DIGESTIVE AND METABOLIC RESPONSES TOWARDS DIET OPTIMIZATION IN LABEO ROHITA
143 / 2
Abstract
Digestive and metabolic responses of Labeo rohita (av. wt. 1.07–1.14 g) to different dietary crude protein (CP) levels ( 25, 30, 35, 40 and 45%) were studied to optimize a practical diet formulation for this species. Soybean meal and fish meal were served as the main protein sources, whereas corn flour and rice polish as major carbohydrate sources. After 45 days of feeding, trypsin and chymotrypsin activities were lower in 25% CP group. Alkaline phosphatase and trypsin activities were maximized (p<0.05) in 35% CP group. Amylase activity was not influenced by the diet composition. Hexokinase (HK) activity in the muscle of fish fed 25 to 35% CP was significantly higher (p<0.05) than the other two groups. Liver also recorded a higher HK activity in low protein fed groups. Similarly, muscle and liver pyruvate kinase activities were significantly higher in 25 and 30% CP fed groups. Malate dehydrogenase activity in muscle was highest at 30% CP group. Muscle aspartate amino-transferase activity was found to be higher in low protein fed groups ( 25 and 30%). Metabolites showed significant change corresponding to the dietary composition. Glucose and glycogen levels matched well with the dietary carbohydrate levels. Muscle and plasma pyruvic acid contents increased as the dietary protein increased, whereas liver pyruvic acid showed opposite trend. Protein fractions in plasma (total protein, albumin and globulin) showed maximum values in 30% CP group.
Key words: Crude protein, digestive enzymes, metabolic enzymes, metabolites, Labeo rohita
References
Baglole, C. J., Goff, G. P. and Wright, G. M., 1998. Distribution and ontogeny of digestive enzymes in larval yellowtail and winter flounder. J. Fish Biol., 53: 767-784.
Bergmeyer, H. U., 1974. Methods of enzymatic analysis. Verlag Chimie, vol. 4, 1704-1708 pp.
Blier, P. U., Lemieux, H. and Devlin, R. H., 2002. Is the growth rate of fish set by digestive enzymes or metabolic capacity of the tissues? Insight from transgenic coho salmon. Aquaculture, 209 : 379-384.
Blier, P. U., Pelletier, D. and Dutil, J. D. 1997. Does aerobic capacity set a limit on fish growth rate? Rev. Fish. Sci., 5 : 323-340.
Borrebaek, B. and Christophersen, B., 2000. Hepatic glucose phosphorylating activities in perch (Perca fluviatilis) after different dietary treatments. Comp. Biochem. Physiol., 125 B : 387-393.
Caseras, A., Meton, I., Fernandez, F. and Baanante, I. V. 2000. Glucokinase gene expression is nutritionally regulated in the liver of gilthead seabream (Sparus aurata). Biochim. Biophys. Acta, 1493 : 135-141.
Chakrabarti, I., Gani, M. D. A., Chaki, K. K., Sur, R. and Misra, K. K., 1995. Digestive enzymes in 11 freshwater teleost fish species in relation to food habit and niche segregation. Comp. Biochem. Physiol., 112 A : 167-177.
Chakravorty, P. and Sinha G. M., 1982. Detection and localization of alkaline and acid phosphatases in the digestive system of the adult Catla catla (Ham.), an Indian freshwater major carp by histochemical methods. Gegenbaurs. Morph. Jahrb., 128 : 799-808.
Cherry, I. S. and Crandell, L. A. Jr. 1932. The specificity
of pancreatic lipase: its appearance in blood after
pancreatic injury. Am. J. Physiol., 100 : 266- 273.
Dalal, S., Bhattacharya, S. and Ray, A. K., 2001. Effects
of dietary protein and carbohydrate levels on growth
performance, feed utilization efficiency and nitrogen
metabolism in rohu, Labeo rohita (Hamilton), fingerlings.
Acta Ichthyol. Piscat., 31: 3-17.
De Moss, R. D., 1955. Glucose-6-phosphate and
-phosphogluconic dehydrogenase from Leuconostoc
mesenteroides. Methods in Enzymology Colowick, S.P.
and Kalpan, N.O., (ed.) Vol. I, Academic Press Inc., New
York, p. 328-32.
Debnath, D., Pal, A. K., Sahu, N. P., Yengkokpam, S., Baruah, K., Choudhury, D. and Venkateshwarlu, G., 2007. Digestive enzymes and metabolic profile of Labeo rohita fingerlings fed diets with different crude protein levels. Comp. Biochem. Physiol., 146 B : 107-114.
Easterby, J. S. and O’Brien, M. J., 1973. Enzymatic assay of Hexokinase. Eur. J. Biochem., 38 : 201-211.
