2018
DOI: 10.1016/j.foodhyd.2018.04.032
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Surface properties of Acacia senegal vs Acacia seyal films and impact on specific functionalities

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Cited by 25 publications
(11 citation statements)
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“…According to Aphibanthammakit, Nigen, Gaucel, Sanchez, and Chalier (2018) films made from biopolymers have bipolar surface properties, i.e. the total surface energy of the films depends on the energy provided by the polar and dispersive (no polar) components of the material surface.…”
Section: Surface Energy Measurements Water Contact Angle (Wca) and Scanning Electron Microscopy (Sem) Of The Thermo-compressed Surfacesmentioning
confidence: 99%
“…According to Aphibanthammakit, Nigen, Gaucel, Sanchez, and Chalier (2018) films made from biopolymers have bipolar surface properties, i.e. the total surface energy of the films depends on the energy provided by the polar and dispersive (no polar) components of the material surface.…”
Section: Surface Energy Measurements Water Contact Angle (Wca) and Scanning Electron Microscopy (Sem) Of The Thermo-compressed Surfacesmentioning
confidence: 99%
“…According to Aphibanthammakit et al. [ 49 ] films made from biopolymers have bipolar surface properties, i.e., the total surface energy of the films is a function of the energy provided by the polar and dispersive (no polar) components of the material surface. This is in line with the results obtained here: both the polar and dispersive components contributed to the total surface energy for all the film systems ( Figure ).…”
Section: Resultsmentioning
confidence: 99%
“…The filmogenic solutions have been prepared by dispersing the biopolymer at a concentration enabling its complete dispersion in a suitable solvent. Being easy to solubilize in water, SPI was simply dispersed in water under heating (30 min at 50°C) to break the non-covalent bonds (mainly van der Waals interactions) and to favor interaction with water of the polymer chains (Ben Arfa et al, 2007a; Aphibanthammakit et al, 2018). By contrast, WG proteins having a low solubility in water because of a low content of ionized polar amino acids, many hydrophobic interactions between non-polar amino acids and the presence of inter and intra-molecular disulfide bonds stabilizing high molecular weight protein fractions, its dispersion in water required sodium sulfite to reduce disulfide bonds and acetic acid to lower the pH value at 4 (Gastaldi et al, 2007).…”
Section: Resultsmentioning
confidence: 99%