2017
DOI: 10.1016/j.fpsl.2016.10.001
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Raman spectroscopy as a tool to identify modification of whey protein concentrate (WPC) during shelf life

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Cited by 26 publications
(20 citation statements)
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“…Their study characterized the bands corresponding to the main constituents of milk powder and modified milk powder by means of Raman spectroscopy analysis of different samples with different levels of lipids and carbohydrates. Results obtained by Stephani et al (2017) demonstrated the spectroscopic profile modification of whey protein concentrate sample in similar bands to those found in the present work. Their results compared the profiles after six months of storage to the spectroscopic profile of α‐lactose monohydrate crystals and demonstrated the vitreous transition of lactose which was characterized by the spectroscopic profile of crystalline lactose.…”
Section: Resultssupporting
confidence: 91%
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“…Their study characterized the bands corresponding to the main constituents of milk powder and modified milk powder by means of Raman spectroscopy analysis of different samples with different levels of lipids and carbohydrates. Results obtained by Stephani et al (2017) demonstrated the spectroscopic profile modification of whey protein concentrate sample in similar bands to those found in the present work. Their results compared the profiles after six months of storage to the spectroscopic profile of α‐lactose monohydrate crystals and demonstrated the vitreous transition of lactose which was characterized by the spectroscopic profile of crystalline lactose.…”
Section: Resultssupporting
confidence: 91%
“…The main differences are found in the 2900 cm −1 region and can be attributed to the C–H bond stretch. Changes were noted in the regions of 1125 cm −1 and 1054 cm −1 involving the modes [ν (C–O) + ν (C–C) + δ (C–O–H)], and also in the 477 cm −1 region involving [δ (C–C–C) + Ƭ (C–H)] (Stephani et al 2017). Spectral changes in the same regions were attributed to lactose in the work of Almeida et al (2012).…”
Section: Resultsmentioning
confidence: 99%
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“…It is well known (Jung, Czarnik-Matusewicz, & Ozaki, 2000) that the existence of a secondary protein structure can be analysed in the amide I and amide III regions, since the frequency dependence of these bands depends strongly on the protein state, environment and the intermolecular interactions. The main intense peaks in the amide I and II regions are as follows: peak 1 at 1669 cm −1 corresponding to the ʋ (C]O) from amide I and ʋ(C]C); peak 2 at ≈1455 cm −1 that corresponds to δ(CH 2 ); peak 3 at ≈1327 cm −1 corresponding to amide III (α-helix structure), ʋ(C-O) and δ(C-H); and the peak 4 at ≈1245 cm −1 that was assigned to β-sheet structure of the protein (Blanpain-Avet et al, 2012;Stephani et al, 2017). In addition, it is also seen the peak 5 at ≈1008 cm −1 which is attributed to C-CH 3 bonds.…”
Section: Spectroscopic Analysis Of the Dried Nanocapsulesmentioning
confidence: 99%
“…Other studies using MIR reported moderate accuracy for the prediction of macroelements in bovine milk (R 2 CV-0.42-0.71) [17] and high accuracy for the prediction of milk protein composition (R 2 CV-0.59-1) [18]. Raman spectroscopy (RS) has also been reported for prediction of nutritional parameters (fat, protein, energetic values, and carbohydrates) in INF and milk powder [19][20][21][22], milk fat or whey in liquid milk [23] and melamine adulterants in liquid and powdered milk [24][25][26]. A few publications have studied the use of RS to detect mineral contents in dairy products.…”
Section: Introductionmentioning
confidence: 99%