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Cannonball jellyfish digestion: an insight into the lipolytic enzymes of the digestive system

Authors :
Raúl Balam Martínez-Pérez
Lourdes Mariana Díaz-Tenorio
Jorge A. Rodriguez
Pablo Gortáres-Moroyoqui
Luis Alonso Leyva Soto
Source :
PeerJ, Vol 8, p e9794 (2020), PeerJ
Publication Year :
2020
Publisher :
PeerJ, 2020.

Abstract

The digestive system and metabolism of the cannonball jellyfishStomolophussp. 2 are not well-known. The digestion study was critical to explain its ecology and bloom success. Different enzymes are involved in food digestion, which hydrolyze carbohydrates, proteins, and lipids. This study detected lipolytic activity in enzymatic extracts from gastric pouches ofStomolophussp. 2 collected in the summer of 2013 at Bahía de Kino, Sonora, México (28°47′47″N 111°57′25″W). Lipase/esterase activity showed optimal pH at 11.0 and 50–60 °C with a half-life (t1/2) of 33 min at 55 °C, whereas halotolerance of this activity was recorded from 0-4 M NaCl. Metal ions Ca2+and Mn2+did not affect the activity, but Mg2+decreased it 14.2% ± 3.15, while chelating agents as ethylenediaminetetraacetic acid reduced the activity 8.55% ± 2.13. Inhibition of lipase/esterase activity with tetrahydrolipstatin and paraoxon-ethyl decreased the activity 18.2% ± 2.3, and 62.80% ± 0.74, respectively, whereas phenylmethanesulfonyl fluoride (a protease inhibitor) did not affect it. The enzyme displayed a higher specificity for short-chain triglycerides, but triolein, coconut oil, olive oil, and fish oil were hydrolyzed. For the first time, phospholipase activity from the gastric pouch ofStomolophussp. 2 was detected using L-α-phosphatidylethanolamine from chicken egg yolk as a substrate. These results suggest thatStomolophussp. 2 hydrolyze several kinds of lipids, and lipolytic enzymes are active at alkaline pH under different saline conditions, which may be essential to digest different preys.

Details

ISSN :
21678359
Volume :
8
Database :
OpenAIRE
Journal :
PeerJ
Accession number :
edsair.doi.dedup.....118af83380a36b49a7d5b82d0f734917
Full Text :
https://doi.org/10.7717/peerj.9794