2021
DOI: 10.1007/s11694-021-01151-x
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Modification of pea protein isolate functionality by freeze–thaw cycling

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Cited by 10 publications
(4 citation statements)
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“…Moreover, constant exposure of hydrophobic groups weakens the binding effect with water molecules and results in reduced solubility. Similarly, the solubility of pea proteins also showed a significant reduction after F-T treatment [5].…”
Section: Functional Propertiesmentioning
confidence: 87%
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“…Moreover, constant exposure of hydrophobic groups weakens the binding effect with water molecules and results in reduced solubility. Similarly, the solubility of pea proteins also showed a significant reduction after F-T treatment [5].…”
Section: Functional Propertiesmentioning
confidence: 87%
“…An increased volume of ice crystals damaged protein structures, causing the formation of reactive oxygen for pro-oxidative components and resulting in increased carbonyl content in proteins [18]. However, the decrease in the rate of carbonyl formation following repeated F-T cycles (3)(4)(5) was probably because of the more compact overall structure CSPI, which was not easy to oxidize.…”
Section: Carbonyl Contentmentioning
confidence: 99%
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“…Nowadays, many other innovative processes are being investigated to try to improve plant-based proteins’ physicochemical properties, such as partial hydrolysis, ohmic heating and freeze-thaw cycle, which are capable of modifying proteins’ structure and intermolecular forces [ 114 , 115 , 116 ]. However, currently, little is known about these modifications when milk and plant proteins are both present in the same medium.…”
Section: Possible Approaches To Improve Dairy-plant Proteins Interact...mentioning
confidence: 99%