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. 2018 Feb 15:241:104-112.
doi: 10.1016/j.foodchem.2017.08.080. Epub 2017 Aug 24.

Isolation and cDNA cloning of a novel red colour-related pigment-binding protein derived from the shell of the shrimp, Litopenaeus vannamei

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Isolation and cDNA cloning of a novel red colour-related pigment-binding protein derived from the shell of the shrimp, Litopenaeus vannamei

Chuang Pan et al. Food Chem. .

Abstract

Pigment-binding proteins play important roles in crustacean shell colour change. In this study, a red colour-related pigment-binding protein, designated LvPBP75, was purified from the shell of Litopenaeus vannamei. HPLC and PAGE analysis showed that LvPBP75 was a homogeneous monomer with molecular mass of 75kDa. Peptide mass fingerprint analysis revealed that LvPBP75 belonged to hemocyanin, and the released pigment from heated LvPBP75 showed a λmax at 481nm in acetone. The significant red-colour change temperatures were detected at 30 and 80°C, respectively. Based on the determined amino acid fragments, a full-length cDNA of LvPBP75 was cloned and sequenced. The ORF encodes a protein of 662 amino acids having 80% identity with penaeidae hemocyanin. These results strongly suggest a novel function of hemocyanin, namely binding with pigment, and its involvement in L. vannamei shell colour change.

Keywords: Carapace; Hemocyanin; Litopenaeus vannamei; MALDI-TOF-MS; Pigment-binding protein; cDNA cloning.

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