Interfacial and emulsifying properties of lentil protein isolate
- Joshi, Matina, Adhikari, Benu, Aldred, Peter, Panozzo, Joe, Kasapis, Stefan, Barrow, Colin
- Authors: Joshi, Matina , Adhikari, Benu , Aldred, Peter , Panozzo, Joe , Kasapis, Stefan , Barrow, Colin
- Date: 2012
- Type: Text , Journal article
- Relation: Food Chemistry Vol.134 no.3 (2012), p.343-1353
- Full Text:
- Reviewed:
- Description: The dynamic interfacial tension (DIFT) at oil-water interface, diffusion coefficients, surface hydrophobicity, zeta potential and emulsifying properties, including emulsion activity index (EAI), emulsion stability index (ESI) and droplet size of lentil protein isolate (LPI), were measured at different pH and LPI concentration, in order to elucidate its emulsifying behaviour. Sodium caseinate (NaCas), whey protein isolate (WPI), bovine serum albumin (BSA) and lysozyme (Lys) were used as benchmark proteins and their emulsifying property was compared with that of LPI. The speed of diffusion-controlled migration of these proteins to the oil/water interface, was in the following order: NaCas > LPI > WPI > BSA > Lys, while their surface hydrophobicity was in the following order: BSA > LPI > NaCas > WPI > Lys. The EAI of emulsions stabilised by the above proteins ranged from 90.3 to 123.3 m 2/g and it was 93.3 ± 0.2 m 2/g in LPI-stabilised emulsion. However, the stability of LPI-stabilised emulsions was slightly lower compared to that of WPI and NaCas-stabilised emulsions at the same protein concentration at pH 7.0. The ESI of LPI emulsions improved substantially with decrease in droplet size when protein concentration was increased (20-30 mg/ml). Reduction of disulphide bonds enhanced both the EAI and ESI compared to untreated samples. Heat treatment of LPI dispersions resulted in poor emulsion stability due to molecular aggregation. The stability of LPI-stabilised emulsions was found to decrease in the presence of NaCl. This study showed that LPI can be as effective emulsifiers of oil-in-water emulsions as are WPI and NaCas at ≥20 mg/ml concentrations both at low and neutral pH. The emulsifying property of LPI can be improved by reducing the intra and inter-disulphide bond by using appropriate reducing agents. © 2012 Elsevier Ltd. All rights reserved.
- Authors: Joshi, Matina , Adhikari, Benu , Aldred, Peter , Panozzo, Joe , Kasapis, Stefan , Barrow, Colin
- Date: 2012
- Type: Text , Journal article
- Relation: Food Chemistry Vol.134 no.3 (2012), p.343-1353
- Full Text:
- Reviewed:
- Description: The dynamic interfacial tension (DIFT) at oil-water interface, diffusion coefficients, surface hydrophobicity, zeta potential and emulsifying properties, including emulsion activity index (EAI), emulsion stability index (ESI) and droplet size of lentil protein isolate (LPI), were measured at different pH and LPI concentration, in order to elucidate its emulsifying behaviour. Sodium caseinate (NaCas), whey protein isolate (WPI), bovine serum albumin (BSA) and lysozyme (Lys) were used as benchmark proteins and their emulsifying property was compared with that of LPI. The speed of diffusion-controlled migration of these proteins to the oil/water interface, was in the following order: NaCas > LPI > WPI > BSA > Lys, while their surface hydrophobicity was in the following order: BSA > LPI > NaCas > WPI > Lys. The EAI of emulsions stabilised by the above proteins ranged from 90.3 to 123.3 m 2/g and it was 93.3 ± 0.2 m 2/g in LPI-stabilised emulsion. However, the stability of LPI-stabilised emulsions was slightly lower compared to that of WPI and NaCas-stabilised emulsions at the same protein concentration at pH 7.0. The ESI of LPI emulsions improved substantially with decrease in droplet size when protein concentration was increased (20-30 mg/ml). Reduction of disulphide bonds enhanced both the EAI and ESI compared to untreated samples. Heat treatment of LPI dispersions resulted in poor emulsion stability due to molecular aggregation. The stability of LPI-stabilised emulsions was found to decrease in the presence of NaCl. This study showed that LPI can be as effective emulsifiers of oil-in-water emulsions as are WPI and NaCas at ≥20 mg/ml concentrations both at low and neutral pH. The emulsifying property of LPI can be improved by reducing the intra and inter-disulphide bond by using appropriate reducing agents. © 2012 Elsevier Ltd. All rights reserved.
A new technique to measure interfacial tension of transformer oil using UV-Vis spectroscopy
- Abu Bakar, Norazhar, Abu-Siada, Ahmed, Islam, Syed, El-Naggar, Mohammed
- Authors: Abu Bakar, Norazhar , Abu-Siada, Ahmed , Islam, Syed , El-Naggar, Mohammed
- Date: 2015
- Type: Text , Journal article
- Relation: IEEE Transactions on Dielectrics and Electrical Insulation Vol. 22, no. 2 (2015), p. 1275-1282
- Full Text:
- Reviewed:
- Description: Interfacial tension (IFT) and acid numbers of insulating oil are correlated with the number of years that a transformer has been in service and are used as a signal for transformer oil reclamation. Oil sampling for IFT measurement calls for extra precautions due to its high sensitivity to various oil parameters and environmental conditions. The current used technique to measure IFT of transformer oil is relatively expensive, requires an expert to conduct the test and it takes long time since the extraction of oil sample, sending it to external laboratory and getting the results back. This paper introduces a new technique to estimate the IFT of transformer oil using ultraviolet-to-visible (UV-Vis) spectroscopy. UV-Vis spectral response of transformer oil can be measured instantly with relatively cheap equipment, does not need an expert person to conduct the test and has the potential to be implemented online. Results show that there is a good correlation between oil spectral response and its IFT value. Artificial neural network (ANN) approach is proposed to model this correlation.
- Authors: Abu Bakar, Norazhar , Abu-Siada, Ahmed , Islam, Syed , El-Naggar, Mohammed
- Date: 2015
- Type: Text , Journal article
- Relation: IEEE Transactions on Dielectrics and Electrical Insulation Vol. 22, no. 2 (2015), p. 1275-1282
- Full Text:
- Reviewed:
- Description: Interfacial tension (IFT) and acid numbers of insulating oil are correlated with the number of years that a transformer has been in service and are used as a signal for transformer oil reclamation. Oil sampling for IFT measurement calls for extra precautions due to its high sensitivity to various oil parameters and environmental conditions. The current used technique to measure IFT of transformer oil is relatively expensive, requires an expert to conduct the test and it takes long time since the extraction of oil sample, sending it to external laboratory and getting the results back. This paper introduces a new technique to estimate the IFT of transformer oil using ultraviolet-to-visible (UV-Vis) spectroscopy. UV-Vis spectral response of transformer oil can be measured instantly with relatively cheap equipment, does not need an expert person to conduct the test and has the potential to be implemented online. Results show that there is a good correlation between oil spectral response and its IFT value. Artificial neural network (ANN) approach is proposed to model this correlation.
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