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

文献类型: 外文期刊

作者: Chen, Hao 1 ; Ji, Hongwu 1 ; Pan, Chuang 6 ; Zhang, Di 1 ; Su, Weiming 1 ; Liu, Shucheng 1 ; Deng, Yijia 1 ; Huang, Xiaodan 1 ;

作者机构: 1.Guangdong Ocean Univ, Coll Food Sci & Technol, Guangdong Prov Key Lab Aquat Prod Proc & Safety, Zhanjiang 524088, Peoples R China

2.Shaoyang Univ, Coll Food & Chem Engn, Hunan Prov Key Lab Soybean Prod Proc & Safety Con, Shaoyang 422000, Peoples R China

3.Guangdong Ocean Univ, Coll Food Sci & Technol, Guangdong Prov Engn Technol Res Ctr Seafood, Zhanjiang 524088, Peoples R China

4.Guangdong Ocean Univ, Coll Food Sci & Technol, Guangdong Prov Engn Lab Marine Biol Prod, Zhanjiang 524088, Peoples R China

5.Guangdong Ocean Univ, Coll Food Sci & Technol, Guangdong Higher Educ Inst, Key Lab Adv Proc Aquat Prod, Zhanjiang 524088, Peoples R China

6.Dalian Polytech Univ, Collaborat Innovat Ctr Seafood Deep Proc, Dalian 116034, Peoples R China

7.Chinese Acad Fishery Sci, South China Sea Fisheries Res Inst, Guangzhou 510300, Peoples R China

关键词: pigment protein; cDNA; red shift properties; red swamp crayfish

期刊名称:FOODS ( 影响因子:5.561; 五年影响因子:5.94 )

ISSN:

年卷期: 2022 年 11 卷 1 期

页码:

收录情况: SCI

摘要: 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 beta-barrel structure for pigment encapsulation. The colour change of F1 was first detected at 40 degrees C, and the red change occurred upon heating above 60 degrees C. Additionally, with increasing temperature, its beta-sheet content increased, and its alpha-helix content reduced. Correlation analysis showed that the redness value of F1 was significantly related to the heating temperature and the beta-sheet content.

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