A front-face fluorescence spectroscopy probe was installed in the wall of a laboratory-scale cheese vat. Excitation and emission filters were chosen for the selective detection of vitamin A, tryptophan, and riboflavin fluorescence. The evolution of the fluorescence of each fluorophore during milk coagulation and syneresis was monitored to determine if they had the potential to act as intrinsic tracers of syneresis and also coagulation. The fluorescence profiles for 2 of the fluorophores during coagulation could be divided into 3 sections relating to enzymatic hydrolysis of κ-casein, aggregation of casein micelles, and crosslinking. A parameter relating to coagulation kinetics was derived from the tryptophan and riboflavin profiles but this was not possible for the vitamin A response. The study also indicated that tryptophan and riboflavin may act as tracer molecules for syneresis, but this was not shown for vitamin A. The evolution of tryptophan and riboflavin fluorescence during syneresis followed a first-order reaction and had strong relationships with curd moisture and whey total solids content (r=0.86-0.96). Simple 1- and 2-parameter models were developed to predict curd moisture content, curd yield, and whey total solids using parameters derived from the sensor profiles (standard error of prediction=0.0005-0.394%; R 2=0.963-0.999). The results of this study highlight the potential of tryptophan and riboflavin to act as intrinsic tracer molecules for noninvasive inline monitoring of milk coagulation and curd syneresis. Further work is required to validate these findings under a wider range of processing conditions.
|Original language||American English|
|Number of pages||9|
|Journal||Journal of Dairy Science|
|Publication status||Published - Nov 2011|
- Fluorescence spectroscopy