2011
DOI: 10.1016/j.foodres.2011.09.019
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Study on the rheological properties of heat-induced whey protein isolate–dextran conjugate gel

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Cited by 107 publications
(63 citation statements)
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“…The DG of the CPH‐NOCC conjugates after 48 hr determined by OPA was 53.3%, which shows that the free amino groups of the CPH decreased by a large margin under the condition of dry heat reaction. In Sun's study (Sun et al., ), the content of the free amino group was markedly decreased by around 35.9% in the whey protein isolate–dextran conjugate through the Maillard reaction applied with the dry heating means. These results show that the CPH could be easier to undergo the Maillard reaction than the whey protein isolate under dry heating conditions.…”
Section: Conclusion and Discussionmentioning
confidence: 99%
“…The DG of the CPH‐NOCC conjugates after 48 hr determined by OPA was 53.3%, which shows that the free amino groups of the CPH decreased by a large margin under the condition of dry heat reaction. In Sun's study (Sun et al., ), the content of the free amino group was markedly decreased by around 35.9% in the whey protein isolate–dextran conjugate through the Maillard reaction applied with the dry heating means. These results show that the CPH could be easier to undergo the Maillard reaction than the whey protein isolate under dry heating conditions.…”
Section: Conclusion and Discussionmentioning
confidence: 99%
“…Browning intensity was measured by the absorbance at 420 nm and often used as an indicator of the Maillard reaction progress (Sun et al 2011), which symbolized an advanced stage of the Maillard reaction. Figure 2 shows the absorbance at 420 nm of SPI and SPI/ sugar MRPs with and without ultrasonic pretreatment.…”
Section: Browning Intensitymentioning
confidence: 99%
“…Maillard reactions, usually occurring in thermal process of foods, are considered to be a promising approach for protein modification (Akhtar & Dickinson, 2003;Sun et al, 2011). It has been well established that the covalent attachment of polysaccharide chains to proteins could lead to great improvements in functional properties of proteins, including solubility, thermal stability, emulsification ability and foaming property (Evans, Ratcliffe, & Williams, 2013;Liu, Zhao, Zhao, Ren, & Yang, 2012;Xu, Wang, Jiang, Yuan, & Gao, 2012).…”
Section: Introductionmentioning
confidence: 99%