ISSN: 0973-7510
E-ISSN: 2581-690X
The surfactants interact with proteins in multifarious ways depending on surfactant concentration and structure. Proteins like PTPases play a key role in the cellular signaling process. The effect of surfactant on PTPase was carried out by immersing peanut (8 day old germinating) seedlings using different concentrations of NaDBS (1-10%) for 2 h. The specific activity of PTPase was found to decrease with increase in surfactant concentration. 8-fold decrease in specific activity of PTPase was noticed at 6% NaDBS. However at high concentration of NaDBS it becomes constant. However the different parts of the peanut seedlings treated with 6% NaDBS for 2 h at room temperature shown that the specific activity (unit/mg-protein) of PTPase was lowered to about 5.0 fold in root and 3.0 fold in cotyledon. This might be due to the inactivation and activation of the PTPase by anionic, cationic and nonionic surfactants involved in both electrostatic and hydrophobic interactions. From our observations it was found that the enzyme-surfactant interaction probably occurred near the active site and the role of PTPases in plants is a stress-related cellular process.
Arachis hypogaea L, Peanut, Protein tyrosine phosphatases (PTPases), Anionic surfactant, Cationic surfactant and Non-ionic surfactant
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