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:
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- 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.
The effect of protein types and low molecular weight surfactants on spray drying of sugar-rich foods
- Jayasundera, Mithila, Adhikari, Benu, Adhikari, Raju, Aldred, Peter
- Authors: Jayasundera, Mithila , Adhikari, Benu , Adhikari, Raju , Aldred, Peter
- Date: 2010
- Type: Text , Journal article
- Relation: Food Hydrocolloids Vol. 25, no. 3 (2010), p. 459-469
- Full Text:
- Reviewed:
- Description: The effect of protein types and low molecular weight surfactants (LMS) on spray drying of sugar-rich foods has been studied using sucrose as a model sugar and sodium caseinate (NaCas) and pea protein isolate (PPI) as model proteins. Sodium stearoyl lactylate (SSL) and Polysorbate 80 (Tween-80) were chosen as model ionic and non-ionic LMS. The sucrose:NaCas and sucrose:PPI solid ratios were maintained at (99.5:0.5) and (99:1), respectively and spray-dried maintaining 25% solids in feed solutions. It was found that the proteins preferentially migrated to the air-water interface reasonably swiftly and the addition of LMS resulted into partial or complete displacement of the proteins from the air-water interface. More than 80% of amorphous sucrose powder was produced with the addition of 0.13% (w/w) of NaCas in feed solution. PPI was not as effective and produced less than 50% recovery even at 0.26% (w/w) in feed. Addition of 0.01-0.05% SSL displaced 2.0% and 29.3% of proteins from the surface of sucrose-NaCas-SSL droplet, respectively, resulting in a 6.5 ± 1.2% to 51.9 ± 1.9% reduction in powder recovery. The extent of protein displacement was higher when SSL was added into sucrose-PPI solution; however, the powder recovery was not much affected. The addition of 0.01% Tween-80 in sucrose-NaCas solution resulted in a 48.2 ± 1.5% reduction in powder recovery and at 0.05% concentration, it displaced a substantial amount or all the NaCas from the droplet surface and no powder was recovered. The addition of 0.01% and 0.05% Tween-80 into sucrose-PPI solution resulted into very low powder recoveries (24.9 ± 0.4% and 29.5 ± 1.8%, respectively). The glass transition temperature (Tg) results revealed that the amount of protein required for successful spray drying of sucrose-protein solutions depends on the amount of proteins present on the droplet surface but not on the bulk concentration. X-ray diffraction and scanning electron microscopy results showed that the powders of sucrose-NaCas/PPI and sucrose-NaCas/PPI with 0.01% SSL were mostly amorphous while those with sucrose-NaCas/PPI-Tween-80 (0.01%), sucrose-PPI-Tween-80 (0.05%) and sucrose-NaCas/PPI-SSL (0.05%) were crystalline. © 2010 Elsevier Ltd. All rights reserved.
The effect of protein types and low molecular weight surfactants on spray drying of sugar-rich foods
- Authors: Jayasundera, Mithila , Adhikari, Benu , Adhikari, Raju , Aldred, Peter
- Date: 2010
- Type: Text , Journal article
- Relation: Food Hydrocolloids Vol. 25, no. 3 (2010), p. 459-469
- Full Text:
- Reviewed:
- Description: The effect of protein types and low molecular weight surfactants (LMS) on spray drying of sugar-rich foods has been studied using sucrose as a model sugar and sodium caseinate (NaCas) and pea protein isolate (PPI) as model proteins. Sodium stearoyl lactylate (SSL) and Polysorbate 80 (Tween-80) were chosen as model ionic and non-ionic LMS. The sucrose:NaCas and sucrose:PPI solid ratios were maintained at (99.5:0.5) and (99:1), respectively and spray-dried maintaining 25% solids in feed solutions. It was found that the proteins preferentially migrated to the air-water interface reasonably swiftly and the addition of LMS resulted into partial or complete displacement of the proteins from the air-water interface. More than 80% of amorphous sucrose powder was produced with the addition of 0.13% (w/w) of NaCas in feed solution. PPI was not as effective and produced less than 50% recovery even at 0.26% (w/w) in feed. Addition of 0.01-0.05% SSL displaced 2.0% and 29.3% of proteins from the surface of sucrose-NaCas-SSL droplet, respectively, resulting in a 6.5 ± 1.2% to 51.9 ± 1.9% reduction in powder recovery. The extent of protein displacement was higher when SSL was added into sucrose-PPI solution; however, the powder recovery was not much affected. The addition of 0.01% Tween-80 in sucrose-NaCas solution resulted in a 48.2 ± 1.5% reduction in powder recovery and at 0.05% concentration, it displaced a substantial amount or all the NaCas from the droplet surface and no powder was recovered. The addition of 0.01% and 0.05% Tween-80 into sucrose-PPI solution resulted into very low powder recoveries (24.9 ± 0.4% and 29.5 ± 1.8%, respectively). The glass transition temperature (Tg) results revealed that the amount of protein required for successful spray drying of sucrose-protein solutions depends on the amount of proteins present on the droplet surface but not on the bulk concentration. X-ray diffraction and scanning electron microscopy results showed that the powders of sucrose-NaCas/PPI and sucrose-NaCas/PPI with 0.01% SSL were mostly amorphous while those with sucrose-NaCas/PPI-Tween-80 (0.01%), sucrose-PPI-Tween-80 (0.05%) and sucrose-NaCas/PPI-SSL (0.05%) were crystalline. © 2010 Elsevier Ltd. All rights reserved.
Surface modification of spray dried food and emulsion powders with surface-active proteins : A review
- Jayasundera, Mithila, Adhikari, Benu, Aldred, Peter, Ghandi, Amir
- Authors: Jayasundera, Mithila , Adhikari, Benu , Aldred, Peter , Ghandi, Amir
- Date: 2009
- Type: Text , Journal article
- Relation: Journal of Food Engineering Vol. 93, no. 3 (2009), p. 266-277
- Full Text:
- Reviewed:
- Description: Spray drying is a well-established and widely used method for transforming a wide range of liquid food products into powder form. Stickiness is the limitation in spray drying of different sugar and acid-rich food products. To minimize this problem process and material science based approaches are in place. However, these remedies have their own drawbacks. Surface modification of droplets/particles is a novel way to minimize stickiness. It is timely that the research efforts on surface modification of droplets/particles be reviewed. Therefore, this review highlights the recent research dealing with surface modification of emulsions and spray dried powders. The theoretical foundation, mechanisms and methods used to achieve surface modification of food and emulsion powders are highlighted. © 2009 Elsevier Ltd. All rights reserved.
- Authors: Jayasundera, Mithila , Adhikari, Benu , Aldred, Peter , Ghandi, Amir
- Date: 2009
- Type: Text , Journal article
- Relation: Journal of Food Engineering Vol. 93, no. 3 (2009), p. 266-277
- Full Text:
- Reviewed:
- Description: Spray drying is a well-established and widely used method for transforming a wide range of liquid food products into powder form. Stickiness is the limitation in spray drying of different sugar and acid-rich food products. To minimize this problem process and material science based approaches are in place. However, these remedies have their own drawbacks. Surface modification of droplets/particles is a novel way to minimize stickiness. It is timely that the research efforts on surface modification of droplets/particles be reviewed. Therefore, this review highlights the recent research dealing with surface modification of emulsions and spray dried powders. The theoretical foundation, mechanisms and methods used to achieve surface modification of food and emulsion powders are highlighted. © 2009 Elsevier Ltd. All rights reserved.
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