Molecular forces involved in heat-induced pea protein gelation: Effects of various reagents on the rheological properties of salt-extracted pea protein gels

Sun, Xiang Dong; Arntfield, Susan D.

doi:10.1016/j.foodhyd.2011.12.014

Cited by 201 publications

(117 citation statements)

References 52 publications

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“…Moreover, the ratio of gliadins and glutenins increased while the ratio of large polymers decreases in wheat grain flour ( Panozzo and Eagles, 2000 ; DuPont and Altenbach, 2003 ). Similarly, in pea, high temperature denatured and aggregated the seed storage proteins (globulins, legumin, and vicilin) in pea ( Mession et al, 2013 ); which might be due to loss of covalent and non-covalent interactions ( Sun and Arntfield, 2012 ). In the same way, heat stress denatured β-conglycinin in soybean ( Iwabuchi and Yamauchi, 1984 ) and damaged globulin and phaseolin ( Hernández-Unzón and Ortega-Delgado, 1988 ).…”

Section: Alterations Of Storage Proteins and Lipids During Seed Fillimentioning

confidence: 99%

Drought or/and Heat-Stress Effects on Seed Filling in Food Crops: Impacts on Functional Biochemistry, Seed Yields, and Nutritional Quality

et al. 2018

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Drought (water deficits) and heat (high temperatures) stress are the prime abiotic constraints, under the current and climate change scenario in future. Any further increase in the occurrence, and extremity of these stresses, either individually or in combination, would severely reduce the crop productivity and food security, globally. Although, they obstruct productivity at all crop growth stages, the extent of damage at reproductive phase of crop growth, mainly the seed filling phase, is critical and causes considerable yield losses. Drought and heat stress substantially affect the seed yields by reducing seed size and number, eventually affecting the commercial trait ‘100 seed weight’ and seed quality. Seed filling is influenced by various metabolic processes occurring in the leaves, especially production and translocation of photoassimilates, importing precursors for biosynthesis of seed reserves, minerals and other functional constituents. These processes are highly sensitive to drought and heat, due to involvement of array of diverse enzymes and transporters, located in the leaves and seeds. We highlight here the findings in various food crops showing how their seed composition is drastically impacted at various cellular levels due to drought and heat stresses, applied separately, or in combination. The combined stresses are extremely detrimental for seed yield and its quality, and thus need more attention. Understanding the precise target sites regulating seed filling events in leaves and seeds, and how they are affected by abiotic stresses, is imperative to enhance the seed quality. It is vital to know the physiological, biochemical and genetic mechanisms, which govern the various seed filling events under stress environments, to devise strategies to improve stress tolerance. Converging modern advances in physiology, biochemistry and biotechnology, especially the “omics” technologies might provide a strong impetus to research on this aspect. Such application, along with effective agronomic management system would pave the way in developing crop genotypes/varieties with improved productivity under drought and/or heat stresses.

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Section: Alterations Of Storage Proteins and Lipids During Seed Fillimentioning

confidence: 99%

Drought or/and Heat-Stress Effects on Seed Filling in Food Crops: Impacts on Functional Biochemistry, Seed Yields, and Nutritional Quality

et al. 2018

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“…() found that gels made by NEM blocked protein had higher firmness, but these gels could be ruptured more easily than those with more disulfide bonds. Sun & Arntfield () monitored the changes of molecular forces in heat‐induced pea protein gel in the presence of different chemicals, and observed that disulfide bonds were not required for gel formation since no significant influence on storage modulus was found when adding different concentrations of β‐mercaptoethanol. The method used by researchers mentioned above to investigate molecular forces involved in gel network was based on inhibiting the formation of different interactions or bonds in gel network by adding denaturing agent before gelling.…”

Section: Introductionmentioning

confidence: 99%

“…The strength of these two forces in gel was characterised by determining the dissolution kinetics of heat‐induced soy protein gels in different dissolving mediums. Sodium dodecyl sulfate (SDS) was known to destabilise hydrophobic interactions (Yu et al ., ), and DTT was used to disrupt disulfide bonds (Sun & Arntfield, ). The protein composition and concentration of dissolving samples of soy gel were analysed by reducing SDS‐PAGE and SEC‐HPLC.…”

