Effect of heat treatment of rennet skim milk induced coagulation on the rheological properties and molecular structure determined by synchronous fluorescence spectroscopy and turbiscan

Rennet‐induced coagulation of raw and heated camel and cow milk gels determined by instrumental techniques: effects of added calcium and phosphate

“…This change could be attributed to the: (1) modification of tryptophan environment due to the exposure of tryptophan to solvent as illustrated by the red shift; 19,32,33 and (2) modification in the protein-protein, protein-water, and/or protein-lipid interactions. 16,17 Similar emission spectra were observed on the gels obtained with control milk samples preheated at 50 and 70 ∘ C and those added with minerals (data not shown).…”

“…Taking into account that the structure of the gel at the molecular level affects the texture of the final product, it would be interesting to control its structure. In this context, fluorescence and infrared methods have been employed to monitor rennet‐induced coagulation of cow milk . However, to the best of our knowledge no papers have been published describing the ability of front‐face fluorescence spectroscopy to monitor rennet‐induced coagulation of camel milk.…”

“…In this context, fluorescence and infrared methods have been employed to monitor rennet-induced coagulation of cow milk. 16 -21 However, to the best of our knowledge no papers have been published describing the ability of front-face fluorescence spectroscopy to monitor rennet-induced coagulation of camel milk. The presence of fluorophores in camel milk makes fluorescence spectroscopy an ideal method to evaluate the molecular changes occurring during rennet-induced coagulation.…”

Milk-clotting properties of plant rennets and their enzymatic, rheological, and sensory role in cheese making: A review

“…As milk ultrafiltration occurs, the effect of this factor on gel rheology was envisaged only in the case of milk gelation by calf rennet. Blecker et al [78] showed that the application of high temperature on milk contributes to the decrease of gel-firming rate during coagulation followed by a reduction in gel viscosity. The values of the maximum gel-firming rate produced by calf chymosin were about 0.0202, 0.0175, and 0.0003 Pa −1 , for fresh raw milk and heat-treated milk at 60°C and 80°C for 20 min, respectively.…”

Laser‐induced volume changes during confocal Raman microscopy of whey‐protein‐stabilized emulsions and their relationship to protein content and particle diameters

“…[13] Common methods for characterization of emulsion stability include particle size analysis (laser diffraction or photon correlation spectroscopy) for measuring coalescence-induced changes in particle size distribution [4] with time, and ultrasonic [14] or turbidimetric analysis of creaming. [15] Of particular relevance to the present study are the techniques aiming to correlate sizes of individual particles to Raman spectra. Raman spectroscopy is known to be suitable for the study of aqueous samples, since water has a weak scattering efficiency.…”