Abstract

Because of the composition and structural complexity of crustacean shells, their color change mechanism during thermal processing remains unclear. This study identified and characterized two intrinsic protein components, hemocyanin (Lv-Hc) and β-1,3-glucan-binding protein (Lv-BGBP) from Litopenaeus vannamei shrimp shells by a combination of ion-exchange chromatography, gel filtration, and mass spectrometry. It was found that a mixture of Lv-Hc, a gray protein, and Lv-BGBP (which is a natural astaxanthin-binding protein with a red color) is responsible for the brown color of fresh shrimp shells. Upon heating to 100 °C, the mixture of these proteins turned red, mimicking the color change observed in cooked shrimp shells. This transition is attributed to the extremely high thermal stability of Lv-BGBP, which has the ability to protect astaxanthin from thermal induced degradation. These findings provide significant insights into the molecular mechanism governing shrimp shell coloration, advancing our understanding of crustacean biochemistry.

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