Effect of Optimum and Suboptimum Dietary Protein on Hemolymph Physiology, Oxidative Physiology, Plasma Fatty Acids, and Histoarchitectural Modulations in Farmed Giant Freshwater Prawns Macrobrachium rosenbergii

REFERENCES

• Antiporda, J. L. 1986. Optimum dietary protein requirement for Macrobrachium rosenbergii juveniles. Food and Agriculture Organization of the United Nations, Network of Aquaculture Centers in Asia, NACA/WP/86/45, Bangkok.
   Google Scholar
• AOAC (Association of Official Analytical Chemists). 1995. Official methods of analysis of AOAC International, 16th edition. AOAC International, Arlington, Virginia.
   Google Scholar
• Augstinasso, K. B. 1957. Assay methods for cholinesterases. Pages 1–63 in D. Glick, editor. Method of biochemical analysis, volume 5. Interscience Publication, New York.
   Google Scholar
• Austic, R. E., R. R. Dietert, Y. J. Sung, and R. L. Taylor. 1991. Amino acids in immune function. Pages 109–114 in Proceedings of the 1991 Cornell nutrition conference for feed manufacturers. Cornell University, Ithaca, New York.
   Google Scholar
• Barton, K. N., M. F. Gerrits, and J. S. Ballantyne. 1995. Effects of exercise on plasma non-esterified fatty acids and free amino acids in Arctic Char. Journal of Experimental Zoology 271:183–189.
   Google Scholar
• Behanan, L., and S. Mathew. 2004. Nucleic acid and protein concentrations in the muscle of Macrobrachium rosenbergii juveniles at different periods of growth. Asian Fisheries Science 17:111–119.
   Google Scholar
• Buentello, J. A., and D. M. Gatlin. 2001. Effects of elevated dietary arginine on resistance of Channel Catfish to exposure to Edwardsiella ictaluri. Journal of Aquatic Animal Health 13:194–201.
   Web of Science ®Google Scholar
• Cheng, W., and J. C. Chen. 2002. The virulence of Enterococcus to freshwater prawn Macrobrachium rosenbergii and its immune resistance under ammonia stress. Fish and Shellfish Immunology 12:97–109.
   PubMed Web of Science ®Google Scholar
• D’Abramo, L. R., and M. B. New. 2000. Nutrition, feeds and feeding. Pages 203–220 in M. B. New and W. C. Valenti, editors. Freshwater prawn culture. Blackwell Science, Oxford, UK.
   Google Scholar
• Das, S. K., V. K. Tiwari, G. Venkateshwarlu, A. K. Reddy, J. Parhi, P. Sharma, and J. K. Chettri. 2007. Growth, survival and fatty acid composition of Macrobrachium rosenbergii (de Man, 1879) postlarvae fed HUFA-enriched Moina micrura. Aquaculture 269:464–475.
   Web of Science ®Google Scholar
• Debnath, D., A. K. Pal, N. P. Sahu, S. Yengkokpam, K. Baruah, D. Choudhury, and G. Venkateshwarlu. 2007. Digestive enzymes and metabolic profile of Labeo rohita fingerlings fed diets with different crude protein levels. Comparative Biochemistry and Physiology Part B 146:107–114.
   PubMed Web of Science ®Google Scholar
• Folch, J., M. Lees, and G. H. Stoane-Stanley. 1957. A simple method for the isolation and purification of total lipids from animal tissue. Journal of Biological Chemistry 226:497–506.
   PubMed Web of Science ®Google Scholar
• Fuentes, G. R., and G. G. Bouchot. 2004. Characterization of cholinesterase activity from different tissues of Nile Tilapia (Oreochromis niloticus). Marine Environmental Research 6:505–509.
   Web of Science ®Google Scholar
• Gai, F., P. G. Peiretti, A. Brugiapaglia, and L. Gasco. 2016. Effects of dietary protein source and feeding regime on growth performance, nutrient digestibility, fatty acids, and quality characteristics of Rainbow Trout, Oncorhynchus mykiss, fillets. Journal of the World Aquaculture Society 47:496–507.
   Web of Science ®Google Scholar
• Hestrin, G. E. 1949. The reaction of acetyl choline esters and other carboxylic acid derivatives with hydroxylamine and its analytical application. Journal of Biological Chemistry 180:249–261.
   PubMed Web of Science ®Google Scholar
• IUBMB (International Union of Biochemistry and Molecular Biology). 1992. Enzyme nomenclature 1992. Academic Press, San Diego, California.
   Google Scholar
• Jones, S. B., S. L. Beauvais, S. K. Brewer, and E. E. Little. 1999. Physiological and behavioural measures of neurotoxicity in Rainbow Trout. Pages 27–28 in C. Kennedy and D. Mackinlay, editors. Fish response to toxic environments: symposium proceedings. Townson University, Baltimore, Maryland.
   Google Scholar
• Kiessling, K. H., and A. Kiessling. 1993. Selective utilization of fatty acids in Rainbow Trout (Oncorhynchus mykiss Walbaum) red muscle mitochondria. Canadian Journal of Zoology 71:248–251.
   Web of Science ®Google Scholar
• Konashi, S., K. Takahashi, and Y. Akiba. 2000. Effects of dietary essential amino acid deficiencies on immunological variables in broiler chickens. British Journal of Nutrition 83:449–456.
   PubMed Web of Science ®Google Scholar
• Kori-Siakpere, O., M. G. Ogbe, and R. B. Ikomi. 2011. Variations in lactate dehydrogenase and creatine kinase activities in the plasma of the African Catfish: Clarias gariepinus (Burchell, 1822) exposed to sub-lethal concentrations of potassium permanganate. Annals of Biological Research 2:19–25.
