Interactions involved in ovomucin gel-forming properties: a rheological-biochemical approach.
Different kinds of interactions involved in the properties of ovomucin gel formation from hen egg white were studied by combining physical and biochemical methods. A decrease in viscosity of the ovomucin gel was observed when it was subjected to chymotrypsin or sonication treatment. The viscosity decrease correlated with a change from non-Newtonian to Newtonian properties of the ovomucin gel. By treatment of the gel with either 5 M guanidinium HCl, 6 M urea, or 5% sodium dodecyl sulfate a change from non-Newtonian to Newtonian properties was also obtained. Although high ionic strength or sialic acid liberation from the ovomucin gel by neuraminidase treatment provoked a decrease in viscosity, it was not followed by a change in non-Newtonian properties. The results obtained suggest that different noncovalent interactions might be involved in gel formation. Electrostatic interactions (partially destroyed by sialic acid removal or 2 M NaCl) and hydrophobic interactions might be responsible for protein-mucin and mucin-mucin interactions. Other bonds susceptible to chymotrypsin treatment and sonication would be involved in the interaction between mucin subunits.
Rabouille
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Laboratoire de Technologie Enzymatique, UA 523 du CNRS, Université de Compiègne, France.
Aon
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Thomas
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D000818:Animals; D002645:Chickens; D002918:Chymotrypsin; D004347:Drug Interactions; D004527:Egg Proteins; D005782:Gels; D006868:Hydrolysis; D007700:Kinetics; D009439:Neuraminidase; D009994:Osmolar Concentration; D010059:Ovomucin; D012212:Rheology; D012995:Solubility; D013010:Sonication; D014783:Viscosity
D004527:Egg Proteins; D005782:Gels; D010059:Ovomucin; D009439:Neuraminidase; D002918:Chymotrypsin