4 research outputs found
Overtures - 1983
Contributers include: Isabelle Wasilewski, Gerald Majer, Cynthia Poe, Larry Swieca, Kelly O\u27Mahoney, Michael Davidson, Susan Mitchell, Sherry Payne, Enid Levenger Powell, Anne Siegel, Sara Esgate, Albert DeGenova, Pamela Miller, William T. Lawlor, Alice Ryerson, Jim Elledge, Gertrude Rubin, Gary Byron, Jeanette L. Fleming, Eleanor Gordon, Jacqueline Disler, John Dickson, Mary Trimble, Isabelle Wasilewski, Carlos Lopez, Daryl Jensen, Rosemary Strabrawa, Timothy Bell, Marta Jankowski, Sherry Payne, Kelly O\u27Mahoneyhttps://neiudc.neiu.edu/overtures/1006/thumbnail.jp
Overtures - 1981
Contributers include: J.M. Marshall, Andrew Byrne, Anne Haskins, Gertrude Rubin, A. Bernard Stein, Marc Davidson, Jill Johnson, Kelly O\u27Mahoney, Lynda Clemmer, Nancy Haglerhttps://neiudc.neiu.edu/overtures/1004/thumbnail.jp
Overtures - 1982
Contributers include: Kelly O\u27Mahoney, Cynthia Poe, Vesle Fenstermaker, William T. Lawlor, J.M. Marshall, Jim Elledge, Jeanette Fleming, Kenneth Schulze,https://neiudc.neiu.edu/overtures/1005/thumbnail.jp
Self-association of bovine β-casein as influenced by calcium chloride, buffer type and temperature
The aim of this study was to investigate the aggregation behaviour of a pure β-casein (β-CNpure) and a β-casein concentrate (β-CNconc) as a function of temperature, buffer type (pH 6.8) and the presence of CaCl2. The particle size distribution and turbidity of β-casein (β-CN) dispersions were measured by dynamic light-scattering (DLS) and UV/vis spectroscopy between 4 and 55 °C. Upon heating (4–55 °C), the particle size of both β-CN samples increased, indicating self-association via hydrophobic interactions. It was shown that the self-association of β-CN increased with increasing β-CN concentration and that β-CNpure self-associated at significantly lower concentration than β-CNconc. Both turbidity and particle size measurements showed that the β-CN samples had similar aggregation behaviour in water and imidazole buffer (pH 6.8) but differed in sodium phosphate buffer (pH 6.8), especially at higher ionic calcium concentrations. Fourier Transform Infrared (FTIR) spectroscopy revealed very little change in the secondary structure of β-CN during heating (4–55 °C). The microstructure of β-CN aggregates was monitored during heating from 10 to 55 °C, followed by cooling to 10 °C, using polarised light microscopy. Spherical and heterogeneous aggregates were observed when heated at temperatures above 37 °C, which were reversible upon cooling. This study confirmed that β-CN undergoes self-association on heating that reverses upon cooling, with the aggregation process being highly dependent on the purity of β-CN, the solvent type and the presence of ionic calcium