Zobrazeno 1 - 10
of 55
pro vyhledávání: '"Allan H. Clark"'
Publikováno v:
Biomacromolecules. 5:2430-2438
Oscillatory shear rheometry has been used to study the gelation of beta-lactoglobulin at ambient in 50% v/v trifluoroethanol (TFE)/pH 7 aqueous buffer and in 50% v/v ethanol (EtOH)/water at pH 2. In contrast to what was found on heating aqueous solut
Publikováno v:
Langmuir. 18:7174-7181
Biology provides us with a unique set of self-assembled fibrillar networks in the form of amyloid fibrils, derived from the self-assembly of a number of peptides or misfolded proteins. These, in turn, are associated with a number of diseases such as
Publikováno v:
Rheologica Acta. 41:276-284
Creep and recovery experiments have been used to investigate the behaviour of heat set protein gels exemplified by those prepared from β-lactoglobulin (β-Lg). Some initial experiments were also performed on heat set BSA gels to establish appropriat
Publikováno v:
Carbohydrate Polymers. 46:383-391
Aqueous cold-set gels from mixtures of agarose and sodium gellan have been characterised structurally and mechanically using optical and electron microscopy, turbidity measurements, differential scanning calorimetry, mechanical spectroscopy and compr
Autor:
David R. Martin, Allan H. Clark, Ian T. Norton, Timothy J. Foster, Pierre Aymard, Kevin P. Plucknett
Publikováno v:
Biopolymers. 59:131-144
Using a multitechnique approach, two temperature domains have been identified in agarose gelation. Below 35°C, fast gelation results in strong, homogeneous and weakly turbid networks. The correlation length, evaluated from the wavelength dependence
Publikováno v:
Langmuir. 17:4372-4379
Mixtures of globular protein (β-lactoglobulin) aggregates and polysaccharides (κ-carrageenan) were studied using dynamic and static light scattering, size exclusion chromatography, and optical microscopy. Above a critical κ-carrageenan concentrati
Publikováno v:
Langmuir. 17:4380-4385
Aqueous solutions of globular proteins (β-lactoglobulin) at pH 7 and 0.1 M NaCl were heated in the presence of various concentrations of polysaccharide (κ-carrageenan). The fraction of unaggregated proteins was determined as a function of heating t
Heat-induced gelation of globular proteins: part 3. Molecular studies on low pH β-lactoglobulin gels
Publikováno v:
International Journal of Biological Macromolecules. 28:41-50
Heat-set gels and aggregates from beta-lactoglobulin (beta-Lg), one of the major globular proteins from milk, have been studied on a molecular distance scale using negative-staining transmission electron microscopy (TEM), wide-angle X-ray diffraction
Publikováno v:
Macromolecules. 33:7029-7037
Mixed globular protein gels, or gel composites, based on heating solutions of proteins from milk have been investigated for many years, although the great majority of these studies have used rather crude whey isolates containing a fixed ratio of the
Publikováno v:
Macromolecules. 32:2542-2552
The structure and internal dynamics of β-lactoglobulin aggregates formed after heat-induced denaturation at pH 2 and different ionic strengths were investigated using light, neutron, and X-ray scattering. Polydisperse aggregates are formed with a ri