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Metabolic effects on growth and muscle of soya-bean protein feeding in cod (Gadus morhua)

Published online by Cambridge University Press:  09 March 2007

A. Von Der Decken  and
E. Lied
A. Von Der Decken
Affiliation:
The Wenner-Gren Institute for Experimenta1 Biology, University of Stockholm, S-106 91 Stockholm, Sweden
E. Lied
Affiliation:
Nutrition Institute, Directorate of Fisheries, N-5024 Bergen, Norway
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Abstract

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The aim of the present study was to investigate the effect of soya-bean protein on growth and muscle metabolism in fish. Cod, Gadus morhua, were fed on a fish-feed formula with the high-quality fish-meal protein being replaced by 100, 200 or 300 g soya-bean protein/kg fish-meal protein. The feeding experiment lasted for 43 d at a water temperature of 7–8º and a sea water salinity of 3.5%. At the 200 g/kg level of soya-bean protein, food intake and growth rate were similar to those of the controls. At the 300 g/kg level of soya-bean protein, food intake was diminished by 6 % and growth by 67 % relative to control levels. In muscle, sarcoplasmic protein (/g wet weight) was significantly decreased by 14%. Myofibrillar protein (/g wet weight) was unchanged. Levels of RNA in the myofibrillar fraction decreased at all three levels of soya-bean protein, and that of the sarcoplasmic fraction decreased at the highest level of legume-protein. With increased levels of soya-bean protein, RNA: DNA declined by 18% from 1.88 to 1.54. The contractile protein myosin heavy chain (/mg protein and /g wet weight) and myosin heavy chain-specific mRNA (/mg RNA) were not significantly affected by dietary conditions. Expressed per g wet weight, the decline by 21 % of the specific mRNA depended on the total RNA content which decreased with the increase in soya-bean protein. Acid proteinase activity was lowest at the 200 g/kg level, showing a decrease of 23%. Glycogen content fell by 46% at both the 200 and 300 g/kg level of dietary soya-bean protein. The results show that muscle metabolic functions responded to the dietary plant protein before there were any measurable changes in growth rate. From the results it is concluded that 200 g/kg or less of the high-quality fish-meal protein may be replaced by soya-bean protein in a fish-feed formula.

Keywords

Soya-bean proteinMuscle metabolismFish
Type
Protein Intake and Growth in Fish
Information
British Journal of Nutrition , Volume 69 , Issue 3 , May 1993 , pp. 689 - 697
Copyright
Copyright © The Nutrition Society 1993

