• Model System for the Production of Enzyme Modified Cheese (EMC) Flavours.

      Kilcawley, Kieran; Beresford, Tom; Lee, B.; Wilkinson, M.G.; Department of Agriculture, Food and the Marine, Ireland; Irish Dairy Levy Research Trust (Teagasc, 01/04/2002)
      Natural cheese flavour ingredients, in the form of enzyme modified cheeses (EMCs), are widely used in the convenience food industry and can provide high volume added opportunities for the cheese industry. Many EMCs are produced using commercial enzyme preparations and previous studies have indicated that they contain side activities in addition to their stated main activity (see DPRC Report No.10). Therefore, it is critical that the exact enzyme complement of these preparations are known before they can be used to produce EMC of specific requirements on a consistent basis. The scientific basis of rapid enzyme mediated flavour formation in the production of EMCs is not fully understood. Consequently this knowledge gap is a major obstacle in the development of high value cheese flavour ingredients. Hence, a major objective of this project was to deepen the scientific understanding of flavour formation with a view to the production of natural enzyme-mediated dairy flavour ingredients with commercial potential. The ultimate aim was to develop the technology to produce customised high value dairy flavour ingredients in an optimised process.
    • Self-association of bovine β-casein as influenced by calcium chloride, buffer type and temperature

      Li, Meng; Auty, Mark; Crowley, Shane V.; Kelly, Alan L.; O'Mahoney, James A.; Brodkorb, Andre; Irish Dairy Levy Research Trust; Teagasc Walsh Fellowship Programme; MDDT 6261 (Elsevier, 2018-09-25)
      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.