1998
DOI: 10.1006/jcis.1997.5376
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Emulsification and Foaming Properties of Hydrophobically Modified Gelatin

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Cited by 59 publications
(27 citation statements)
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“…Grafting of C 10 or C 12 alkyl chains to peptides resulted in molecules more effective than C 14 in decreasing the surface tension, which is in agreement with the foaming properties previously observed for these acylated peptides [6]. The influence of the hydrophobic chain of a molecule on the surface tension has been evaluated in alkylglycosides [3,4] and in proteins [9,10]. In general, within a series of proteins or sugars, the length increase of the hydrophobic chain results in lower surface tension values.…”
Section: Surface Tension Measurements At Air-water Interfacesupporting
confidence: 79%
See 1 more Smart Citation
“…Grafting of C 10 or C 12 alkyl chains to peptides resulted in molecules more effective than C 14 in decreasing the surface tension, which is in agreement with the foaming properties previously observed for these acylated peptides [6]. The influence of the hydrophobic chain of a molecule on the surface tension has been evaluated in alkylglycosides [3,4] and in proteins [9,10]. In general, within a series of proteins or sugars, the length increase of the hydrophobic chain results in lower surface tension values.…”
Section: Surface Tension Measurements At Air-water Interfacesupporting
confidence: 79%
“…It could be claimed that there was a decrease of the droplet size and an increase of their stability when increasing the length of the alkyl chain. This type of relationship has been demonstrated for lipophilized proteins and attributed to an enhancement of the affinity toward the oil-water interface when the hydrophobicity increases [9].…”
Section: Droplet Size Of Emulsionsmentioning
confidence: 92%
“…Structural studies of proteins adsorbed onto oil droplets are limited by the heterogeneity and polydispersity of emulsion systems. However, the amount of protein adsorbed to the oil surface can be measured by separating emulsion droplets from the aqueous phase and analyzing the aqueous phase for protein content (12)(13)(14). This technique enabled Fang and Dalgleish (12) to determine surface coverages for casein-stabilized emulsions.…”
Section: Introductionmentioning
confidence: 99%
“…Yet, due to their hydrophilic features, they are not such good barriers to water vapor 2, 4–11. As a consequence, several strategies have been proposed to improve the moisture resistance of gelatin–based films including chemical, physical, and enzymatic crosslinking6–8, 12–15 and compositing with other moisture resistant polymers and biopolymers 9, 16–20. Another way of overcoming such drawback is by creating multilayer structures.…”
Section: Introductionmentioning
confidence: 99%