransferase (CGTase) from aqueous suspension to fine solid particles via electrospraying |
title_short |
Transformation of cyclodextrin glucanotransferase (CGTase) from aqueous suspension to fine solid particles via electrospraying |
title_full |
Transformation of cyclodextrin glucanotransferase (CGTase) from aqueous suspension to fine solid particles via electrospraying |
title_fullStr |
Transformation of cyclodextrin glucanotransferase (CGTase) from aqueous suspension to fine solid particles via electrospraying |
title_full_unstemmed |
Transformation of cyclodextrin glucanotransferase (CGTase) from aqueous suspension to fine solid particles via electrospraying |
title_sort |
Transformation of cyclodextrin glucanotransferase (CGTase) from aqueous suspension to fine solid particles via electrospraying |
publishDate |
2014 |
container_title |
Enzyme and Microbial Technology |
container_volume |
64-65 |
container_issue |
|
doi_str_mv |
10.1016/j.enzmictec.2014.06.002 |
url |
https://www.scopus.com/inward/record.uri?eid=2-s2.0-84905391050&doi=10.1016%2fj.enzmictec.2014.06.002&partnerID=40&md5=4b17df68e307aff0a4f9ce6d1db577a9 |
description |
In this study, the potential of electrohydrodynamic atomization or electrospraying to produce nanometer-order CGTase particles from aqueous suspension was demonstrated. CGTase enzyme was prepared in acetate buffer solution (1% v/v), followed by electrospraying in stable Taylor cone-jet mode. The deposits were collected on aluminium foil (collector) at variable distances from the tip of spraying needle, ranging from 10 to 25 cm. The Coulomb fission that occurs during electrospraying process successfully transformed the enzyme to the solid state without any functional group deterioration. The functional group verification was conducted by FTIR analysis. Comparison between the deposit and the as-received enzyme in dry state indicates almost identical spectra. By increasing the distance of the collector from the needle tip, the average particle size of the solidified enzyme was reduced from 200 ± 117 nm to 75 ± 34 nm. The average particle sizes produced from the droplet fission were in agreement with the scaling law models. Enzyme activity analysis showed that the enzyme retained its initial activity after the electrospraying process. The enzyme particles collected at the longest distance (25 cm) demonstrated the highest enzyme activity, which indicates that the activity was controlled by the enzyme particle size. © 2014 Elsevier Inc.. |
publisher |
Elsevier Inc. |
issn |
1410229 |
language |
English |
format |
Article |
accesstype |
All Open Access; Green Open Access |
record_format |
scopus |
collection |
Scopus |
_version_ |
1809678487891476480 |