Hostname: page-component-586b7cd67f-dsjbd Total loading time: 0 Render date: 2024-11-20T14:30:06.571Z Has data issue: false hasContentIssue false

Impact of exocrine pancreatic adaptation on in vitro protein digestibility

Published online by Cambridge University Press:  09 March 2007

P. Valette
Affiliation:
Département de Nutrition humaine et consommation, FSAA, Université Laval, Québec, GIK7P4, Canada
H. Malouin
Affiliation:
Département de Nutrition humaine et consommation, FSAA, Université Laval, Québec, GIK7P4, Canada
T. Corring
Affiliation:
Département de Nutrition humaine et consommation, FSAA, Université Laval, Québec, GIK7P4, Canada
L. Savoie
Affiliation:
Département de Nutrition humaine et consommation, FSAA, Université Laval, Québec, GIK7P4, Canada
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

An in vitro enzymic method was used to study the kinetics of digestion of casein and rapeseed proteins. After a predigestion step with pepsin (EC 3.4.23.1), the protein substrates were submitted to a 24 h hydrolysis either with pancreatin or pancreatic juices of pigs adapted either to casein or rapeseed diets and whose enzyme activities were different. After 3, 6 and 24 h of in vitro digestion, dialysates were collected and analysed for content of nitrogen, amino acids and low-molecular-weight peptides. For a long-term hydrolysis (24 h), overall digestibility of both substrates was not affected by the composition of pancreatic enzyme mixtures. However, at the beginning of hydrolysis a significant effect of pancreatic juices was observed, i.e. individual amino acid digestibility was generally higher when casein pancreatic juice was used for hydrolysis and their relative pattern of release was modified. For both substrates the proportion of amino acids released as low-molecular-weight peptides was not affected by the enzyme mixture used and made up about two-thirds of the total digested material. It is concluded that exocrine pancreatic adaptation to protein sources does not affect the total capacity of protein digestion. However, the changes in initial kinetics of release of amino acids are more dependent on the nature of the protein tested than on the composition of pancreatic enzyme mixtures.

Type
Hormonal Effects on Protein Digestibility
Copyright
Copyright © The Nutrition Society 1993

References

REFERENCES

Adibi, S. A. & Mercer, D. W. (1973). Protein digestion in human intestine as reflected in luminal, mucosal and plasma amino acid concentrations after meals. Journal of Clinical Investigation 52, 15861594.CrossRefGoogle ScholarPubMed
Adler-Nissen, J. (1986). Enzymatic Hydrolysis of Food Proteins. London: Elsevier, Applied Science Publishers.Google Scholar
Akeson, W. R. & Stahmann, M. A. (1964). A pepsin pancreatin digest index of protein quality evaluation. Journal of Nutrition 83, 257261.CrossRefGoogle ScholarPubMed
Camus, M. C. & Laporte, J. C. (1980). Protéolyse in vitro de la caséine et du gluten par les enzymes pancréatiques (In vitro proteolysis of casein and gluten by pancreatic enzymes). Reproduction, Nutrition, Développement 20, 10251039.CrossRefGoogle Scholar
Corring, T. (1980). The adaptation of digestive enzymes to the diet: its physiological significance. Reproduction, Nutrition, Développement 20, 12171235.CrossRefGoogle Scholar
Folk, J. E., Piez, K. A., Carroll, W. R. & Gladner, J. A. (1960). Carboxypeptidase B. VI. Purification and characterization of the porcine enzyme. Journal of Biological Chemistry 235, 22722277.CrossRefGoogle Scholar
Gertler, A., Abrahami, B. & Bondi, A. (1980). Specific contribution of porcine pancreatic proteinases to in vitro digestion of animal and plant proteins. Nutrition Reports International 22, 771779.Google Scholar
Gertler, A. & Hofmann, T. H. (1970). Acetyl-L-alanyl-L-alanyl-L-alanine methyl ester: a new highly specific elastase substrate. Canadian Journal of Biochemistry 48, 384386.CrossRefGoogle Scholar
Gray, G. M. & Cooper, H. L. (1971). Protein digestion and absorption. Gastroenterology 61, 535544.CrossRefGoogle ScholarPubMed
Hsu, H. W., Vavak, D. L., Satterlee, L. D. & Miller, G. A. (1977). A multienzyme technique for estimating protein digestibility. Journal of Food Science 42, 12691273.CrossRefGoogle Scholar
Kakade, M. S. (1974). Biochemical basis for the differences in plant protein utilization. Journal of Agricultural Food Chemistry 22, 550555.CrossRefGoogle ScholarPubMed
Maga, J. A., Lorentz, K. & Onayemi, O. (1973). Digestive acceptability of proteins as measured by the initial rate on in vitro proteolysis. Journal of Food Science 38, 173174.CrossRefGoogle Scholar
Nixon, S. E. & Mawer, G. E. (1970). The digestion and absorption of protein in man. 2. The form in which digested protein is absorbed. British Journal of Nutrition 24, 241258.CrossRefGoogle ScholarPubMed
Pelissier, J. P. (1984). Protéolyse des caséines (Proteolysis of casein). Sciences des Aliments 4, 135.Google Scholar
Reboud, J. P., Ben Abdeljlil, A. & Desnuelle, P. (1962). Variations de la teneur en enzymes du pancréas de rat en fonction de la composition des régimes (Variation of the enzymic content of rat pancreas as a function of the composition of the diet). Biochimica et Biophysica Acta 58, 326337.CrossRefGoogle Scholar
SAS Institute Inc. (1982). SAS User's Guide: Basics. Cary, North Carolina: SAS Institute Inc.Google Scholar
Savoie, L. & Charbonneau, R. (1990). Specific role of endopeptidases on modulating the nature of proteins digestion products. Plant Food for Hiiniun Nutrition 40, 233242.CrossRefGoogle ScholarPubMed
Savoie, L., Charbonneau, R. & Parent, G. (1989). In vitro amino acid digestibility of various protein sources. Plant Food for Human Nutrition 30, 93107.CrossRefGoogle Scholar
Savoie, L., Galibois, I., Parent, G. & Charbonneau, R. (1988). Sequential release of amino acids and peptides during in vitro digestion of casein and rapeseed proteins. Nutrition Research 8, 13191326.CrossRefGoogle Scholar
Savoie, L. & Gauthier, S. (1986). Dialysis cell for the in vitro measurement of protein digestibility. Journal of Food Science 51, 494498.CrossRefGoogle Scholar
Savoie, L. & Parent, G. (1987). Characterization of protein in vitro digestion products by copper-Sephadex chromatography. Nutrition Reports International 35, 783791.Google Scholar
Silano, V. (1977). Factors affecting digestibility and availability of proteins in cereals. In Nutritional Evaluation of Cereal Mutants, pp. 1346. Vienna: International Atomic Energy Agency.Google Scholar
Steel, R. C. D. & Torrie, J. H. (1980). Principles und Procedures of Statistics. 2nd ed. New York: McGraw-Hill.Google Scholar
Valette, P., Malouin, H., Corring, T., Savoie, L., Gueugneau, A. M. & Berot, S. (1992). Effects of diets containing casein and rapeseed on enzyme secretion from the exocrine pancreas in the pig. British Journal of Nutrition 67, 215222.CrossRefGoogle ScholarPubMed
Yamasaki, M., Brown, J. R., Cox, D. I., Greenshields, R. N., Wade, R. D. & Neurath, H. (1963). Procarboxypeptidase A-S6. Further studies of its isolation and properties. Biochemistry 2, 859866.CrossRefGoogle Scholar