Ellman, G. L., 1959. Tissue sulfhydryl groups. Arch. Biochem. Biophys., 82 : 70-77.
Fiske, C. H. and Subbarow, Y., 1925. The colorimetric determination of phosphorus. J. Biol. Chem., 66 : 375-400.
Friedemann, T. E., and Haugen, G. E., 1943. Pyruvic acid 2. The determination of keto acids in blood and urine. J. Biol. Chem., 47 : 415-442.
Garen, A. and Levinthal, C. A., 1960. Fine structure, genetic and chemical study of enzyme alkaline phosphatase of E. coli. Purification and characterisation of alkaline phosphatase. Biochem. Biophys. Acta, 38 : 470.
Gisbert, E., Sarasquete, M. C., Willot, P. and Castello-Orvay, F., 1999. Histochemistry of the development of the digestive system of Siberian
sturgeon during early ontogeny. J. Fish. Biol., 55 : 596-616.
Hassid, W. J., Abraham, S., 1957. Chemical procedures for analysis of polysaccharide. In: Methods in Enzymology ( Colowich, S.P. and Kalplan, N.O.ed.), Vol. 3. Academic Press. Inc., New York, pp. 35-36.
Kheyyali, D., Shimeno, S. and Takeda, M., 1989. Effect of dietary carbohydrate and lipid levels on hepatopancreatic enzymes and body composition in carp. In: The Current Status of Fish Nutrition in
Aquaculture (Takeda, M. and Watanabe, T.ed. ), Tokyo University of Fisheries, Tokyo, pp. 451-460.
Klein, S., Cohn, S. M. and Alpers, D. H., 1998. The alimentary tract in nutrition. In: Modern Nutrition in Health and Disease ( Shils, M.E., Olson, A.J., Shike, M. and Ross, A.C.ed.), pp. 605-630.
Krogdahl, A., McKellep, A. M. B. and Baeverfjord, G., 2003. Effects of graded levels of standard soybean meal on intestinal structure, mucosal enzyme activities, and pancreatic response in Atlantic salmon (Salmo salar L.). Aqua. Nutr., 9 : 361-371.
Kunitz, M., 1947. Crystalline soybean trypsin inhibitor: II. General properties. J. Gen. Physiol., 30 : 291-310.
Lemieux, H., Blier, P. and Dutil, J. D., 1999. Do digestive enzymes set a physiological limit on growth rate and food conversion efficiency in the Atlantic cod (Gadus morhua)? Fish Physiol. Biochem., 20 : 293-303.
Lopez-lopez, S., Nolasco, H., Villarreal-Colmenares, H. and Civera-Cerecedo, R., 2005. Digestive enzyme response to supplemental ingredients in practical diets for juvenile freshwater crayfish Cherax
quadricarinatus. Aqua. Nutr., 11 : 79-85.
Lowry, O. H., Rosebrough, N. J., Farr, A. L. and Randall, R. J. 1951. Protein measurement with Folin Phenol Reagent. J. Biol. Chem., 193 : 265-276.
Lundstedt, L. M., Bibiano Melo, J. F. and Moraes, G., 2004. Digestive enzymes and metabolic profile of Pseudoplatystoma corruscans (Teleostei: Siluriformes) in response to diet composition. Comp. Biochem. Physiol., 137 B : 331-339.
Lupianez, J. A., Sanchez-Lozano, M. J., Garcia-Rejón, L., and De La Higuera, M., 1989. Long-term effect of a high-protein/non-carbohydrate diet on the primary liver and kidney metabolism in rainbow trout (Salmo gairdneri). Aquaculture, 79 : 91-101.
Lyndon, A. R. and Houlihan, D. F., 1998. Gill protein turnover: costs of adaptation. Comp. Biochem. Physiol., 119 A : 27-34.
Marjoric, A. S., 1964. Methods in Enzymology. (Colowick, S. P. and Kaplan, N.O. (ed), Vol. II, Academic Press Inc., New York, p. 541.
Meton, I., Caseras, A., Mediavilla, D., Fernandez, F. and Baanante, I. V., 1999. Molecular cloning of a cDNA encoding 6-phosphofructo-2-kinase/fructose-2,6- bisphosphatase from liver of Sparus aurata: nutritional regulation of enzyme expression. Biochem. Biophys.
Acta, 1444 : 153-165.
Moon, T. W. and Foster, G. D., 1995. Tissue carbohydrate metabolism, gluconeogenesis and hormonal and environmental influences. In: Hochachka, P. W. and Mommsen, T. P. Metabolic Biochemistry (ed.), Elsevier, Amsterdam. pp. 65-100.
Moore, S. Stein, W. H. 1948. Photometric ninhydrin method for use in the chromography of amino acids, J. Biot. Chem. 176 : 367-388.