   Google Scholar
• Krogdahl, A., A. M. Bakke-McKellep, K. H. Røed, and G. Baeverfjord. 2000. Feeding Atlantic Salmon Salmo salar L. soybean products: effects on disease resistance (furunculosis), and lysozyme and IgM levels in the intestinal mucosa. Aquaculture Nutrition 6:77–84.
   Web of Science ®Google Scholar
• Kumar, S., N. P. Sahu, A. K. Pal, D. Choudhury, Y. Sona, and S. C. Mukherjee. 2005. Effect of dietary carbohydrate on hematology, respiratory burst activity and histological changes in Labeo rohita juveniles. Fish and Shellfish Immunology 19:331–344.
   PubMed Web of Science ®Google Scholar
• Manush, S. M., A. K. Pal, T. Das, and S. C. Mukherjee. 2005. Dietary high protein and vitamin C mitigate stress due to chelate claw ablation in Macrobrachium rosenbergii males. Comparative Biochemistry and Physiology Part A 142:10–18.
   PubMed Web of Science ®Google Scholar
• Miller, E. L. 2004. Protein nutrition requirements of farmed livestock and dietary supply. Pages 29–76 in Protein sources for the animal feed industry, expert consultation and workshop, Bangkok. Food and Agriculture Organization of the United Nations, Rome.
   Google Scholar
• Molina, R., I. Moreno, S. A. Pichardo, R. Moyano, J. G. Monterde, and A. Cameán. 2005. Acid and alkaline phosphatase activities and pathological changes induced in tilapia fish (Oreochromis sp.) exposed sub-chronically to microcystins from toxic cyanobacterial blooms under laboratory conditions. Toxicon 46:725–735.
   Google Scholar
• Murthy, V. K., Y. D. Reddy, R. M. Reddy, K. M. Bhaskar, and S. Govindappa. 1984. Changes in brain acetyl cholinesterase activity in behavior of freshwater fish in acid polluted environment. Environment and Ecology 2:79–82.
   Google Scholar
• Oser, B. L. 1976. Hawk’s physiological chemistry, 14th edition. Tata McGraw Hill, New Delhi.
   Google Scholar
• Paulose, C. L. 1996. Effect of dietary proteins on growth, food conversion and digestive enzyme activity of juvenile Macrobrachium rosenbergii. Doctoral dissertation. Cochin University of Science and Technology, Cochin, India.
   Google Scholar
• Reed, L. 1987. Nutrition of juvenile Macrobrachium rosenbergii: evaluation of an experimental system and the effects of dietary lecithin and protein quantity. Master’s thesis. Mississippi State University, Mississippi State.
   Google Scholar
• Reigh, R. C., and R. R. Stickney. 1989. Effects of purified dietary fatty acids on the fatty acid composition of freshwater shrimp, Macrobrachium rosenbergii. Aquaculture 77:157–174.
   Web of Science ®Google Scholar
• Reinhold, J. G. 1953. Manual determination of serum total protein, albumin and globulin fraction by Biuret method. Pages 88–98 in M. Reiner, editor. Standard method of clinical chemistry. Academic Press, New York.
   Google Scholar
• Roberts, R. J. 1989. Nutritional pathology of teleosts. Pages 337–362 in R. J. Roberts, editor. Fish pathology. Bailliere Tindall, London.
   Google Scholar
• Rooke, J. A., M. Slessor, H. Fraser, and J. R. Thonson. 1998. Growth performance and gut function of piglets weaned at four weeks of age and fed protease-treated soya-bean meal. Animal Feed Science and Technology 70:175–190.
   Web of Science ®Google Scholar
• Sagar, V., N. P. Sahu, A. K. Pal, K. K. Jain, and G. Venugopal. 2009. Growth and digestive enzymes of Macrobrachium rosenbergii juveniles: effect of different stock types and dietary protein levels under a similar culture environment. Aquaculture Research 40:1383–1393.
   Web of Science ®Google Scholar
• Sarma, K. 2004. Biochemical responses of Channa punctatus to endosulfan and its implication in environmental monitoring. Doctoral dissertation. Central Institute of Fisheries Education, Mumbai, India.
   Google Scholar
• Takahara, S., B. H. Hamilton, J. V. Nell, T. Y. Kobra, Y. Ogawa, and E. T. Nishimura. 1960. Hypocatalasemia: a new genetic carried state. Journal of Clinical Investigation 29:610–619.
   Web of Science ®Google Scholar
• Tsiagbe, V. K., M. E. Cook, A. E. Harper, and M. L. Sunde. 1987. Efficacy of cysteine in replacing methionine in the immune response of broiler chicks. Poultry Science 66:1138–1146.
   PubMed Web of Science ®Google Scholar
• Viveros, A., A. Brenes, I. Arija, and C. Centeno. 2002. Effects of microbial phytase supplementation on mineral utilization and serum enzyme activities in broiler chicks fed different levels of phosphorous. Poultry Science 81:1172–1183.
   PubMed Web of Science ®Google Scholar
• Waltz, O. P., and J. Pallauf. 2002. Microbial phytase combined with amino acid supplementation reduces P and N excretion of growing and finishing pigs without loss of performance. International Journal of Food Science and Technology 371:835–848.
   Web of Science ®Google Scholar
• Wang, L., J. Wu, W. N. Wang, D. X. Cai, Y. Liu, and A. L. Wang. 2012. Glutathione peroxidase from the white shrimp Litopenaeus vannamei: characterization and its regulation upon pH and Cd exposure. Ecotoxicology 21:1585–1592.
   PubMed Web of Science ®Google Scholar