Intercalation of papain enzyme into hydrotalcite type layered double hydroxide

N. Zou, J. Plank

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Abstract

Intercalation of proteolytic enzyme papain into hydrotalcite type LDH structure was achieved by controlled co-precipitation at pH=9.0 in the presence of papain. Characterization of the MgAl-papain-LDH phase was carried out using X-ray powder diffraction (XRD), elemental analysis, infrared spectroscopy (IR) and thermogravimetry (TG). According to XRD, papain was successfully intercalated. The d-value for the basal spacing of MgAl-papain-LDH was found at ∼5.3 nm. Consequently, original papain (hydrodynamic diameter ∼7.2 nm) attains a compressed conformation during intercalation. Formation of MgAl-papain-LDH was confirmed by elemental analysis and transmission electron microscopy (TEM). Under SEM, MgAl-papain-LDH phases appear as nanothin platelets which are intergrown to flower-like aggregates. Steric size and activity of the enzyme was retained after deintercalation from MgAl-LDH framework, as was evidenced by light scattering and UV/vis measurements. Thus, papain is not denatured during intercalation, and LDH is a suitable host structure which can provide a time-controlled release of the biomolecule.

Original languageEnglish
Pages (from-to)1127-1130
Number of pages4
JournalJournal of Physics and Chemistry of Solids
Volume73
Issue number9
DOIs
StatePublished - Sep 2012
Externally publishedYes

Keywords

  • A. Nanostructures
  • B. Chemical synthesis
  • B. Electron microscopy
  • C. Thermogravimetric analysis (TGA)
  • C. X-ray diffraction

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