Abstract
Sea bass (Dicentrarchus labrax) larvae were weaned at day 25 with microparticulated diets in which 10% of the nitrogen supply had different molecular forms: amino acid mixture (SLAA), casein hydrolysate (SLH) or fish meal (SLP). The control group (LP) was fed live prey. No difference was observed in larval growth between the weaned groups, but the survival was significantly higher in the SLH group. Trypsin secretion was stimulated in the SLAA group, whereas the SLH diet reduced the secretion from the exocrine pancreas. The activity of the leucine-alanine peptidase, located in the cytosol of enterocytes, remained high in all weaned groups. However, the activity of the peptidases of the brush border membrane increased during the development phase in the control group. These results suggest that weaning with a classic compound diet delays enterocyte differentiation by maintaining the larval features of digestion. A compound diet containing protein hydrolysate can attenuate the delay of intestinal maturation.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References cited
Alliot, E. 1979. Evolution de quelques activités digestives au cours du développement larvaire de téléostéens. In Nutrition des Poissons. pp. 79–87. Edited by M. Fontaine. Actes de Colloques CNERMA, Paris.
Baragi, V. and Lovell, R.T. 1986. Digestives enzyme activities in striped bass from first feeding through larva development. Trans. Am. Fish. Soc. 115: 478–484.
Bell, J.G., Buddington, R.K., Walton, M.J. and Cowey, C.B. 1987. Studies on the putative role of γ-glutamyl transpeptidase in intestinal transport of amino acids in Atlantic salmon. J. Comp. Physiol. 157: 161–169.
Boulhic, M. and Gabaudan, J. 1992. Histological study of the organogenesis of the digestive system and swim bladder of the Dover sole, Solea solea (Linneaus 1758). Aquaculture 102: 373–396.
Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248–254.
Buddington, R.K. and Diamon, J.M. 1989. Ontogenic development of intestinal nutrients transporters. Ann. Rev. Physiol. 51: 601–619.
Cahu, C.L. and Zambonino Infante, J.L. 1994. Early weaning of sea bass (Dicentrarchus labrax) larvae with a compound diet: effect on digestive enzymes. Comp. Biochem. Physiol. 109A: 213–222.
Chey, W.Y. 1993. Hormonal control of pancreatic exocrine secretion. In The Pancreas: Biology, Pathobiology and Disease. pp. 403–424. 2nd edition. Edited by V.L.W. Go, J.D. Gardner, F.P. Brooks, E. Lebenthal, E.P. DiMagno and G.A. Sheele. Raven Press, New York.
Crane, R.K., Boge, G. and Rigal, A. 1979. Isolation of brush border membranes in vesicular form from the intestinal spiral valve of the small dogfish (Scyliorhinus canicula). Biochim. Biophys. Acta 554: 264–267.
Ferraris, R.P., Kwan, W.W. and Diamond, J. 1988. Regulatory signals for intestinal amino acid transporters and peptidases. Am. J. Physiol. 255: G151–G157.
Gabaudan, J., Pigott, G.M. and Halver, J.E. 1980. The effect of processing on protein ingredients for larval diets: biological evaluation. Proc. World Maricul. Soc. 11: 424–432.
Garvey, T.Q., Hyman, P.E. and Isselbacher, K.J. 1976. γ-Glutamyl transpeptidase of rat intestine: localization and possible role in amino acid transport. Gastroenterology 71: 778–785.
Grendell, J.H. and Rothman, S.S. 1981. Digestive end products mobilize secretory proteins from subcellular stores in the pancres. Am. J. Physiol. 241: G67–G73.
Grimble, G.H., Rees, R.G., Kehoane, P.P., Cartwright, T., Desreumaux, M. and Silk, D.B.A. 1987. Effect of peptide chain length on absorption of egg protein hydrolysates in the normal human jejunum. Gastroenterology 92: 136–142.
Heintges, T., Lüthen, R. and Niederau, C. 1994. Inhibition of exocrine pancreatic secretion by somatostatin and its analogues. Digestion 55: 1–9.
Henning, S.J. 1987. Functional development of the gastrointestinal tract. In Physiology of the Gastrointestinal Tract. pp. 285–300. 2nd edition. Edited by L.R. Johnson. Raven Press, New York.
