Impact of proteins-κ-carrageenan interactions on foam properties
Foaming properties of κ-carrageenan (κ-C)+β-lactoglobulin (β-lg), native and denatured soy protein and the thermal stability of foams were investigated. Apparent viscosity measurements were used to obtain the gelation rate and maximum viscosity of foams. Gelling and melting temperatures of the solut...
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| Autores principales: | , , , |
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| Formato: | JOUR |
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00236438_v37_n5_p573_Carp |
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| Sumario: | Foaming properties of κ-carrageenan (κ-C)+β-lactoglobulin (β-lg), native and denatured soy protein and the thermal stability of foams were investigated. Apparent viscosity measurements were used to obtain the gelation rate and maximum viscosity of foams. Gelling and melting temperatures of the solutions determined by dynamic rheology were related to the thermal stability of foams. Foam expansion of the mixed κ-C+ protein solutions followed the same order as the pure protein solutions (β-lg>DSP>NSP). However, the presence of κ-C reduced foam expansion due to the higher viscosity of the systems. No liquid drainage or collapse was observed while apparent viscosity was measured. DSP induced a greater synergistic effect with κ-C, reflected in a faster gelling rate and increased foam stability. The thermal stability of foams stored at temperatures between 5°C and 45°C showed significant differences when they were pre-gelled at 5°C. A large increase in foam stability was observed at 25°C, which is above the average T gel and below the melting temperatures of the systems. The kinetic analysis of the process revealed that different mechanisms were involved in the drainage of pre-gelled or non-gelled foams. © 2004 Swiss Society of Food Science and Technology. Published by Elsevier Ltd. All rights reserved. |
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