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Enzyme dehydration using Microglassification™ preserves the protein's structure and function.

Publication ,  Journal Article
Aniket; Gaul, DA; Bitterfield, DL; Su, JT; Li, VM; Singh, I; Morton, J; Needham, D
Published in: Journal of pharmaceutical sciences
February 2015

Controlled enzyme dehydration using a new processing technique of Microglassification™ has been investigated. Aqueous solution microdroplets of lysozyme, α-chymotrypsin, catalase, and horseradish peroxidase were dehydrated in n-pentanol, n-octanol, n-decanol, triacetin, or butyl lactate, and changes in their structure and function were analyzed upon rehydration. Water solubility and microdroplet dissolution rate in each solvent decreased in the order: butyl lactate > n-pentanol > triacetin > n-octanol > n-decanol. Enzymes Microglassified™ in n-pentanol retained higher activity (93%-98%) than n-octanol (78%-85%) or n-decanol (75%-89%), whereas those Microglassified™ in triacetin (36%-75%) and butyl lactate (48%-79%) retained markedly lower activity. FTIR spectroscopy analyses showed α-helix to β-sheet transformation for all enzymes upon Microglassification™, reflecting a loss of bound water in the dried state; however, the enzymes reverted to native-like conformation upon rehydration. Accelerated stressed-storage tests using Microglassified™ lysozyme showed a significant (p < 0.01) decrease in enzymatic activity from 46,560 ± 2736 to 31,060 ± 4327 units/mg after 3 months of incubation; however, it was comparable to the activity of the lyophilized formulation throughout the test period. These results establish Microglassification™ as a viable technique for enzyme preservation without affecting its structure or function.

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Published In

Journal of pharmaceutical sciences

DOI

EISSN

1520-6017

ISSN

0022-3549

Publication Date

February 2015

Volume

104

Issue

2

Start / End Page

640 / 651

Related Subject Headings

  • Pharmacology & Pharmacy
  • Muramidase
  • Microtechnology
  • Horseradish Peroxidase
  • Glass
  • Freeze Drying
  • Enzyme Activation
  • Desiccation
  • Chymotrypsin
  • Chickens
 

Citation

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Aniket, ., Gaul, D. A., Bitterfield, D. L., Su, J. T., Li, V. M., Singh, I., … Needham, D. (2015). Enzyme dehydration using Microglassification™ preserves the protein's structure and function. Journal of Pharmaceutical Sciences, 104(2), 640–651. https://doi.org/10.1002/jps.24279
Aniket, Sharda, David A. Gaul, Deborah L. Bitterfield, Jonathan T. Su, Victoria M. Li, Ishita Singh, Jackson Morton, and David Needham. “Enzyme dehydration using Microglassification™ preserves the protein's structure and function.Journal of Pharmaceutical Sciences 104, no. 2 (February 2015): 640–51. https://doi.org/10.1002/jps.24279.
Aniket, Gaul DA, Bitterfield DL, Su JT, Li VM, Singh I, et al. Enzyme dehydration using Microglassification™ preserves the protein's structure and function. Journal of pharmaceutical sciences. 2015 Feb;104(2):640–51.
Aniket, Sharda, et al. “Enzyme dehydration using Microglassification™ preserves the protein's structure and function.Journal of Pharmaceutical Sciences, vol. 104, no. 2, Feb. 2015, pp. 640–51. Epmc, doi:10.1002/jps.24279.
Aniket, Gaul DA, Bitterfield DL, Su JT, Li VM, Singh I, Morton J, Needham D. Enzyme dehydration using Microglassification™ preserves the protein's structure and function. Journal of pharmaceutical sciences. 2015 Feb;104(2):640–651.
Journal cover image

Published In

Journal of pharmaceutical sciences

DOI

EISSN

1520-6017

ISSN

0022-3549

Publication Date

February 2015

Volume

104

Issue

2

Start / End Page

640 / 651

Related Subject Headings

  • Pharmacology & Pharmacy
  • Muramidase
  • Microtechnology
  • Horseradish Peroxidase
  • Glass
  • Freeze Drying
  • Enzyme Activation
  • Desiccation
  • Chymotrypsin
  • Chickens