Effect of polyols on the conformational stability and biological activity of a model protein lysozyme.

Somnath Singh, Jagdish Singh

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

The purpose of this study was to investigate the stabilizing action of polyols against various protein degradation mechanisms (eg, aggregation, deamidation, oxidation), using a model protein lysozyme. Differential scanning calorimeter (DSC) was used to measure the thermodynamic parameters, mid point transition temperature and calorimetric enthalpy, in order to evaluate conformational stability. Enzyme activity assay was used to corroborate the DSC results. Mannitol, sucrose, lactose, glycerol, and propylene glycol were used as polyols to stabilize lysozyme against aggregation, deamidation, and oxidation. Mannitol was found to stabilize lysozyme against aggregation, sucrose against deamidation both at neutral pH and at acidic pH, and lactose against oxidation. Stabilizers that provided greater conformational stability of lysozyme against various degradation mechanisms also protected specific enzyme activity to a greater extent. It was concluded that DSC and bioassay could be valuable tools for screening stabilizers in protein formulations.

Original languageEnglish
JournalAAPS PharmSciTech
Volume4
Issue number3
StatePublished - 2003

Fingerprint

polyols
deamidation
Muramidase
lysozyme
calorimeters
bioactive properties
Mannitol
oxidation
Lactose
mannitol
lactose
Sucrose
Proteins
proteins
sucrose
enzyme activity
Propylene Glycol
propylene glycol
Transition Temperature
Enzyme Assays

All Science Journal Classification (ASJC) codes

  • Molecular Medicine
  • Pharmaceutical Science

Cite this

Effect of polyols on the conformational stability and biological activity of a model protein lysozyme. / Singh, Somnath; Singh, Jagdish.

In: AAPS PharmSciTech, Vol. 4, No. 3, 2003.

Research output: Contribution to journalArticle

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