2021
DOI: 10.1016/j.tifs.2021.03.001
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Hydrophobins and chaplins: Novel bio-surfactants for food dispersions a review

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Cited by 14 publications
(14 citation statements)
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“…Hydrophobins are globular proteins, with low molecular weight (< 20 kDa) and primary sequence of about 100–150 amino acids and have 8 cysteine residues that form 4 intramolecular disulfide bonds, stabilizing their tertiary structure and promoting surfactant and emulsifying activity [ 137 , 138 ]. Hydrophobins are classified into two classes (I and II) according to their assembly characteristics at hydrophobic–hydrophilic interfaces, solubility and hydropathy.…”
Section: Structural Classes Properties and Applicationsmentioning
confidence: 99%
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“…Hydrophobins are globular proteins, with low molecular weight (< 20 kDa) and primary sequence of about 100–150 amino acids and have 8 cysteine residues that form 4 intramolecular disulfide bonds, stabilizing their tertiary structure and promoting surfactant and emulsifying activity [ 137 , 138 ]. Hydrophobins are classified into two classes (I and II) according to their assembly characteristics at hydrophobic–hydrophilic interfaces, solubility and hydropathy.…”
Section: Structural Classes Properties and Applicationsmentioning
confidence: 99%
“…Class I hydrophobins form structures similar to amyloid fibrils, termed rodlet layers with a β-sheet conformation and are soluble only in strong acids, on the other hand, class II hydrophobins form regular crystalline structures with a random spiral conformation and can be easily dissolved with organic solvents or detergents [ 139 , 140 ]. Some of these proteins may exhibit glycosylation [ 137 , 139 ]. Although some hydrophobins can form oligomers as a strategy to increase their solubility in solution, others remain monomeric even at high concentrations [ 13 , 141 ].…”
Section: Structural Classes Properties and Applicationsmentioning
confidence: 99%
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