Influence of feeding habits of fish on the characteristics of their visceral alkaline proteases with special reference to detergent compatibility

• Published in: Aquaculture research Vol. 52; no. 1; pp. 364 - 372
• Main Authors: Mohanty, Biswajit, Mohanty, Upasana, Majumdar, Ranendra K.
• Format: Journal Article
• Language: English
• Published: Oxford Hindawi Limited 01-01-2021
• Subjects: Alkaline protease; alkaline proteases; Ammonium sulfate; Carp; Chemical precipitation; Compatibility; Cyprinus carpio; Detergents; Dialysis; enzyme activators; enzyme inhibitors; Enzymes; Ethylenediaminetetraacetic acids; Fish; Freshwater; Freshwater fish; Freshwater fishes; Herbivores; Hydrogen peroxide; Inland water environment; Molecular weight; Oxidation; Oxidizing agents; pH effects; Pollutants; Protease; Proteolysis; Sodium; Sodium perborate; Stability; Surfactants; Temperature; Water purification
• ISSN: 1355-557X; 1365-2109
• DOI: 10.1111/are.14899

Technical characteristics and detergent compatibility of visceral alkaline proteases of three freshwater fish, namely Labeo rohita, Pangasianodon hypophthalmus and Cyprinus carpio of different feeding habits, were studied. Crude enzyme extract was partially purified by (NH4)2SO4 precipitation and dialysis. The molecular weight was in the range of 20–63 kDa. The enzyme purification folds post‐dialysis were found to be 1.55, 1.81 and 2.17 in case of Rohu, Pangas and Common carp respectively. The alkaline protease from Rohu, Pangas and Common carp exhibited maximum activity at pH 10.0, 9.0 and 11.0 respectively. The enzyme temperature optima observed were 60°C (Rohu and Pangas) and 70°C (Common carp). SBTI and EDTA inhibited more than 90% of the activity at conc. of 50 mM. Exposure of the proteases to non‐ionic surfactants like Tween 20–80 retained about 92%–100% and 76%–100% of their activity at conc. (v/v) of 1% and 5% respectively. Proteases were found less stable in the presence of SDS. There was moderate to lesser influence of H2O2 and sodium perborate on the proteolytic activity. The alkaline protease from omnivorous fish was found superior compared to the herbivore and carnivore in respect of pH and temperature optima and stability with detergents and oxidizing agents.