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Article

Purification and Characterisation of Two Novel Pigment Proteins from the Carapace of Red Swamp Crayfish (Procambarus clarkii)

by 1,2, 1,3,4,5,6,*, 6,7, 1,3,4,5, 1,3,4,5, 1,3,4,5,6, 1 and 1
1
Guangdong Provincial Key Laboratory of Aquatic Product Processing and Safety, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, China
2
Hunan Provincial Key Laboratory of Soybean Products Processing and Safety Control, College of Food and Chemical Engineering, Shaoyang University, Shaoyang 422000, China
3
Guangdong Provincial Engineering Technology Research Center of Seafood, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, China
4
Guangdong Province Engineering Laboratory for Marine Biological Products, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, China
5
Key Laboratory of Advanced Processing of Aquatic Product of Guangdong Higher Education Institution, College of Food Science and Technology, Guangdong Ocean University, Zhanjiang 524088, China
6
Collaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian 116034, China
7
South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Guangzhou 510300, China
*
Author to whom correspondence should be addressed.
Academic Editors: Isidra Recio and Maria Antonietta Ciardiello
Foods 2022, 11(1), 35; https://doi.org/10.3390/foods11010035
Received: 23 November 2021 / Revised: 15 December 2021 / Accepted: 21 December 2021 / Published: 23 December 2021
(This article belongs to the Section Foods of Marine Origin)
Pigment proteins play a vital role in the red colour change of the red swamp crayfish (Procambarus clarkii) shell after cooking. In this study, two red-change-related pigment proteins with molecular weights of approximately 170 and 43 kDa—denoted as F1 and F2, respectively—were purified by ammonium sulphate salting-out and size exclusion chromatography. F1 and F2 entirely comprised homomultimeric protein complexes composed of 21 kDa subunits. LC-MS/MS analysis showed that the 21 kDa protein subunit belonged to the crustacyanin family, named P. clarkii crustacyanin A2 (PcCRA2). The full-length cDNA of PcCRA2 was cloned, which encoded 190 amino acid residues and was highly homologous (91.58%) with Cherax quadricarinatus crustacyanin A. The predicted 3D structure showed that PcCRA2 had a β-barrel structure for pigment encapsulation. The colour change of F1 was first detected at 40 °C, and the red change occurred upon heating above 60 °C. Additionally, with increasing temperature, its β-sheet content increased, and its α-helix content reduced. Correlation analysis showed that the redness value of F1 was significantly related to the heating temperature and the β-sheet content. View Full-Text
Keywords: pigment protein; cDNA; red shift properties; red swamp crayfish pigment protein; cDNA; red shift properties; red swamp crayfish
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MDPI and ACS Style

Chen, H.; Ji, H.; Pan, C.; Zhang, D.; Su, W.; Liu, S.; Deng, Y.; Huang, X. Purification and Characterisation of Two Novel Pigment Proteins from the Carapace of Red Swamp Crayfish (Procambarus clarkii). Foods 2022, 11, 35. https://doi.org/10.3390/foods11010035

AMA Style

Chen H, Ji H, Pan C, Zhang D, Su W, Liu S, Deng Y, Huang X. Purification and Characterisation of Two Novel Pigment Proteins from the Carapace of Red Swamp Crayfish (Procambarus clarkii). Foods. 2022; 11(1):35. https://doi.org/10.3390/foods11010035

Chicago/Turabian Style

Chen, Hao, Hongwu Ji, Chuang Pan, Di Zhang, Weiming Su, Shucheng Liu, Yijia Deng, and Xiaodan Huang. 2022. "Purification and Characterisation of Two Novel Pigment Proteins from the Carapace of Red Swamp Crayfish (Procambarus clarkii)" Foods 11, no. 1: 35. https://doi.org/10.3390/foods11010035

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