Entity

Time filter

Source Type

Bristol, United Kingdom

Bilgainya R.,Dr Hari Singh Gour University | Khan F.,Dr Hari Singh Gour University | Mann S.,Center for Organized Matter Chemistry
Materials Science and Engineering C | Year: 2010

Novel polysaccharide sponges containing a network of capillaries and pore structures have been prepared by freeze drying of Ca2+ ion cross-linked sodium carboxymethylcellulose/sodium alginate hydrogels with or without addition of dextran. The iontropic gels consisted of capillaries, 5 to 40 μm in width, which comprised small pores, 1-25 μm in size. Gold, Fe3O4 or TiO2 nanoparticles were encapsulated in the patterned gels and the mechanical strength of the resulting sponges investigated. Crown Copyright © 2009. Source


Sharma K.P.,Center for Organized Matter Chemistry | Zhang Y.,Center for Organized Matter Chemistry | Thomas M.R.,Center for Organized Matter Chemistry | Thomas M.R.,University of Bristol | And 4 more authors.
Journal of Physical Chemistry B | Year: 2014

An anisotropic glucose oxidase-polymer surfactant nanoconjugate is synthesized and shown to exhibit complex temperature-dependent phase behavior in the solvent-free state. At close to room temperature, the nanoconjugate crystallizes as a mesolamellar soft solid with an expanded interlayer spacing of ca. 12 nm and interchain correlation lengths consistent with alkyl tail-tail and PEO-PEO ordering. The soft solid displays a birefringent spherulitic texture and melts at 40 °C to produce a solvent-free liquid protein without loss of enzyme secondary structure. The nanoconjugate melt exhibits a birefringent dendritic texture below the conformation transition temperature (Tc) of glucose oxidase (58 °C) and retains interchain PEO-PEO ordering. Our results indicate that the shape anisotropy of the protein-polymer surfactant globular building block plays a key role in directing mesolamellar formation in the solvent-free solid and suggests that the microstructure observed in the solvent-free liquid protein below Tc is associated with restrictions in the intramolecular motions of the protein core of the nanoconjugate. © 2014 American Chemical Society. Source

Discover hidden collaborations