文献类型：期刊文献

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

作者：Pan, Chuang[1];Ishizaki, Shoichiro[1];Nagashima, Yuji[1];Gao, Jialong[2];Watabe, Shugo[3]

机构：[1]Tokyo Univ Marine Sci & Technol, Grad Sch Marine Sci & Technol, Minato Ku, 4-5-7 Konan, Tokyo 1088477, Japan;[2]Guangdong Ocean Univ, Coll Food Sci & Technol, Haida Rd 1, Zhanjiang 524088, Guangdong, Peoples R China;[3]Kitasato Univ, Sch Marine Biosci, Sagamihara, Kanagawa 2520373, Japan

年份：2018

卷号：241

起止页码：104

外文期刊名：FOOD CHEMISTRY

收录：SCI-EXPANDED(收录号：WOS:000411624400013)、、WOS

基金：This work was partially supported by the Sasakawa Scientific Research Grant from The Japan Science Society (29-301).

语种：英文

外文关键词：Carapace; cDNA cloning; Hemocyanin; Litopenaeus vannamei; MALDI-TOF-MS; Pigment-binding protein

外文摘要：Pigment-binding proteins play important roles in crustacean shell colour change. In this study, a red colourrelated 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 75 kDa. Peptide mass fingerprint analysis revealed that LvPBP75 belonged to hemocyanin, and the released pigment from heated LvPBP75 showed lambda(max) at 481 nm in acetone. The significant red-colour change temperatures were detected at 30 and 80 degrees 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.