Examination of the effects of triacylglycerol lipase on astaxanthin conversion in the black tiger prawn Penaeus monodon

The enzyme triacylglycerol lipase (TGL) catalyses the hydrolysis of triacylglycerols, and is characterized by catalytic esterification and ester exchange functionality. However, at present, there is comparatively little information regarding the sequences and functional validation of TGLs in crustaceans. In this study, we cloned the TGL1 gene of the black tiger prawn Penaeus monodon. The full-length cDNA of PmTGL1 comprises 1807 base pairs (bp), including an 80-bp 5 '-untranslated region (UTR), a 149-bp 3 '-UTR, and a 1578-bp open-reading frame (ORF), and encodes a putative 525-amino acid protein of 58.71 kDa with a theoretical isoelectric point of 4.81. Homology and phylogenetic tree analyses revealed that PmTGL1 is most closely related to the TGL of Penaeus chinensis, with which it clusters in a single group (similarity of up to 97.52%). Quantitative real-time PCR analysis further revealed that PmTGL1 is most highly expressed in the shrimp hepatopancreas. Although the expression of PmTGL1 was not significantly influenced by the differences in the background colour of the rearing pond, it was significantly promoted in response to dietary supplementation with astaxanthin. As an adipokinetic hormone in P. monodon, PmRPCH (red pigment-concentrating hormone) plays an important role in body colour changes and lipid metabolism. Based on our findings, we speculate that the PmTGL1 facilitates astaxanthin metabolism in P. monodon via the hydrolysis of esterified astaxanthin to yield free astaxanthin and that the activity of TGL in these shrimps is regulated via an adipokinetic hormone cascade.