Himukai, M., Konno, T. and Hoshi, T. 1980. Age-dependent change in intestinal absorption of dipeptides and their constituent amino acids in the guinea pig. Pediatr. Res. 14: 1272–1275.
Lockwood, S.J. 1973. Weight and length of O-group plaice (Pleuronectes platessa L.) after preservation in 4% neutral formalin. J. Cons. Int. Explor. Mer. 35: 100–101.
Maroux, S., Louvard, D. and Baratti, J. 1973. The aminopeptidase from hog-intestinal brush border. Biochim. Biophys. Acta 321: 282–295.
Metais, P. and Bieth, J. 1968. Détermination de l'α-amylase par une microtechnique. Ann. Biol. Clin. 26: 133–142.
Nicholson, J.A., McCarthy, D.M. and Kim, Y.S. 1974. The responses of rat intestinal brush border and cytosol peptide hydrolases activities to variation in dietary protein content. Dietary regulation of intestinal peptide hydrolases. J. Clin. Invest. 54: 890–898.
Nicholson, J.A. and Kim, Y.S. 1975. A one-step L-amino acid oxidase assay for intestinal peptide hydrolase activity. Anal. Biochem. 63: 110–117.
Pedersen, B.H., Nilssen, E.M. and Hjelmeland, K. 1987. Variations in the content of trypsin and trypsinogen in larval herring (Clupea harengus) digesting copepod nauplii. Mar. Biol. 94: 171–181.
Person Le Ruyet, J. 1989. Early weaning of marine fish larvae onto microdiets: constraints and perspectives. In Advances in Tropical Aquaculture, IFREMER. Actes de Colloque 9. pp. 625–642. Edited by IFREMER.
Person Le Ruyet, J., Alexandre, J.C., Thébaud, L. and Mugnier, C. 1993. Marine fish larvae feeding: formulated diets or live preys? J. World Aquac. Soc. 24: 211–224.
Pigott, G.M., Heck, N.E., Stockard, R.D. and Halver, J.E. 1982. Engineering aspects of a new process for producing dry larval feed. Aquacult. Engin. 1: 215–226.
Rubino, A. 1975. Absorption of amino acids and peptides during development. Mod. Probl. Paediatr. 15: 201–212.
Stein, E.R., Chang, S.D. and Diamond, J.M. 1987. Comparison of different dietary amino acids as inducers of intestinal amino acid transport. Am. J. Physiol. 252: G626–G635.
Steinhardt, H.J., Paleos, G.A., Brandl, M., Fekl, W.L. and Adibi, S.A. 1984. Efficacy of a synthetic dipeptide mixture as the source of amino acids for total parenteral nutrition in a subhuman primate (Baboon). Gastroenterology 86: 1562–1569.
Szlaminska, M., Escaffre, A.M., Charlon, N. and Bergot, P. 1991. Preliminary data on semisynthetic diets for goldfish (Carassius auratus L.) larvae. In Fish Nutrition in Practice. Les Colloques 61. pp. 607–612. Edited by INRA.
Spyridakis, P., Gabaudan, J., Metailler, R. and Guillaume, J. 1988. Digestibilité des protéines et disponibilité des acides aminés de quelques matières premières chez le bar (Dicentrarchus labrax). Reprod. Nutr. Dévelop. 28: 1509–1517.
Tseng, H.C., Grendell, J.H. and Rothman, S.S. 1982. Food, duodenal extracts, and enzyme secretion by the pancreas. Am. J. Physiol. 243: G304–G312.
Zambonino Infante, J.L. and Cahu, C. 1994a. Development and response to a diet change of some digestive enzymes in sea bass (Dicentrarchus labrax) larvae. Fish Physiol. Biochem. 12: 399–408.
Zambonino Infante, J.L. and Cahu, C.L. 1994b. Influence of diet on pepsin and some pancreatic enzymes in sea bass (Dicentrarchus labrax) larvae. Comp. Biochem. Physiol. 109A: 209–212.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Cahu, C.L., Infante, J.L.Z. Effect of the molecular form of dietary nitrogen supply in sea bass larvae: Response of pancreatic enzymes and intestinal peptidases. Fish Physiol Biochem 14, 209–214 (1995). https://doi.org/10.1007/BF00004311
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00004311