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Das, K. P.
- Protein-Fatty Acid Interaction in Spread Monolayers
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Authors
Affiliations
1 Department of Food Technology & Biochemical Engineering, Jadavpur University, Kolkata-700 032, IN
1 Department of Food Technology & Biochemical Engineering, Jadavpur University, Kolkata-700 032, IN
Source
Journal of Surface Science and Technology, Vol 29, No 1-2 (2013), Pagination: 85-100Abstract
The pressure-area isotherms at air-water interface of pure protein (bovine serum albumin, β-lactoglobulin, α-lactalbumin) and pure fatty acid (stearic acid and arachidic acid) and their mixtures of different weight fractions have been studied at pH 3.0, 7.0 and 12.0 respectively using Langmuir balance method. The surface pressures π of protein monolayer at different surface areas A of the pure proteins at different pH-values of the subphase are fitted in a virial equation expressed in linear form so that virial coefficients of different proteins have been evaluated at fixed pH. From the plot of second virial co-efficient Bs against several pH values, the isoelectric pH of BSA adsorbed at air-water interface is observed to be 7.0. From the analysis of π-A curves for the fatty acid and pure protein of several binary surface compositions, π-A curves for their mixtures have been obtained. These experimental values have been compared with their ideal values using additivity rule. Such analysis indicates that fatty acid and protein undergo binding interaction in monolayer phase at a given value of in many cases.Keywords
Spread Monolayer, Protein-Fatty Acid, Lipid Protein Interaction, Virial Coefficient, Airwater Interface.
- Adsorption of Ionic Surfactants at the Alumina/Water Interface
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Authors
Affiliations
1 Department of Food Technology and Biochemical Engineering, Jadavpur University, Calcutta-700 032, IN
1 Department of Food Technology and Biochemical Engineering, Jadavpur University, Calcutta-700 032, IN
Source
Journal of Surface Science and Technology, Vol 2, No 1 (1986), Pagination: 25-33Abstract
Adsorption of cationic and anionic surfactants from aqueous solutions on alumina particles has been studied. The alumina used was characterised by measuring isoelectric pH and the specific surface area. Adsorption experiments of cationic surfactants have been done on negatively charged alumina and of anionic surfactant on positively charged alumina. Adsorption is found to depend on the chain length of the surfactants. DTAB was found to be adsorbed perpendicularly while CTAB was almost flat at the interface. MTAB showed intermediate orientation. It was also observed that the saturation adsorption of surfactants occured at concentrations (csc) often not identical with cmc, but in most cases csc was less than cmc. SDS showed interfacial coagulation behaviour both at 30°C and 50°C. Increase of ionic strength decreases the amount of adsorption, Interchain cohesion within adsorbed monolayer was weak for CTAB adsorption, but was rather strong in case of MTAB and DTAB. As a result of this, some of the isotherms of MTAB DTAB showed steps. The results have been analysed according to thermodynamic principles.- Adsorption and Binding Interaction of Anionic Surfactant to Polysaccharides
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Authors
Affiliations
1 Department of Food Technology & Biochemical Engineering, Jadavpur University, Kolkata-700 032, IN
2 Chemistry Department, Bose Institute, 93, Acharya Prafulla Chandra Road, Kolkata-700 009, IN
1 Department of Food Technology & Biochemical Engineering, Jadavpur University, Kolkata-700 032, IN
2 Chemistry Department, Bose Institute, 93, Acharya Prafulla Chandra Road, Kolkata-700 009, IN
Source
Journal of Surface Science and Technology, Vol 19, No 1-2 (2003), Pagination: 21-34Abstract
The extents of adsorption of SDS (Sodium Dodecyl Sulphate) onto cellulose and binding of SDS to dextrin in aqueous medium have been measured as a function of surfactant concentration (C2) under different physicochemical conditions. Γ12 increases with increase of C2, until it reaches the maximum value, Γm2 at a critical concentration, Cm2. With increase of C2 further, Γ12 decreases linearly with C2 until it becomes zero at the azeotropic state. Γ12 becomes negative and its magnitude increases with increase of C2 further without reaching a limiting value. Using the concept of Gibbs surface excess, it has been shown that binding and adsorption of both surfactant and water to polysaccharide are responsible for the overall shape of the isotherm. The standard Gibbs free energy change, ΔG0 for the transfer of moles of surfactant to 1 kg of dextrin or cellulose at the state of surface saturation has been calculated using an integrated form of the Gibbs adsorption equation. The values of ΔG0 follow the same order as those of Γm2. The average slope of the linear plot of ΔG0 vs Γm2 is equal to 28.4 kJ/mol for binding experiment, and 27.9 kJ/mol for adsorption experiment. This corresponds to the standard free energy change (ΔG0B) for the transfer of 1 mol of surfactant from the bulk solution to the polysaccharide boundary when the bulk mole fraction of surfactant is altered from zero to unity. The values of ΔG0hy for different systems at high surfactant concentration have also been calculated using a linear extrapolation method, and they are found to be positive in all cases due to excess positive hydration of polysaccharide.Keywords
Adsorption, Binding, Surfactant, Polysaccharides.- Structural Stabilization and Functional Enhancement of Miceller Protein α-Crystallin by ATP and Zn2+
Abstract Views :287 |
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Authors
Affiliations
1 Protein Chemistry Laboratory, Department of Chemistry, Bose Institute, 93/1 A.P.C. Road, Kolkata - 700 009, West Bengal, IN
1 Protein Chemistry Laboratory, Department of Chemistry, Bose Institute, 93/1 A.P.C. Road, Kolkata - 700 009, West Bengal, IN
Source
Journal of Surface Science and Technology, Vol 31, No 1-2 (2015), Pagination: 13-20Abstract
α-Crystallin is the most abundant protein of the eye lens. It has a micelle like associated structure and has a special chaperone- like property to prevent aggregation of other proteins. This function of α-crystallin plays a crucial role in maintaining the transparency of eye lens. Because of the absence of protein turn over in the lens, the proteins in the lens must survive the entire lifetime of the living species. This requires high structural stability of α-crystallin. In this article we present a brief review of our work on the mechanism of stabilization of α-crystallin by Zn. We have shown that some metal ions, Zn in particular play a very important role in enhancing the function of α-crystallin by enhancing its exposed hydrophobic surface. We have also characterized the Zn binding to α-crystallin by MALDI mass spectrometry and have shown that the structural stabilization occurs through intersubunit bridging by Zn. The binding region in the α-crystallin sequence has also been identified. The physiological relevance of enhanced chaperone function and structural stability is discussed.Keywords
Alpha Crystallin, Chaperone Function, Eye Lens Protein, Metal Binding, Miceller Protein, Protein AggregationReferences
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