2022
DOI: 10.1016/j.cis.2022.102725
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Sunflower protein isolates-composition, extraction and functional properties

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Cited by 51 publications
(14 citation statements)
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“…In terms of foaming stability, as seen in Table 4 , the foams had high stability of over 96% at all concentrations studied except the foams of AOB protein isolates prepared at 1% w / v . The foaming stability of AOB was higher than values reported in the literature for other seed proteins, such as sunflower protein isolates (36%) and local beans of Turkey (81%) [ 31 , 56 ]. Generally, the results indicate that the interfacial film formed by AOB and soy protein isolates possesses desirable characteristics such as having suitable mechanical strength as well as being impermeable and flexible.…”
Section: Resultsmentioning
confidence: 63%
“…In terms of foaming stability, as seen in Table 4 , the foams had high stability of over 96% at all concentrations studied except the foams of AOB protein isolates prepared at 1% w / v . The foaming stability of AOB was higher than values reported in the literature for other seed proteins, such as sunflower protein isolates (36%) and local beans of Turkey (81%) [ 31 , 56 ]. Generally, the results indicate that the interfacial film formed by AOB and soy protein isolates possesses desirable characteristics such as having suitable mechanical strength as well as being impermeable and flexible.…”
Section: Resultsmentioning
confidence: 63%
“…Soy and pea protein presents a great capacity for binding water and fat, in addition to emulsifying properties [ 15 , 17 , 35 ]. Sunflower protein, in the same way, has shown excellent functional properties, especially fat absorption, emulsifying, and foaming ability [ 22 , 23 , 25 ]. 11S globulins, the main fraction in these proteins, are recognized as good emulsifiers [ 24 ].…”
Section: Resultsmentioning
confidence: 99%
“…Among oilseed proteins, sunflower protein has attracted interest due to its wide availability, minimal anti-nutritive compounds, and low cost [ 22 ]. Sunflower has two main protein types: water-soluble albumins (2S) and salt-soluble globulins (helianthinin, 11S).…”
Section: Introductionmentioning
confidence: 99%
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“…The formation of gels from dietary proteins, particularly globular proteins, occurs when these proteins are denatured by heating in an aqueous solution and the interaction between the protein and solvent reaches a balance [91]. Globulins exhibit the ability to dissociate and re-associate during heating, leading to the production of different gels with varying characteristics [92]. Partially unfolded proteins can also transform into gels by forming crosslinked networks of uncoiled polypeptide fragments.…”
Section: Gelling Propertiesmentioning
confidence: 99%