References

Ambrose, J. A. (1974). Fluorometric measurement of tyrosine in serum and plasma. Clinical Chemistry 20, 505–510.CrossRefGoogle ScholarPubMed
Ando, S., Hatano, M. & Zama, K. (1986). Protein degradation and protease activity of chum salmon (Oncorhynchus keta) muscle during spawning migration. Fish Physiology and Biochemistry 1, 17–26.CrossRefGoogle ScholarPubMed
Batterham, E. S., Andersen, L. M., Baigent, D. R., Darnell, R. E. & Taverner, M. R. (1990). A comparison of the availability and ileal digestibility of lysine in cottonseed and soya-bean meals for grower/finisher pigs. British Journal of Nutrition 64, 663–667.Google Scholar
Block, R. J. & Bolling, D. (1947). The Amino Acid Composition Proteins and Foods, pp. 303–305. Springfield, IL: Charles Thomas.Google Scholar
Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72, 248–254.CrossRefGoogle ScholarPubMed
Circle, S. J. & Smith, A. K. (1972). Soybeans: Chemistry and Technology, pp. 264–338. Westport, CT: Avi Publishing.Google Scholar
Cowey, C. B. & Walton, M. J. (1989). Intermediary metabolism. In Fish Nutrition, 2nd ed., pp. 259–329 [Halver, J. E., editor]. New York and London: Academic Press.Google Scholar
Crooke, W. M. & Simpson, W. E. (1971). Determination of ammonium in Kjeldahl digest of crops by an automated procedure. Journal of the Science of Food and Agriculture 22, 9–10.Google Scholar
Fleck, A. & Munro, H. N. (1962). The precision of ultraviolet absorption measurements in the Schmidt-Thannhauser procedure for nucleic acid estimation. Biochimica et Biophysica Acta 55, 571–583.Google Scholar
Harris, R. C., Hultman, C. & Nordesjo, L.-O. (1974). Glycogen, glycolytic intermediates and high-energy phosphates determined by biopsy samples of musculus Quadriceps femoris of men at rest. Methods and variance of values. Scandinavian Journal of Clinical and Lnboratory Investigation 33, 109–120.CrossRefGoogle Scholar
Ketola, H. G. (1982). Amino acid nutrition of fishes: requirements and supplementation of diets. Comparative Biochemistry and Physiology 73B, 17–24.Google Scholar
Lied, E. & Rosenlund, G. (1984). The influence of the ratio of protein energy to total energy in the feed on the activity of protein synthesis in vitro, the level of ribosomal RNA and the RNA–DNA ratio in white trunk muscle of Atlantic cod (Gadus morhua). Comparative Biochemistry and Physiology 77A, 489–494.Google Scholar
Lied, E. & von der Decken, A. (1985). Purification of fish muscle myosin heavy chain and quantification of the specific polyribosome-bound polypeptide. Biochemical Journal 232, 467–470.CrossRefGoogle ScholarPubMed
Lund, B. & von der Decken, A. (1980). Protein synthesis in vitro after cryopreservation of rat skeletal muscle. Zeitschrift fur Tierphysiologie, Tierernahrung und Futtermittelkunde 44, 255–266.Google Scholar
Mackie, A. M. & Mitchell, A. I. (1985). Identification of gustatory feeding stimulants for fish – applications in aquaculture. In Nutrition andFeeding in Fish, pp. 177–189 [Cowey, C. B., Mackie, A. M. and Bell, J. G., editors]. New York and London: Academic Press.Google Scholar
Mommsen, T. P., French, C. J. & Hochachka, P. W. (1980). Sites and patterns of protein and amino acid utilization during the spawning migration of salmon. Canadian Journal of Zoology 58, 1785–1799.CrossRefGoogle Scholar
Nazar, S. D., Persson, G., Olin, T., Waters, S. & von der Decken, A. (1991). Sarcoplasmic and myofibrillar proteins in white trunk muscle of salmon (Salmo salar) after estradiol treatment. Comparative Biochemistry und Physiology 98B, 109–114.Google Scholar
Omstedt, P. T. & von der Decken, A. (1972). The influence of the nutritive value of proteins on the level of protein synthesis in vitro in rat skeletal muscle. British Journal of Nutrition 27, 467–474.Google Scholar
Persson, G., Lofberg, E. H. A. & von der Decken, A. (1991). Antigenicity of myosin heavy chain from skeletal muscle of fish species and humans as determined by the ELISA technique. Biochemical Archives 7, 1–11.Google Scholar
Setaro, F. & Morley, C. G. D. (1976). A modified fluorometric method for the determination of microgram quantities of DNA from cell or tissue cultures. Analytical, Biochemistry 71, 313–317.Google Scholar
Snedecor, G. W. & Cochran, W. G. (1980). Statistical Methods, 7th ed., pp. 149–174, 235–237. Ames, IA: The Iowa State University Press.Google Scholar
Suarez, R. K. & Mommsen, T. P. (1987). Gluconeogenesis in teleost fishes. Canadian Journal of Zoology 65, 1869–1882.Google Scholar
Tacon, A. G. J. & Jackson, A. J. (1985). Utilisation of conventional and unconventional protein sources in practical fish feeds. In Nutrition and Feeding in Fish, pp. 119–145 [Cowey, C. B., Mackie, A. M. and Bell, J. G., editors]. New York and London: Academic Press.Google Scholar
von der Decken, A. & Lied, E. (1992). Dietary protein levels affect growth and protein metabolism in trunk muscle of cod, Gadus morhua. Journal of Comparative Physiology B 162, 351–357.Google Scholar