Potato pectin contains some proteinaceous components and exhibits emulsifying and emulsion stabilizing abilities. The objective of this study was to elucidate the effect of the pectin moiety of pectin-protein conjugate present in pectic extracts from potato tubers on their interfacial properties. Potato pectin was extracted from highly purified cell wall materials to avoid the contamination of unconjugated proteins. Abilities of the potato pectin to adsorb to graphite surfaces and to resist surfactant-induced competitive displacement from the air-water interface were investigated using atomic force microscopy. The pectin moiety of the potato pectin was capable of adsorbing to graphite surfaces even after alkali treatment. Furthermore, the potato pectin exhibited enhanced resistance to surfactant-induced competitive displacement from the interface as a result of the formation of network structures of self-assembled pectin moieties at the interface. The present results suggest the importance of the pectin moiety on interfacial properties of potato pectin.
This article was published in the following journal.
Name: Journal of agricultural and food chemistry
ISSN: 1520-5118
Pages:
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Pulmonary Surfactant-associated Protein C
A pulmonary surfactant associated protein that plays a role in alveolar stability by lowering the surface tension at the air-liquid interface. It is a membrane-bound protein that constitutes 1-2% of the pulmonary surfactant mass. Pulmonary surfactant-associated protein C is one of the most hydrophobic peptides yet isolated and contains an alpha-helical domain with a central poly-valine segment that binds to phospholipid bilayers.
Pulmonary Surfactant-associated Protein B
A pulmonary surfactant associated-protein that plays an essential role in alveolar stability by lowering the surface tension at the air-liquid interface. Inherited deficiency of pulmonary surfactant-associated protein B is one cause of RESPIRATORY DISTRESS SYNDROME, NEWBORN.
Pulmonary Surfactant-associated Protein D
An abundant pulmonary surfactant-associated protein that binds to a variety of lung pathogens and enhances their opsinization and killing by phagocytic cells. Surfactant protein D contains a N-terminal collagen-like domain and a C-terminal lectin domain that are characteristic of members of the collectin family of proteins.
Pulmonary Surfactant-associated Protein A
An abundant pulmonary surfactant-associated protein that binds to a variety of lung pathogens, resulting in their opsinization. It also stimulates MACROPHAGES to undergo PHAGOCYTOSIS of microorganisms. Surfactant protein A contains a N-terminal collagen-like domain and a C-terminal lectin domain that are characteristic of members of the collectin family of proteins.
Binding, Competitive
The interaction of two or more substrates or ligands with the same binding site. The displacement of one by the other is used in quantitative and selective affinity measurements.
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