The effects of the composition of a fat globule surface in reconstituted milks on the properties of rennet-induced coagulums were studied by rheological measurements and by front-face fluorescence spectroscopy in combination with a multivariate statistical method to investigate, at a molecular level, the evolution of the structure during the milk coagulation process. Reconstituted milks used in this study were prepared from different fat-in-water emulsions stabilized by whole skim-milk proteins, beta -casein, or beta -lactoglobulin. Coagulation of milk reconstituted with natural fat globules was also investigated. The study showed that the fat droplet/water interface influences the theological properties (G ' modulus) of the reconstituted milks during the coagulation process. The tryptophan fluorescence emission spectra of proteins were recorded during the kinetics of coagulation. The results of the principal component analysis performed on the spectral data showed a discrimination in the different systems investigated. It was shown that the fluorescence properties of protein tryptophans and, consequently, the structures of the protein networks were different for the investigated systems. The development of fluorescence transfer between protein tryptophans and fat-globule vitamin A during the coagulation kinetics agreed with the interactions between the protein network and fat globules.