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| one publication added to basket [293786] |
Kinetics of heat induced muscle protein denaturation of brown shrimp (Crangon crangon)
Verhaeghe, T.; Vlaemynck, G.; De Block, J.; Van Weyenberg, S.; Braeckman, R.; Hendrickx, M.E. (2016). Kinetics of heat induced muscle protein denaturation of brown shrimp (Crangon crangon). Journal of Food Engineering 191: 88-94. https://dx.doi.org/10.1016/j.jfoodeng.2016.07.010
In: Journal of Food Engineering. Elsevier SCI Ltd: Oxford. ISSN 0260-8774; e-ISSN 1873-5770, meer
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| Trefwoorden |
Crangon crangon (Linnaeus, 1758) [WoRMS]
Marien/Kust |
| Author keywords |
Crangon crangon; Muscle protein denaturation; Actin; Thermal stability;Kinetics |
| Auteurs | | Top |
- Verhaeghe, T.
- Vlaemynck, G., meer
- De Block, J., meer
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- Van Weyenberg, S., meer
- Braeckman, R., meer
- Hendrickx, M.E., meer
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| Abstract |
To optimize the quality of cooked brown shrimp (Crangon crangon), quantitative data on the influence of all relevant process parameters (treatment time, temperature, NaCl concentration) on several quality attributes are required. Surprisingly, kinetic data and models on heat induced quality changes of brown shrimp are scarce. In this study, the denaturation of muscle proteins was studied by differential scanning calorimetry. The thermal denaturation kinetics of actin, the most heat resistant muscle protein, were determined and showed a first order decay with k72 °C = 0.038 ± 0.001 min−1 and Ea = 388 ± 7.3 kJ/mol. Spiking experiments showed that NaCl (concentrations in the range from 1 to 5% NaCl) had a negligible influence on the actin thermal stability. The kinetic data obtained can be used to quantitatively evaluate the doneness of cooked shrimp. |
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