Intercalation of cellulase enzyme into a hydrotalcite layer structure. (January 2015)

• Record Type: Journal Article
• Authors: Zou, N.; Plank, J.
• Is Part Of: Journal of physics and chemistry of solids. Volume 76(2015:Jan.)
• Page Start: 34
• Page End: 39
• Publication Date: 2015-01
• Subjects: A. Nanostructures -- A. Multilayers -- B. Chemical synthesis -- C. X-ray diffraction -- C. Electron microscopy; Solids -- Periodicals; Solides -- Périodiques; Solids; Periodicals; 530.41
• DOI: 10.1016/j.jpcs.2014.08.005
• Languages: English
• ISSNs: 0022-3697

Abstract

Abstract: A new inorganic–organic hybrid material whereby cellulase enzyme is incorporated into a hydrotalcite type layered double hydroxide (LDH) structure is reported. The Mg2 Al–cellulase–LDH was synthesized via co-precipitation from Mg/Al nitrate at pH=9.6. Characterization was performed using X-ray powder diffraction (XRD), small angle X-ray scattering (SAXS), elemental analysis, infrared spectroscopy (IR) and thermogravimetry (TG). From XRD and SAXS measurements, a d -value of ~5.0 nm was identified for the basal spacing of the Mg2 Al–cellulase–LDH. Consequently, the cellulase enzyme (hydrodynamic diameter ~6.6 nm) attains a slightly compressed conformation when intercalated. Formation of the LDH hybrid was also confirmed via scanning electron microscopy (SEM) and transmission electron microscopy (TEM). Mg2 Al–cellulase–LDH phases appear as ~20 nm thin foils which are intergrown to flower-like aggregates. Activity of the enzyme was retained after deintercalation from the Mg2 Al–LDH framework using anion exchange. Accordingly, cellulase is not denatured during the intercalation process, and LDH presents a suitable host structure for time-controlled release of the biomolecule. graphical abstract: Highlights: Cellulase enzyme was intercalated into a layered double hydroxide to yield Mg2 Al–cellulase–LDH. Synthesis of the cellulase–LDH composite was achieved via controlled co-precipitation. An interlayer distance of 5.0 nm was found for the Mg2 Al–cellulase–LDH. Cellulase enzyme can be released from the LDH structure via anion-exchange. Cellulase maintains its initial size and activity after release from the LDH.