Background/Objectives: The Pacific white shrimp (L. vannamei) 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 L. vannamei are not fully understood. This study aimed to explore the molecular and functional properties of CPB in L. vannamei. Methods: The Lv-CPB gene was cloned, and bioinformatics analysis, qRT-PCR, in situ hybridization, recombinant protein expression in Escherichia coli, and an enzyme activity assay were performed. Results: 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. Conclusions: 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.
Keywords: Pacific white shrimp; enzymatic activity; functional analysis; molecular characterization.