Nelson, J. W. and Somogyi, M. 1945. Hawk’s Physiological Chemistry (ed. Oser, B.L.), 14th Ed., McGraw Hill Publication, New York, USA, pp. 113.
NRC (National Research Council), 1993. Nutrient requirements of fish. National Academy Press, Washington, DC. pp. 114.
Ochoa, S., 1955. Malic enzyme. Methods in Enzymology (Colowick, S. P. and Kaplan, N. O. ed.), vol. 1, Academic Press, New York, pp. 739- 753.
Panserat, S., Plagnes-Juan, E. and Kaushik, S., 2001. Nutritional regulation and tissue specificity of gene expression for proteins involved in hepatic glucose metabolism in rainbow trout (Oncorhynchus mykiss). J. Expt. Biol., 204 : 2351-2360.
Pelletier, D., Blier, P. U., Dutil, J. D. and Guderley, H., 1995. How should enzyme activities be used in fish growth studies? J. Expt. Biol., 198 : 1493-1497.
Pelletier, D., Guderley, H. and Dutil, J. D., 1993. Effects of growth rate, temperature, season and body size on glycolytic enzyme activities in the white muscle of Atlantic cod (Gadus morhua). J. Expt. Zool., 5 : 466-477.
Post, R. L. and Sen, A. K., 1967. Methods in Enzymology (Colowick, S. P. and Kaplan, N.O.ed. ), Vol. 10, Academic Press Inc., New York, pp. 762.
Ribeiro, L., Zambonino Infante, J. L., Cahu, C. and Dinis, M.T., 1999. Development of digestive enzymes in larvae of Solea senegalensis, Kaup 1858. Aquaculture, 179 : 465-473.
Rick, W. and Stegbauer, H. P., 1974. Amylase measurement of reducing groups. In: Methods of Enzymatic Analysis. Bergmeyer, H.V. (ed.), 2nd edition, Vol. 2., Academic Press, New York, pp. 885- 889.
Sinha, G. M., 1979. Histochemical localization of alkaline and acid phosphatases in the alimentary tract of hatchling of a teleost fish, Cirrhinus mrigala (Ham.). Mikroskopie, 35 : 101-107.
Spannhof, L. and Plantikow, H., 1983. Studies on carbohydrate digestion in rainbow trout. Aquaculture, 30 : 95-108.
Suarez, M. D., Hidalgo, M. C., Garcia Galego, M., Sanz, A. and De La Higuera, M. 1995. Influence of the relative proportions of the energy yielding nutrients on the liver intermediary metabolism of the European eel. Comp. Biochem. Physiol., 111A : 421-428.
Suarez, M. D., Sanz, A., Bazoco, J. and Garcia-Gallego, M., 2002. Metabolic effects of changes in the dietary protein: carbohydrate ratio in eel (Anguilla anguilla) and trout (Oncorhynchus mykiss). Aqua. Int.,
: 143-156.
Sundby, A., Hemre, G. I., Borrebaek, B., Christophersen, B. and Blom, A. K., 1991. Insulin and glucagon family peptides in relation to activities of hepatic hexokinase and other enzymes in fed and starved Atlantic salmon (Salmo salar) and cod (Gadus morhua). Comp.
Biochem. Physiol., 100 B : 467-470.
Twining, S. S., Alexander, P. A., Huibregste, K. and Glick, D. M., 1983. A pepsinogen from rainbow trout. Comp. Biochem. Physiol., 75 B : 109-112.
Vieira, V. P., Inoue, L. A. K. and Moraes, G., 2005. Metabolic responses of matrinxa (Brycon cephalus) to dietary protein level. Comp. Biochem. Physiol., 140 A : 337-342.
Walford, J. and Lam, T. J., 1993. Development of digestive tract and proteolytic enzyme activity in seabass (Lates calcarifer) larvae and juveniles. Aquaculture, 109 : 187-205.
Walton, M. J. and Cowey, C. B. 1977. Aspects of ammoniogenesis in rainbow trout, Salnlo gairdneri. Comp. Biochem. Phvsiol., 57 B : 143-149.
Walton, M. J. and Cowey, C. B., 1982. Aspects of intermediary metabolism in salmonid fish. Comp. Biohem. Physiol., 73 B : 59-79.
Wooten, I. D. P., 1964. Microanalysis. Medical Biochemistry. 4th edn. J. & A. Churchill, London, pp. 101-107.
Wroblewski and Ladue, 1955. LDH activity in blood. Proc. Soc. Exp. Biol. Med., 90 : 210-213.
Downloads
Submitted
Published
Issue
Section
License
In case of publication of the article in the journal, author(s) are required to assign copyright to the Journal of the Inland Fisheries Society of India for its publication in any form/language including all media (print and electronic, or presently unknown), and exclusive right to use the matter for the life of the work (no time restriction on re use of matter).