Comparative study of deteriorative changes in the ageing of milk powder

Yazdanpanah, Nima; Langrish, T.A.G.

doi:10.1016/j.jfoodeng.2012.07.026

Cited by 34 publications

(8 citation statements)

References 53 publications

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“…2018) have been reported previously. The detection of storage‐induced alteration in dairy ingredients, for example lactose crystalisation, has also been reported previously (Yazdanpanah and Langrish 2013; Stephani et al . 2017).…”

Section: Introductionsupporting

confidence: 76%

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Raman spectra of micellar casein powders prepared with wet blending of glycomacropeptide and micellar casein concentrate

Panthi

Shibu

Ochalski

et al. 2022

Int J of Dairy Tech

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Understanding the molecular properties and interactions of components within high-protein dairy powders is important in predicting rehydration performance. Raman spectroscopy was used to generate molecular information which provided insights into interactions between caseins in micellar casein concentrate (MCC) powder formulated with varying proportions of glycomacropeptide (GMP). The Raman bands showed intense peaks at 1446 to 1476 cm À1 (due to CH 2 vibration) and 1653 to 1668 cm À1 (due to C=O of Amide I and C=C bond) in MCC powder samples blended with GMP. Enhanced rehydration characteristics of MCC powder containing GMP matched with these differences in Raman peak intensity.

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Section: Introductionsupporting

confidence: 76%

“…(2020); [2] Rodrigues Junior et al . (2016); [3] Yazdanpanah and Langrish (2013); [4] McGoverin et al . (2010); [5] Wang et al .…”

Section: Introductionmentioning

confidence: 99%

Raman spectra of micellar casein powders prepared with wet blending of glycomacropeptide and micellar casein concentrate

Panthi

Shibu

Ochalski

et al. 2022

Int J of Dairy Tech

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show abstract

“…The FSD curves were fitted with Gaussian shape and were analyzed by local least-squares (LLS) algorithm. Percentage of secondary structures (α-helix, β-sheets, β-turns, and random coils) was estimated using eq , secondary structure (%) = italicA ind / italicA total × 100 where A ind = sum of area of individual secondary structure in amide I band and A total = sum of area of total secondary structure in amide I band.…”

Section: Methodsmentioning

confidence: 99%

Drying and Denaturation Characteristics of α-Lactalbumin, β-Lactoglobulin, and Bovine Serum Albumin in a Convective Drying Process

Hanson

Aldred

et al. 2014

J. Agric. Food Chem.

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Drying and denaturation kinetics of aqueous droplets of α-lactalbumin (α-lac), β-lactoglobulin (β-lg), and bovine serum albumin (BSA) were measured in a convective drying environment. Single droplets having an initial droplet diameter of 2 ± 0.1 mm and containing 10% (w/v) protein concentration were dried using conditioned air (65 and 80 °C, 2-3% RH, 0.5 m/s velocity) for 600 s. The denaturation of these proteins was measured by using reversed-phase HPLC. At the end of 600 s of drying 13.3 and 19.4% α-lac was found to be lost due to denaturation at 65 and 80 °C, respectively. Up to 31.0% of β-lg was found to be denatured, whereas BSA was not found to be significantly (p > 0.05) denatured in these drying conditions. The formation and strength of skin and the associated morphological features were found to be linked with the degree of denaturation of these proteins. The secondary structure of these proteins was significantly (p < 0.05) affected and altered by the drying stresses. The β-sheet and random coil contents were increased in α-lac by 6.5 and 4.0%, respectively, whereas the α-helix and β-turn contents decreased by 5.5 and 5.0%, respectively. The β-sheet and random coil contents in β-lg were increased by 7.5 and 2.0%, respectively, whereas the α-helix and β-turn contents decreased by 3.5 and 6.0%, respectively. In the case of BSA the β-sheet, α-helix, and random coil contents were found to increase, whereas the β-turn content decreased.

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“…The available lysine content of WP–Lac model was lower than that of CN–WP–Lac and CN–Lac models in a w 0.33 and 0.43, illustrating the pronounced glycation and LC in WP–Lac model. However, due to the increase of a w , the interaction between water and protein was enhanced on the protein surface, and the swelling and degradation of protein advanced structures led to the exposure of the side‐chain groups, which further accelerated the protein denaturation (Haque et al., 2010; Yazdanpanah & Langrish, 2013).…”

Section: Resultsmentioning

confidence: 99%

Lactose crystallization and Maillard reaction in simulated milk powder based on the change in water activity

Yan

Liu

2022

Journal of Food Science

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Maillard reaction (MR) and lactose crystallization (LC) are important reactions in the storage of milk powder. In this study, three models with different proteins based on skimmed milk powder were established to investigate the relationship between MR and LC at different water activities (a w ). Moisture sorption isotherm, glass transition temperature (T g ), and glycation products were evaluated, and the protein structure and lactose crystallinity were determined. The results indicated that MR product content, browning, and LC subsequently enhanced with the increase in a w . The T g value dropped lower than 0 at a w 0.43 in whey protein isolate-lactose (WP-Lac) model and at a w 0.54 in casein-whey protein isolate-lactose (CN-WP-Lac) model and casein-lactose (CN-Lac) model.The crystallinity of α-lactose monohydrate and anhydrous β-lactose in WP-Lac model was more significant than CN-WP-Lac and CN-Lac models (p < 0.05).The molecular band of whey protein gradually blurred in the Sodium dodecylsulfate polyacrylamide gel electrophoresis image, and the content of α-helix of WP-Lac model increased by 45.15% from a w 0.33 to 0.53 (p < 0.05), while that of CN-WP-Lac model increased by only 3.95% (p < 0.05). With the increase in a w , WP-Lac model formed more browning and crystallization products than CN-WP-Lac model, indicating that the presence of micelle macromolecules and the interaction between casein and whey proteins limited the browning and crystallization in CN-WP-Lac model. Practical Application: Maillard reaction and lactose crystallization are important reactions in the storage of milk powder, and the result will provide theoretical guidance for the development of milk powder in the food industry.

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Comparative study of deteriorative changes in the ageing of milk powder

Cited by 34 publications

References 53 publications

Raman spectra of micellar casein powders prepared with wet blending of glycomacropeptide and micellar casein concentrate

Raman spectra of micellar casein powders prepared with wet blending of glycomacropeptide and micellar casein concentrate

Drying and Denaturation Characteristics of α-Lactalbumin, β-Lactoglobulin, and Bovine Serum Albumin in a Convective Drying Process

Lactose crystallization and Maillard reaction in simulated milk powder based on the change in water activity

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