Section: Introductionmentioning

confidence: 99%

The relationship between breaking force and hydrophobic interactions or disulfide bonds involved in heat‐induced soy protein gels as affected by heating time and temperature

Hua

2018

Int J of Food Sci Tech

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Hydrophobic interactions and disulfide bonds involved in heat-induced soy protein gels were characterised by determining the dissolution kinetics of gels. Reducing SDS-PAGE results revealed that all proteins in gel network could be dissolved simultaneously by 1% (w/v) SDS solution, while a majority of glycinin (11S) A polypeptide and a moderate amount of 11S-B polypeptides, 7S-a 0 , a, c, and b subunits were found in 2% (w/v) DTT dissolving samples. Stronger interaction force between proteins in gel network would result in lower dissolution constant rate. The breaking force of soy gels increased from 543 to 2171 g force with increasing heating temperature from 85 to 100°C, and denaturation of 11S globulins played an important role in the development of gel network. As increasing heating time from 30 to 120 min, the breaking force of gels increased from 1687 to 2175 g force , then decreased to 1253 g force when the time was prolonged to 240 min. Negative correlations were observed between breaking force and dissolution constant rate k SDS or Dk, which suggested that the strengthening of both hydrophobic interactions and disulfide bonds.

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“…The crosslinking of proteins is caused by various molecular forces, including hydrogen bonding, hydrophobic interactions, disulphide bonding, ionic attractions, or a combination of these forces. [30] Mizuno et al [29] pointed out that the Tg of biopolymers in general can be determined by the state of the noncovalent bonds. Taylor [31] stated that lower glass transition of matrix could be due to less hydrogen bonding involvement in glassy state.…”

Section: Differential Scanning Calorimetermentioning

confidence: 99%

Gelling properties of myofibrillar protein from abalone (Haliotis Discus Hannai Ino) muscle

Chen

et al. 2018

International Journal of Food Properties

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Texture of muscle food is dependent on the gelation properties of myofibrillar protein. Defining the performance of myofibrillar protein during gelation is beneficial for maintaining quality and developing muscle food. The myofibrillar protein from abalone muscle (AMP) was extracted and the gel-forming ability was investigated. The lowest protein solubility of AMP in distilled water was obtained at pH 5.5, but shifted to a lower pH value by ionic strength. The breaking force and deformation of AMP gel formed at pH 7.0 were 48.00 g and 27.70 mm, respectively, but they could not be detected at pH 5.0 and pH 5.5 due to the low gel-forming ability. Scanning electron microscopy data showed that a coarse and disorder gel containing clusters of agglomerates was observed at pH 5.0 and pH 5.5, but gradual compact network structure was observed in the gel formed at increasing pH. The glass transition temperature (Tg) of AMP gel formed at pH 5.5 was higher than that of AMP, and the Tg of AMP gel was increased with increasing the pH of gel-forming solution. It was found that the unfolding of tertiary structure of AMP at pH 7.0 was easier than that at pH 5.5 through the result of infrared spectra. We therefore conclude that both the solubility and gel-forming ability of AMP are pH dependent.

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Molecular forces involved in heat-induced pea protein gelation: Effects of various reagents on the rheological properties of salt-extracted pea protein gels

Cited by 201 publications

References 52 publications

Drought or/and Heat-Stress Effects on Seed Filling in Food Crops: Impacts on Functional Biochemistry, Seed Yields, and Nutritional Quality

Drought or/and Heat-Stress Effects on Seed Filling in Food Crops: Impacts on Functional Biochemistry, Seed Yields, and Nutritional Quality

The relationship between breaking force and hydrophobic interactions or disulfide bonds involved in heat‐induced soy protein gels as affected by heating time and temperature

Gelling properties of myofibrillar protein from abalone (Haliotis Discus Hannai Ino) muscle

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