Abstract
The glass transition behavior of processed fish muscles (bonito, tuna, mackerel, sea bream, cod) and its muscle protein fractions (sarcoplasmic and myofibrillar proteins) were studied using differential scanning calorimetry. Each dried processed fish muscle and the extracted protein fractions showed clear glass transition phenomenon. The Tg values of muscles and myofibrillar proteins from red muscle fishes tended to be lower than those from white muscle fishes though there was no difference on Tg of sarcoplasmic proteins. The Tg value of whole muscle was considerably lower than that of extracted protein fractions because of the plasticizing effects of low molecular weight materials contained in the muscle.
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Hashimoto, T., Suzuki, T., Hagiwara, T., & Takai, R. (2004). Study on the transition for several processed fish muscles and its protein fractions using differential scanning calorimetry. Fisheries Science, 70(6), 1144–1152. https://doi.org/10.1111/j.1444-2906.2004.00916.x
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