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Volumn 430, Issue , 2014, Pages 69-77
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Improved emulsion stability by succinylation of patatin is caused by partial unfolding rather than charge effects
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Author keywords
DLVO theory; Electrostatic interaction; Flocculation; Hydrophobicity; Interfacial properties; Modification; Molecular properties; Oil in water; Protein
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Indexed keywords
ADSORPTION;
COULOMB INTERACTIONS;
EMULSIFICATION;
EMULSIONS;
FLOCCULATION;
HYDROPHOBICITY;
IONIC STRENGTH;
PHASE INTERFACES;
STABILITY;
DLVO THEORY;
INTERFACIAL PROPERTY;
MODIFICATION;
MOLECULAR PROPERTIES;
OIL-IN-WATER;
PROTEINS;
OIL;
PATATIN;
PROTEIN;
UNCLASSIFIED DRUG;
WATER;
CARBOXYLIC ESTER HYDROLASES;
EMULSIONS;
PATATIN PROTEIN, SOLANUM TUBEROSUM;
PLANT PROTEINS;
SUCCINIC ACID;
ADSORPTION;
AMINO ACID SEQUENCE;
ARTICLE;
EMULSION;
FLOCCULATION;
HYDROPHOBICITY;
IONIC STRENGTH;
PRIORITY JOURNAL;
PROTEIN MODIFICATION;
PROTEIN STABILITY;
PROTEIN STRUCTURE;
PROTEIN UNFOLDING;
SUCCINYLATION;
YOUNG MODULUS;
ZETA POTENTIAL;
CHEMISTRY;
EMULSIONS;
CARBOXYLIC ESTER HYDROLASES;
EMULSIONS;
PLANT PROTEINS;
PROTEIN STABILITY;
PROTEIN UNFOLDING;
SUCCINIC ACID;
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EID: 84902110257
PISSN: 00219797
EISSN: 10957103
Source Type: Journal
DOI: 10.1016/j.jcis.2014.05.019 Document Type: Article |
Times cited : (30)
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References (37)
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