Purification, characterization and antibacterial activities of red color-related protein found in the shell of kuruma shrimp, Marsupenaeus japonicus. (25th April 2020)

• Record Type: Journal Article
• Authors: Pan, Chuang; Ishizaki, Shoichiro; Chen, Shengjun; Hao, Shuxian; Zhou, Jie; Yang, Xianqing
• Is Part Of: Food chemistry. Volume 310(2020)
• Publication Date: 2020-04-25
• Subjects: Antibacterial activity -- Color change -- Hemocyanin -- Marsupenaeus japonicas -- Shrimp shell; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2019.125819
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: A 75 kDa protein was isolated from kuruma shrimp shell. The protein was identified as a hemocyanin-astaxanthin binding protein. The protein was found to be responsible for the shell color. The protein also showed clear antibacterial activities in vitro . Abstract: The well-known red color change plays a significant role in consumer acceptability of crustacean species. In this study, we described the purification of the red color-related protein named MjRCP75 from the shell of Marsupenaeus japonicus . It was a homogeneous monomer with molecular mass of 75 kDa and rich in α-helix conformation. The α-helix content decreased within the increasing of heating temperature and was transformed dominantly to β types. Identification and structural analysis revealed that MjRCP75 belonged to hemocyanin family. The released pigment from heated MjRCP75 showed a λmax at 483 nm in acetone. MjRCP75 showed clearly antibacterial activity against Escherichia coli, Staphylococcus aureus, and Vibrio parahaemolyticus . These findings identify MjRCP75 as the red color-related protein in M. japonicus shell and reveal its involvement in antibacterial activities.