Interfacial Properties of Diglycerol Esters and Caseinate Mixed Films at the Air−Water Interface

2007 ◽  
Vol 111 (12) ◽  
pp. 4790-4799 ◽  
Author(s):  
José M. Álvarez Gómez ◽  
Juan M. Rodríguez Patino
2006 ◽  
Vol 40 (34) ◽  
pp. 6606-6614 ◽  
Author(s):  
Jessica B. Gilman ◽  
Heikki Tervahattu ◽  
Veronica Vaida

1986 ◽  
Vol 19 (10) ◽  
pp. 2606-2612 ◽  
Author(s):  
Masami Kawaguchi ◽  
Masahito Sano ◽  
Yen Lane Chen ◽  
George Zografi ◽  
Hyuk Yu

1999 ◽  
Vol 47 (12) ◽  
pp. 4998-5008 ◽  
Author(s):  
Juan M. Rodríguez Patino ◽  
Cecilio Carrera Sánchez ◽  
M. Rosario Rodríguez Niño

2002 ◽  
Vol 41 (13) ◽  
pp. 3169-3178 ◽  
Author(s):  
Juan M. Rodríguez Patino ◽  
Ma. Rosario Rodríguez Niño ◽  
Cecilio Carrera Sánchez

2006 ◽  
Vol 398 (3) ◽  
pp. 569-576 ◽  
Author(s):  
Silvia Belem-Gonçalves ◽  
Pascale Tsan ◽  
Jean-Marc Lancelin ◽  
Tito L. M. Alves ◽  
Vera M. Salim ◽  
...  

The interfacial properties of bovine testicular hyaluronidase were investigated by demonstrating the association of hyaluronidase activity with membranes prepared from bovine testis. Protein adsorption to the air/water interface was investigated using surface pressure-area isotherms. In whichever way the interfacial films were obtained (protein injection or deposition), the hyaluronidase exhibited a significant affinity for the air/water interface. The isotherm obtained 180 min after protein injection into a pH 5.3 subphase was similar to the isotherm obtained after spreading the same amount of protein onto the same subphase, indicating that bovine testicular hyaluronidase molecules adopted a similar arrangement and/or conformation at the interface. Increasing the subphase pH from 5.3 to 8 resulted in changes of the protein isotherms. These modifications, which could correspond to the small pH-induced conformational changes observed by Fourier-transform IR spectroscopy, were discussed in relation to the pH influence on the hyaluronidase activity. Adding hyaluronic acid, the enzyme substrate, to the subphase tested the stability of the interfacial properties of hyaluronidase. The presence of hyaluronic acid in the subphase did not modify the protein adsorption and allowed substrate binding to a preformed film of hyaluronidase at pH 5.3, the optimal pH for the enzyme activity. Such effects of hyaluronic acid were not observed when the subphase was constituted of pure water, a medium where the enzyme activity was negligible. These influences of hyaluronic acid were discussed in relation to the modelled structure of bovine testis hyaluronidase where a hydrophobic region was proposed to be opposite of the catalytic site.


2013 ◽  
Vol 117 (42) ◽  
pp. 21838-21848 ◽  
Author(s):  
Luisa Ariza-Carmona ◽  
María T. Martín-Romero ◽  
Juan J. Giner-Casares ◽  
Marta Pérez-Morales ◽  
Luis Camacho

2005 ◽  
Vol 19 (3) ◽  
pp. 395-405 ◽  
Author(s):  
C SANCHEZ ◽  
M ROSARIORODRIGUEZNINO ◽  
J PATINO

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