Effect of superfine grinding on the structural and physicochemical properties of whey protein and applications for microparticulated proteins

Sun, Chanchan; Liu, Rui; Wu, Tao; Liang, Bin; Shi, Chunyue; Zhang, Min

doi:10.1007/s10068-015-0212-y

Cited by 49 publications

(26 citation statements)

References 30 publications

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“…The results showed that ball‐milling treatment did not lead to obvious changes of protein bands. This indicated that ball‐milling treatment could not change the primary structure of mussel protein, which was similar to whey protein concentrate and soybean protein isolate (Sun et al ., ; Liu et al ., ). In addition, we speculated that the band of 100 kDa may be paramyosin (Suzuki et al ., ; Wang et al ., ) and the band of 42 kDa is likely to be actin (Patwary, ; Bryant et al ., ; Ma et al ., ) according to findings in scallop and abalone.…”

Section: Resultsmentioning

confidence: 99%

“…Therefore, more BPB had access to bind with the nonpolar part of the protein molecule, and the surface hydrophobicity increased. Similar changes were also demonstrated in soybean protein isolate and whey protein concentrate after ball‐milling treatment (Sun et al ., ; Liu et al ., ).…”

Section: Resultsmentioning

confidence: 99%

“…The powder became denser and more homogeneous. Similar microstructures were observed in ball‐milled soybean protein isolate and whey protein concentrate (Sun et al ., ; Liu et al ., ). The results indicated that high collision, shear force and friction of ball‐milling treatment changed the surface appearance of mussel protein.…”

Section: Resultsmentioning

confidence: 99%

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Effects of ball‐milling treatment on mussel (Mytilus edulis) protein: structure, functional properties and in vitro digestibility

Cha

et al. 2017

Int J of Food Sci Tech

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Summary In this study, the effects of ball‐milling treatment on structural properties and functional properties of mussel protein were investigated. In vitro protein digestibility and free amino acid contents were also evaluated. Ball‐milling treatment did not change the primary structure of mussel protein, but caused changes of secondary structure. The tertiary and quaternary structure also changed. After 20 min of ball‐milling treatment, the whiteness and oil‐binding capability of mussel protein significantly improved from 13.67 to 26.62 and 43.76% to 196.00%, while the protein solubility and water‐holding capability of mussel protein significantly decreased from 74.89% to 53.10% and 215.67% to 90.91%. Ball‐milling treatment increased the in vitro digestibility significantly. These results provide theoretical basis for the utilisation of mussel protein in food industry.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Effects of ball‐milling treatment on mussel (Mytilus edulis) protein: structure, functional properties and in vitro digestibility

Cha

et al. 2017

Int J of Food Sci Tech

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“…Superfine soy flour had higher WHC, solubility, swelling, fat binding, and sensory scores compared with the control (Muttakin and others ). Milling WPC increased its solubility, hydrophobicity, oil binding capacity, and foaming properties, but decreased its WHC (Sun and others ,b). Surface hydrophobicity of acid casein and egg white powder increased as particle size decreased (Hayakawa and others ).…”

Section: Introductionmentioning

confidence: 99%

“…This redistribution of water is a commonly proposed mechanism for time‐dependent texture change (Cho ; Hazen ). Protein powder WHC and surface hydrophobicity are influenced by particle size reduction (Hayakawa and others ; Sun and others ,b). Hydrophobic protein powder particles may slow hydration during HPN bar manufacture, but may also help inhibit moisture migration during storage.…”

Section: Introductionmentioning

confidence: 99%

Particle Size of Milk Protein Concentrate Powder Affects the Texture of High‐Protein Nutrition Bars During Storage

Banach

Clark

Lamsal

2017

Journal of Food Science

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Milk protein concentrate powder with 85% protein (MPC85) was jet-milled to give 2 particle size distributions (that is, JM-Coarse and JM-Fine) or freeze-dried (FD), in order to improve the functional properties of MPC85 for use in high-protein nutrition (HPN) bars. Volume-weighted mean diameter decreased from 86 μm to 49, 22, and 8 μm in FD, JM-Coarse, and JM-Fine, respectively (P < 0.05). The MPC85 powders modified by jet-milling and freeze-drying were significantly denser than the control MPC85 (P < 0.05). Volume of occluded air in the modified powders decreased (P < 0.05) by an order of magnitude, yet only FD possessed a lower volume of interstitial air (P < 0.05). Particle size reduction and freeze-drying MPC85 decreased its water holding capacity and improved its dispersibility by at least 20%. Contact angle measurements showed that these modifications increased initial hydrophobicity and did not improve wettability. HPN bars made from JM-Fine or FD were firmer by 40 or 17 N, respectively, than the control on day 0 (P < 0.05). HPN bar maximum compressive force increased by 38%, 33%, and 242% after 42 d at 32 °C when formulated with JM-Fine, FD, or control MPC85, respectively. HPN bars prepared with JM-Fine were less crumbly than those formulated with control or FD MPC85. Physically altering the particle structure of MPC85 improved its ability to plasticize within HPN bars and this improved their cohesiveness and textural stability. Volume-weighted mean diameter decreased from 86 micron to 49, 22, and 8 micron in FD, JMCoarse, and JM-Fine, respectively (P < 0.05). The MPC85 powders modified by jet-milling and freeze-drying were significantly denser than the control MPC85 (P < 0.05). Volume of occluded air in the modified powders decreased (P < 0.05) by an order of magnitude, yet only FD possessed a lower volume of interstitial air (P < 0.05). Physical modifications like particle size reduction or freeze-drying of MPC85 decreased water holding capacity and improved dispersibility by at least 20%. Contact angle measurements showed that these modifications increased initial hydrophobicity, yet did not improve wettability. HPN bars made from FD or JM-Fine were firmer by 40 or 17 N, respectively, than the control on day 0 (P < 0.05). HPN bar maximum compressive force increased by 38, 33, and 242% after 42 days at 32°C when formulated with FD, JM-Fine, or control MPC85, respectively. HPN bars prepared with JMFine were less crumbly than those formulated with control or FD MPC85. Physically altering the particle structure of MPC85 improved its ability to plasticize within HPN bars and this improved their cohesiveness and textural stability.Keywords: Jet-milling, freeze-drying, protein bar, texture profile analysis (TPA), cohesiveness 3 Practical ApplicationMilk protein concentrate (MPC) powder particle size significantly influences the texture of high-protein nutrition (HPN) bars. Use of finely jet-milled MPC85 powder produced HPN bars with increased firmness and cohesiveness. Particle size reduction improve...

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Whey Wastes and Powders

Chandrapala

2018

Microstructure of Dairy Products

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Effect of superfine grinding on the structural and physicochemical properties of whey protein and applications for microparticulated proteins

Cited by 49 publications

References 30 publications

Effects of ball‐milling treatment on mussel (Mytilus edulis) protein: structure, functional properties and in vitro digestibility

Effects of ball‐milling treatment on mussel (Mytilus edulis) protein: structure, functional properties and in vitro digestibility

Particle Size of Milk Protein Concentrate Powder Affects the Texture of High‐Protein Nutrition Bars During Storage

Whey Wastes and Powders

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