2022
DOI: 10.1016/j.foodchem.2022.133031
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Effects of heat treatment and pH on the physicochemical and emulsifying properties of coconut (Cocos nucifera L.) globulins

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Cited by 37 publications
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“…A brief description of the modification methods and the mechanisms of proteins associated with emulsifying functionalities is shown in Figure 2a. The exposure of hydrophobic groups and disulfide aggregation induced by heat treatments also contribute to the enhanced emulsifying performance of proteins (Ma et al., 2022). Previous reports have suggested that the formation of nondisulfide covalent bonds between absorbed proteins induced by malondialdehyde (MDA) contributed to the formation of cold‐set emulsion gels with enhanced quality (Figure 2b) (F. Zhou et al., 2015).…”
Section: Factorsmentioning
confidence: 99%
“…A brief description of the modification methods and the mechanisms of proteins associated with emulsifying functionalities is shown in Figure 2a. The exposure of hydrophobic groups and disulfide aggregation induced by heat treatments also contribute to the enhanced emulsifying performance of proteins (Ma et al., 2022). Previous reports have suggested that the formation of nondisulfide covalent bonds between absorbed proteins induced by malondialdehyde (MDA) contributed to the formation of cold‐set emulsion gels with enhanced quality (Figure 2b) (F. Zhou et al., 2015).…”
Section: Factorsmentioning
confidence: 99%