First insights into the activity of major digestive enzymes in the intestine of the European catfish Silurus glanis and protective anti-enzymatic potential of its gut parasite Silurotaenia siluri.


Journal

Journal of fish biology
ISSN: 1095-8649
Titre abrégé: J Fish Biol
Pays: England
ID NLM: 0214055

Informations de publication

Date de publication:
Nov 2023
Historique:
revised: 16 06 2023
received: 21 04 2023
accepted: 02 07 2023
medline: 14 11 2023
pubmed: 4 7 2023
entrez: 4 7 2023
Statut: ppublish

Résumé

The European catfish Silurus glanis is attracting growing interest as an object of fisheries and aquaculture, which is reinforced by the expansion of its natural range under climate change. Shaping the effective exploitation strategy for this valuable species requires detailed knowledge of its biology, including feeding and digestion processes, especially near the natural limits of the species range. Meanwhile, the digestion physiology of the European catfish remains poorly explored, including the activity of major digestive enzymes and the possible effect of intestinal parasites on this activity. In this regard, the activity of proteinases and α-amylase in the intestinal mucosa of the catfish was studied. Adult catfish were collected in the Rybinsk reservoir (Upper Volga) located close to the northern limit of the species range. It was shown that all subclasses of intestinal digestive proteinases, including serine proteinases, metalloproteases and cysteine (thiol) proteinases, function in the gut mucosa of the catfish. The mucosal levels of total proteolytic activity depended on fish size, in contrast to those of trypsin, chymotrypsin and α-amylase. The level of chymotrypsin activity was significantly higher than that of trypsin activity. It was also found that the incubation medium and extract of the cestodes Silurotaenia siluri parasitizing the catfish gut had a significant inhibitory effect on the activity of serine proteases (trypsin and chymotrypsin) operating in the intestines of the host fish.

Identifiants

pubmed: 37401562
doi: 10.1111/jfb.15498
doi:

Substances chimiques

Trypsin EC 3.4.21.4
Chymotrypsin EC 3.4.21.1
Peptide Hydrolases EC 3.4.-
alpha-Amylases EC 3.2.1.1

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

985-993

Subventions

Organisme : the Russian Science Foundation
ID : 22-24-00248

Informations de copyright

© 2023 Fisheries Society of the British Isles.

Références

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Auteurs

Tatyana V Frolova (TV)

Laboratory of Ecological Parasitology, Papanin Institute for Biology of Inland Waters, Russian Academy of Sciences, Borok, Russia.

Evgeny I Izvekov (EI)

Laboratory of Ecological Parasitology, Papanin Institute for Biology of Inland Waters, Russian Academy of Sciences, Borok, Russia.

Galina I Izvekova (GI)

Laboratory of Ecological Parasitology, Papanin Institute for Biology of Inland Waters, Russian Academy of Sciences, Borok, Russia.

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