2023
DOI: 10.1016/j.cemconcomp.2023.105121
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Effect of proteins on the mineralization, microstructure and mechanical properties of carbonation cured calcium silicate

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Cited by 11 publications
(9 citation statements)
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“…38 In a high-pH solution, the conformational and molecular structure of the proteins change through the breakage of hydrogen, hydrophobic, van der Waals, and disulfide bonds. Compared to other studies, 3,9 it was noticed that the negative surface charge exhibited by the proteins in this study is relatively low. The charge-screening effect due to the presence of Ca 2+ in SPS and the formation of complexes and agglomerates results in a lower negative charge of the proteins.…”
Section: ζ Potentialcontrasting
confidence: 81%
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“…38 In a high-pH solution, the conformational and molecular structure of the proteins change through the breakage of hydrogen, hydrophobic, van der Waals, and disulfide bonds. Compared to other studies, 3,9 it was noticed that the negative surface charge exhibited by the proteins in this study is relatively low. The charge-screening effect due to the presence of Ca 2+ in SPS and the formation of complexes and agglomerates results in a lower negative charge of the proteins.…”
Section: ζ Potentialcontrasting
confidence: 81%
“…These proteins were purchased from commercial vendors. The native molecular structures of whey protein, albumin, NFMP, and SBI are reported to be globular, while CP is reported to have a fibrous structure. The molecular weight and structure of these proteins have been studied in previous investigations. ,, The differences in the characteristics of these proteins and their availability are the reasons for including them in this study. Lignin is a hydrophobic phenolic compound found in biomass and possesses several functional groups including alcohol hydroxyl, phenol hydroxyl, and carboxyl groups capable of reacting with proteins to form protein–lignin complexes, hydrophobic networks, and hydrogen and ionic bonds .…”
Section: Methodsmentioning
confidence: 99%
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