TY - JOUR
T1 - Interactions involved in ovomucin gel-forming properties
T2 - A rheological-biochemical approach
AU - Rabouille, Catherine
AU - Aon, Miguel A.
AU - Thomas, Daniel
PY - 1989/5/1
Y1 - 1989/5/1
N2 - 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 proteinmucin and mucin-mucin interactions. Other bonds susceptible to chymotrypsin treatment and sonication would be involved in the interaction between mucin subunits.
AB - 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 proteinmucin and mucin-mucin interactions. Other bonds susceptible to chymotrypsin treatment and sonication would be involved in the interaction between mucin subunits.
UR - http://www.scopus.com/inward/record.url?scp=0024523005&partnerID=8YFLogxK
U2 - 10.1016/0003-9861(89)90531-6
DO - 10.1016/0003-9861(89)90531-6
M3 - Article
C2 - 2705776
AN - SCOPUS:0024523005
SN - 0003-9861
VL - 270
SP - 495
EP - 503
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 2
ER -