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. 2025 Jul 18:S0022-0302(25)00542-9.
doi: 10.3168/jds.2025-26765. Online ahead of print.

Predicting whey's functional properties through synchronous front-face fluorescence spectroscopy

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Free article

Predicting whey's functional properties through synchronous front-face fluorescence spectroscopy

Paulina Freire et al. J Dairy Sci. .
Free article

Abstract

Whey is widely used across various food industries, and its functional properties are critical for product quality and consumer acceptance. The current study aimed to assess the feasibility of using front-face fluorescence spectroscopy (FFF) as a nondestructive technique to predict the technological functionality of whey, particularly its foaming, gel-forming, and emulsifying capabilities. Heat treatments were applied on reconstituted skim milk enriched with whey protein isolated (80°C with 7 holding times) to induce variability in all the studied functional properties. Then, whey samples were obtained by isoelectric precipitation of caseins from enriched milk. Synchronous FFF of whey was measured at an excitation of 250 to 550 nm (λ0 = 20 nm and Δλ = 10 nm). Excitation and emission wavelengths and maximum intensities were collected for 10 areas. These FFF parameters and their mathematical transformations were used in the maximum R2 procedure of SAS software (version 9.4, SAS Institute Inc.) to select the predictors and obtain the best models, which were cross-validated. Excellent prediction models (R2 > 0.95, ratio of performance deviation [RPD] >4) were obtained for gel-forming and emulsifying properties. However, for foam properties, the obtained models were successful for foam overrun (0.90 ≤ R2 ≤ 0.95, 3 ≤ RPD ≤4) and moderately successful (0.80 ≤ R2 < 0.90, 2.25 ≤ RPD <3) for foam stability. This research demonstrated that FFF spectroscopy has the potential to become a method for assessing whey functional properties, leading to improved industry process control and new products.

Keywords: front-face fluorescence; heat treatment; synchronous fluorescence spectroscopy; whey functionality.

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