2018
DOI: 10.1016/j.foodres.2018.03.015
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The effect of carrageenan on the acid-induced aggregation and gelation conditions of quinoa proteins

Abstract: The effect of carrageenan on the acid-induced aggregation and gelation conditions of quinoa proteins

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Cited by 19 publications
(11 citation statements)
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“…The minimal amount of dispersed sample required for gel formation was significantly different between both CPI ( P = 0.008). Results obtained (Table S1) are in the same range as those reported for the acid‐induced gelation of whey proteins (Alting et al ., 2000) but smaller than those required for quinoa protein isolates (Montellano Duran et al ., 2018). By contrast, a greater amount of sample was required for thermal induced gels of honey bee brood soluble proteins (Mishyna et al ., 2019), high‐pressure induced gels from β‐lactoglobulin (Li et al ., 2018) or gels obtained by transglutaminase crosslinking of pea albumin and globulins (Djoullah et al ., 2015).…”
Section: Resultsmentioning
confidence: 99%
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“…The minimal amount of dispersed sample required for gel formation was significantly different between both CPI ( P = 0.008). Results obtained (Table S1) are in the same range as those reported for the acid‐induced gelation of whey proteins (Alting et al ., 2000) but smaller than those required for quinoa protein isolates (Montellano Duran et al ., 2018). By contrast, a greater amount of sample was required for thermal induced gels of honey bee brood soluble proteins (Mishyna et al ., 2019), high‐pressure induced gels from β‐lactoglobulin (Li et al ., 2018) or gels obtained by transglutaminase crosslinking of pea albumin and globulins (Djoullah et al ., 2015).…”
Section: Resultsmentioning
confidence: 99%
“…For CPI12, the β value reached a minimum at pH = 4.6, after which it increased and remained nearly constant. This behaviour has already been reported for the acid‐induced aggregation of sodium caseinate (Hidalgo et al ., 2015) and quinoa proteins (Montellano Duran et al ., 2018), suggesting the formation of larger protein aggregates by the association among particles due to the lack of electrostatic repulsion. Since CPI10 showed no further increase in the β value, soluble aggregates formed from this sample were not able to restructure to form larger aggregates in the period of time analysed.…”
Section: Resultsmentioning
confidence: 99%
“…Last but not least, both foaming and interfacial rheology can easily be extended to other pH-sensitive polymers or proteins [ 46 , 47 , 48 , 49 , 50 ] (and potentially to other water-soluble gas components). We therefore believe that our findings may inspire much wider activities pertaining to gas-initiated material fabrication.…”
Section: Discussionmentioning
confidence: 99%
“…Another change in QPI techno‐functional properties was observed when carrageenan (carr) was added to solutions containing QPI. According to Duran et al ., 72 carr improved the solubility of QPI near the isoelectric point (from pH 2.5 to 5.5), whereas the opposite occurred at the pH where the protein is most soluble. In addition, carr can induce minor conformational changes in QPI and can also protect these proteins from thermal denaturation.…”
Section: Modifications Of Pseudocereal Proteinsmentioning
confidence: 99%