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Distribution of activity of hydrolytic enzymes in the digestive tract of rabbits

Published online by Cambridge University Press:  09 March 2007

M. Marounek ,
S. J. Vovk  and
V. Skřivanová
M. Marounek
Affiliation:
Institute of Animal Physiology and Genetics, Czech Academy of Sciences, 104 00, Prague 10 - Uhřiněves, Czech Republic
S. J. Vovk
Affiliation:
Institute of Animal Physiology and Genetics, Czech Academy of Sciences, 104 00, Prague 10 - Uhřiněves, Czech Republic
V. Skřivanová
Affiliation:
Research Institute of Animal Production, 104 00, Prague 10- Uhřiněves, Czech Republic
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Abstract

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Activities of twelve hydrolytic enzymes in the digestive tract of young rabbits before weaning (4 weeks old) and adult rabbits (3 months old) were measured. The principal digestive enzymes in both groups of rabbits appeared to be amylase (EC 3.2.1.1), maltase (EC 3.2.1.20), pectinase (EC 3.2.1.15) and proteinases. The stomach of young rabbits contained most of the lipolytic activity and 45.7 % of the total proteolytic activity of the digestive tract. The highest specific activities (per g digesta) of amylase, maltase and proteinase in young rabbits were found in the small intestine. Total activities (per segment) of amylase and maltase in the small intestine and the caecum were similar. Activities of cellulase (EC 3.2.1.4), inulinase (EC 3.2.1.7) and β-glucosidase (EC 3.2.1.21) were low and activity of pectinase was fairly high in all segments of the digestive tract. The highest activity of urease (EC 3.5.1.5) was found in the caecum. Enzymic profiles of the colonic chymus resembled those of the caecum. Total hydrolytic activity was lower in the colon than in the caecum. Specific activities of amylase and invertase (EC 3.2.1.26) were lower and those of inulinase and lactase (EC 3.2.1.23) higher in 4-week-old rabbits than in 3-month-old rabbits. Gastric proteinase represented almost half of the total proteolytic activity of the digestive tract, whereas lipolytic activity of gastric contents was not found in measurable quantities in adult rabbits. The caecal contents of adult rabbits contained most of the total activity of lipase (EC 3.1.1.3), cellulase, xylanase (EC 3.2.1.32), pectinase, lactase, invertase, β-glucosidase and urease present in the digestive tract. The presence of microbial enzymes (pectinase, cellulase, xylanase, inulinase and urease) in non-fermentative segments of the digestive tract reflects the reingestion of caecal contents during coprophagy.

Keywords

Hydrolytic enyzmesDigestive tractRabbit
Type
Enzyme distribution in the rabbit digestive tract
Information
British Journal of Nutrition , Volume 73 , Issue 3 , March 1995 , pp. 463 - 469
Copyright
Copyright © The Nutrition Society 1995

