Both Hemocyanin and β-1,3-Glucan-Binding Protein from the Shrimp Shell of Litopenaeus vannamei Are Responsible for Its Color Change from Brown to Red during Thermal Processing

被引:1
作者
Guan, Leying [1 ]
Ji, Ruiyang [1 ]
Zang, Jiachen [1 ]
Zhang, Tuo [1 ]
Lv, Chenyan [1 ]
Zhao, Guanghua [1 ]
机构
[1] China Agr Univ, Coll Food Sci & Nutr Engn, Beijing 100083, Peoples R China
基金
国家重点研发计划; 中国国家自然科学基金;
关键词
beta-1,3-glucan-bindingprotein; color change; shrimp shell; hemocyanin; BINDING-PROTEIN; STRUCTURAL CHEMISTRY; MOLECULAR-CLONING; OXYGEN-BINDING; LOBSTER SHELL; PURIFICATION; CAROTENOIDS; CAROTENOPROTEINS; MECHANISM;
D O I
10.1021/acs.jafc.4c06238
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
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 beta-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 degrees 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.
引用
收藏
页码:23544 / 23553
页数:10
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