Physicochemical and functional properties of lentil protein isolates prepared by different drying methods
- Authors: Joshi, Matina , Adhikari, Benu , Aldred, Peter , Panozzo, Joe , Kasapis, Stefan
- Date: 2011
- Type: Text , Journal article
- Relation: Food Chemistry Vol. 129, no. 4 (2011), p. 1513-1522
- Full Text: false
- Description: Lentil protein isolate (LPI) extract was converted into powder by freeze drying, spray drying and vacuum drying. Differences in particle size distribution, protein subunit composition and colour and surface morphology were observed amongst the three drying methods. Spray and freeze-dried LPI powders exhibited higher solubility (81% and 78%, respectively) compared to vacuum dried powders (50%). The spray dried powders showed a low water absorption capacity (0.43 ± 0.02 g/g) compared to freeze (0.48 ± 0.02 g/g) and vacuum-dried (0.47 ± 0.01 g/g) LPI powders. Spray and freeze-dried powders displayed better gelation ability and higher gel strength, compared to vacuum-dried powder. Both spray and freeze-dried gels showed typical viscoelastic gel characteristics, with G′ dominating over G″ and very low loss tangent. The holding time required for gelation of vacuum dried powder at 90 °C was significantly longer, compared to spray and freeze dried powders. Hence, drying methods used for preparation of lentil protein isolate powders can affect physicochemical and associated functional properties. © 2011 Elsevier Ltd. All rights reserved.
Interfacial and emulsifying properties of lentil protein isolate
- 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:
- 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.