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

Autor: Martínez-Pérez RB; Departamento de Biotecnología y Ciencias Alimentarias, Instituto Tecnológico de Sonora, Ciudad Obregón, Sonora, Mexico.; Biotecnología Industrial, Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C., Zapopan, Jalisco, Mexico., Rodríguez JA; Biotecnología Industrial, Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C., Zapopan, Jalisco, Mexico., Leyva Soto LA; Departamento de Biotecnología y Ciencias Alimentarias, Instituto Tecnológico de Sonora, Ciudad Obregón, Sonora, Mexico.; Dirección de Cátedras, Consejo Nacional de Ciencia y Tecnología, Ciudad de México, Mexico., Gortáres-Moroyoqui P; Departamento de Biotecnología y Ciencias Alimentarias, Instituto Tecnológico de Sonora, Ciudad Obregón, Sonora, Mexico., Diaz-Tenorio LM; Departamento de Biotecnología y Ciencias Alimentarias, Instituto Tecnológico de Sonora, Ciudad Obregón, Sonora, Mexico.
Jazyk: angličtina
Zdroj: PeerJ [PeerJ] 2020 Sep 08; Vol. 8, pp. e9794. Date of Electronic Publication: 2020 Sep 08 (Print Publication: 2020).
DOI: 10.7717/peerj.9794
Abstrakt: The digestive system and metabolism of the cannonball jellyfish Stomolophus sp. 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 of Stomolophus sp. 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 (t 1/2 ) of 33 min at 55 °C, whereas halotolerance of this activity was recorded from 0-4 M NaCl. Metal ions Ca 2+ and Mn 2+ did not affect the activity, but Mg 2+ 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 of Stomolophus sp. 2 was detected using L-α-phosphatidylethanolamine from chicken egg yolk as a substrate. These results suggest that Stomolophus sp. 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.
Competing Interests: The authors declare there are no competing interests.
(©2020 Martínez-Pérez et al.)
Databáze: MEDLINE
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