References

Altman, P. L. & Dittmer, D. S. (1961). Blood and Other Body Fluids. Washington, DC: Federation of American Societies for Experimental Biology.Google Scholar
Alus, G. & Edwards, N. A. (1977). Development of the digestive tract of the rabbit from birth to weaning. Proceedings of the Nutrition Society 36, 3A.Google ScholarPubMed
Bier, M. (1955). Lipases. In Methods in Enzymology, Vol. 1, pp. 627–642 [Colowick, S. P. and Kaplan, N. O., editors]. New York: Academic Press.CrossRefGoogle Scholar
Borel, P., Armand, M., Senft, M., Andre, M., Lafont, H. & Lairon, D. (1991). Gastric lipase - evidence of an adaptive response to dietary fat in the rabbit. Gastroenterology 100, 1582–1589.CrossRefGoogle ScholarPubMed
Forsythe, S. J. & Parker, D. S. (1985). Nitrogen metabolism by the microbial flora of the rabbit caecum. Journal of Applied Bacteriology 58, 363–369.CrossRefGoogle ScholarPubMed
Gidenne, T. (1992). Effect of fibre level, particle size and adaptation period on digestibility and rate of passage as measured at the ileum and in the faeces in the adult rabbit. British Journal of Nutrition 67, 133–146.CrossRefGoogle ScholarPubMed
Gidenne, T., Carre, B., Segura, M., Lapanouse, A. & Gomez, J. (1991 a). Fibre digestion and rate of passage in the rabbit: effect of particle size and level of lucerne meal. Animal Feed Science and Technology 32, 215–221.CrossRefGoogle Scholar
Gidenne, T. & Perez, J. M. (1993). Effect of dietary starch origin on digestion in the rabbit. 1. Digestibility measurements from weaning to slaughter. Animal Feed Science and Technology 42, 237–247.CrossRefGoogle Scholar
Gidenne, T., Scalabrini, F. & Marchais, C. (1991 b). Adaptation digestive du lapin a la teneur en constituants parietaux du regime (Digestive adaptation of the rabbit to the level of dietary fibre). Annates de Zootechnie 40, 73–84.CrossRefGoogle Scholar
Griffiths, M. & Davies, D. (1963). The role of soft pellets in the production of lactic acid in the rabbit stomach. Journal of Nutrition 80, 171–180.CrossRefGoogle ScholarPubMed
Jung, H. G. & Vogel, K. P. (1986). Influence of lignin on digestibility of forage cell wall material. Journal of Animal Science 62, 1703–1712.CrossRefGoogle ScholarPubMed
Kopecny, J. & Bartos, S. (1990). Activity of hydrolases in the gastrointestinal tract of goats. Small Ruminant Research 3, 25–35.CrossRefGoogle Scholar
Levy, E., Rouleau, T., Lepage, G., Smith, L., Junien, J. L. & Roy, C. C. (1991). Partially purified rabbit gastric lipase - in vitro and in vivo experiments to assess its potential contribution to gastric and intestinal lipolysis. Nutrition Research 11, 607–619.CrossRefGoogle Scholar
Makkar, H. P. S. & Singh, B. (1987). Comparative enzymatic profiles of rabbit cecum and bovine rumen contents. Journal of Applied Rabbit Research 10, 172–174.Google Scholar
Moreau, H., Gargouri, Y., Lecat, D., Junien, J. L. & Verger, R. (1988). Screening of preduodenal lipases in several mammals. Biochimica et Biophysica Acta 959, 247–252.CrossRefGoogle ScholarPubMed
Sakaguchi, E., Itoh, H., Uchida, S. & Horigome, T. (1987). Comparison of fibre digestion and digesta retention time between rabbits, guinea-pigs, rats and hamsters. British Journal of Nutrition 58, 149–158.CrossRefGoogle Scholar
Sakaguchi, E., Kaizu, K. & Nakamichi, M. (1992). Fibre digestion and digesta retention from different physical forms of the feed in the rabbit. Comparative Biochemistry and Physiology 102A, 559–563.CrossRefGoogle Scholar
Slade, L. M. & Hintz, H. F. (1969). Comparison of digestion in horses, ponies, rabbits and guinea pigs. Journal of Animal Science 28, 842–843.CrossRefGoogle ScholarPubMed
Somogyi, M. (1952). Notes on sugar determination. Journal of Biological Chemistry 195, 19–23.CrossRefGoogle Scholar
Stephens, A. G. (1977). Digestibility and coprophagy in the growing rabbit. Proceedings of the Nutrition Society 36, 4A.Google ScholarPubMed
Williams, A. G. & Withers, S. E. (1981). Hemicellulose-degrading enzymes synthesized by rumen bacteria. Journal of Applied Bacteriology 51, 375–385.CrossRefGoogle Scholar
Yu, B. & Tsen, H. Y. (1993). An in vitro assessment of several enzymes for the supplementation of rabbit diets. Animal Feed Science and Technology 40, 309–320.CrossRefGoogle Scholar