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| Main Authors: | , , , , , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
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2025
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| Subjects: | |
| Online Access: | https://pubmed.ncbi.nlm.nih.gov/39858615/ |
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| _version_ | 1868266252608208896 |
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| author | Li, Hongmei Lin, Hai Yang, Hao Ren, Chunhua He, Yi Jiang, Xiao Chen, Ting Hu, Chaoqun |
| author_facet | Li, Hongmei Lin, Hai Yang, Hao Ren, Chunhua He, Yi Jiang, Xiao Chen, Ting Hu, Chaoqun Li, Hongmei Lin, Hai Yang, Hao Ren, Chunhua He, Yi Jiang, Xiao Chen, Ting Hu, Chaoqun |
| collection | PubMed - marine biology |
| contents | Molecular Characterization, Recombinant Expression, and Functional Analysis of Carboxypeptidase B in . Li, Hongmei Lin, Hai Yang, Hao Ren, Chunhua He, Yi Jiang, Xiao Chen, Ting Hu, Chaoqun Animals Penaeidae Recombinant Proteins Carboxypeptidase B Cloning, Molecular Arthropod Proteins Hepatopancreas Amino Acid Sequence Escherichia coli The Pacific white shrimp () is economically significant, and its growth is regulated by multiple factors. Carboxypeptidase B (CPB) is related to protein digestion, but its gene sequence and features in are not fully understood. This study aimed to explore the molecular and functional properties of CPB in . The Lv-CPB gene was cloned, and bioinformatics analysis, qRT-PCR, in situ hybridization, recombinant protein expression in , and an enzyme activity assay were performed. The Lv-CPB gene is 1414 bp long with a 1263 bp ORF encoding a 420-amino-acid protein. It is stable, hydrophilic, and is highly expressed in the hepatopancreas. The recombinant protein was efficiently expressed with a molecular weight of about 47 kDa. The optimal pH and temperature for Lv-CPB were 8.0 and 50 °C, respectively. This study revealed the molecular and functional characteristics of Lv-CPB, providing insights into its role in shrimp digestion, as well as suggestions for improving aquaculture practices. |
| format | Artículo científico |
| id | pubmed_39858615 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Genes |
| record_format | pubmed |
| spellingShingle | Molecular Characterization, Recombinant Expression, and Functional Analysis of Carboxypeptidase B in . Li, Hongmei Lin, Hai Yang, Hao Ren, Chunhua He, Yi Jiang, Xiao Chen, Ting Hu, Chaoqun Animals Penaeidae Recombinant Proteins Carboxypeptidase B Cloning, Molecular Arthropod Proteins Hepatopancreas Amino Acid Sequence Escherichia coli Molecular Characterization, Recombinant Expression, and Functional Analysis of Carboxypeptidase B in . Li, Hongmei Lin, Hai Yang, Hao Ren, Chunhua He, Yi Jiang, Xiao Chen, Ting Hu, Chaoqun Animals Penaeidae Recombinant Proteins Carboxypeptidase B Cloning, Molecular Arthropod Proteins Hepatopancreas Amino Acid Sequence Escherichia coli The Pacific white shrimp () is economically significant, and its growth is regulated by multiple factors. Carboxypeptidase B (CPB) is related to protein digestion, but its gene sequence and features in are not fully understood. This study aimed to explore the molecular and functional properties of CPB in . The Lv-CPB gene was cloned, and bioinformatics analysis, qRT-PCR, in situ hybridization, recombinant protein expression in , and an enzyme activity assay were performed. The Lv-CPB gene is 1414 bp long with a 1263 bp ORF encoding a 420-amino-acid protein. It is stable, hydrophilic, and is highly expressed in the hepatopancreas. The recombinant protein was efficiently expressed with a molecular weight of about 47 kDa. The optimal pH and temperature for Lv-CPB were 8.0 and 50 °C, respectively. This study revealed the molecular and functional characteristics of Lv-CPB, providing insights into its role in shrimp digestion, as well as suggestions for improving aquaculture practices. |
| title | Molecular Characterization, Recombinant Expression, and Functional Analysis of Carboxypeptidase B in . |
| topic | Animals Penaeidae Recombinant Proteins Carboxypeptidase B Cloning, Molecular Arthropod Proteins Hepatopancreas Amino Acid Sequence Escherichia coli |
| url | https://pubmed.ncbi.nlm.nih.gov/39858615/ |