Annual ryegrass (Lolium rigidum Gaud) competition altered wheat grain quality : A study under elevated atmospheric CO2 levels and drought conditions
- Fernando, Nimesha, Florentine, Singarayer, Naiker, Mani, Panozzo, Joe, Chauhan, Bhagirath
- Authors: Fernando, Nimesha , Florentine, Singarayer , Naiker, Mani , Panozzo, Joe , Chauhan, Bhagirath
- Date: 2019
- Type: Text , Journal article
- Relation: Food Chemistry Vol. 276, no. (2019), p. 285-290
- Full Text:
- Reviewed:
- Description: Annual ryegrass is one of the most serious, costly weeds of winter cropping systems in Australia. To determine whether its competition-mediated plant defence mechanisms effect on wheat grain quality, wheat (cv. Yitpi) and annual ryegrass were grown under two levels of CO2 (400 ppm; (a[CO2]) vs 700 ppm; (e[CO2]), two levels of water (well-watered vs drought) and two types of competition (wheat only; (W), and wheatxannual ryegrass; (W x R) with four replicates. The competitionx[CO2] interaction had a significant effect on wheat grain protein content, where it was increased in W x R under both e[CO2] (+ 17%) and a[CO2] (+ 21%). Grain yield, total grain reducing power and phenolic content were significantly affected by [CO2] x drought x competition. In a summary, annual ryegrass competition significantly altered the wheat grain quality under both [CO2] levels (depending on the soil water level), while also decreasing the grain yield.
- Authors: Fernando, Nimesha , Florentine, Singarayer , Naiker, Mani , Panozzo, Joe , Chauhan, Bhagirath
- Date: 2019
- Type: Text , Journal article
- Relation: Food Chemistry Vol. 276, no. (2019), p. 285-290
- Full Text:
- Reviewed:
- Description: Annual ryegrass is one of the most serious, costly weeds of winter cropping systems in Australia. To determine whether its competition-mediated plant defence mechanisms effect on wheat grain quality, wheat (cv. Yitpi) and annual ryegrass were grown under two levels of CO2 (400 ppm; (a[CO2]) vs 700 ppm; (e[CO2]), two levels of water (well-watered vs drought) and two types of competition (wheat only; (W), and wheatxannual ryegrass; (W x R) with four replicates. The competitionx[CO2] interaction had a significant effect on wheat grain protein content, where it was increased in W x R under both e[CO2] (+ 17%) and a[CO2] (+ 21%). Grain yield, total grain reducing power and phenolic content were significantly affected by [CO2] x drought x competition. In a summary, annual ryegrass competition significantly altered the wheat grain quality under both [CO2] levels (depending on the soil water level), while also decreasing the grain yield.
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.
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