Fontanari, G. G.Batistuti, J. P.Bannach, G.Pastre, I. A.Ionashiro, E. Y.Fertonani, F. L.2014-05-202014-05-202006-03-01Journal of Thermal Analysis and Calorimetry. Dordrecht: Springer, v. 83, n. 3, p. 709-713, 2006.1388-6150http://hdl.handle.net/11449/7736The guava seed protein isolate ( PI) was obtained from the protein precipitation belonging to the class of the gluteline (Ip 4.5). The conditions for the preparation of the PI were determined by both the solubility curve and simultaneous thermogravimetry-differential thermal analysis (TG-DTA): pH 11.5, absence of NaCl and whiteners and T=( 25 +/- 3) degrees C. Under these conditions a yield of 77.0 +/- 0.4%, protein content of 94.2 +/- 0.3, ashes 0.50 +/- 0.05% and thermal stability, T= 200 degrees C, were obtained. The TG-DTA curves and the PI emulsification capacity study showed the presence of hydrophobic microdomains at pH 11.5 and 3.0 suggesting a random coil protein conformation and, to pH 10.0, an open protein conformation. The capacity of emulsification (CE), in the absence of NaCl, was verified for: 1 - pH 3.0 and 8.5, using the IP extracted at pH 10.0 and 11.5, CE >= 343 +/- 5 g of emulsified oil/g of protein; 2 - pH 6.60 just for the PI obtained at pH 11.5, CE >= 140 +/- 8 g of emulsified oil/g of protein.709-713engglutelinsguava seedprotein isolateTG-DTATG/DTGArtigo10.1007/s10973-005-6802-9WOS:000236616400032Acesso restrito2453255846842174