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Viscosity and Gel Formation of Micel...

Dunn, Marshall Robert.

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Viscosity and Gel Formation of Micellar Casein Concentrates.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Viscosity and Gel Formation of Micellar Casein Concentrates./
作者:	Dunn, Marshall Robert.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2021,
面頁冊數:	138 p.
附註:	Source: Masters Abstracts International, Volume: 83-03.
Contained By:	Masters Abstracts International83-03.
標題:	Behavior. -
電子資源:	https://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=28552469
ISBN:	9798522940812

Viscosity and Gel Formation of Micellar Casein Concentrates.
Dunn, Marshall Robert.

Viscosity and Gel Formation of Micellar Casein Concentrates. - Ann Arbor : ProQuest Dissertations & Theses, 2021 - 138 p.

Source: Masters Abstracts International, Volume: 83-03.

Thesis (M.Sc.)--North Carolina State University, 2021.

This item must not be sold to any third party vendors.

Milk protein products have gained widespread use in the food and sports nutrition industries. Processing techniques, such as micro and ultrafiltration (UF), have led to the development of novel protein ingredients, particularly micellar casein concentrate (MCC). Liquid MCC has unique rheological properties, specifically that it will form a thermo-reversible gel at colder temperatures. The mechanisms responsible for the rheological properties of MCC are not completely understood but are thought to be related to jamming of the micelles and to the dissociation of β-casein from the micelle at colder temperatures. This thesis determined the basis for viscosity increase and cold gelation of liquid MCC at protein concentrations from 6 to 20% during refrigerated storage. Skim milk (ca 350 kg) was pasteurized (72°C for 16 sec) and filtered through a ceramic MF system to make micellar casein concentrate (MCC). The liquid MCC was immediately concentrated via a plate ultrafiltration (UF) system to 18% protein (w/w). The MCC was then diluted to various concentrations (6 to 18%, w/w). Apparent viscosity readings were collected from liquid MCC samples (6, 8, 10, 12% protein w/w) at 4, 20, and 37°C. Instron compression force of MCC gels (14, 16, 18% protein w/w) was collected over a period of 2 weeks at 4°C. The maximum compressive load was compared at each time point to assess the changes in gel strength over time. Supernatants from MCC of 6.5 and 10.5% protein were collected after ultracentrifugation (100,605 x g for 2 h at 4, 20 and 37°C) and the nitrogen distribution (total, noncasein, casein, and nonprotein nitrogen) was determined. The entire experiment was replicated 3 times. The highest protein concentrations of MCC formed gels almost immediately on cooling to 4°C, while lower concentrations of MCC were viscous liquids. The protein, casein, and casein as a percent of true protein in the liquid phase around casein micelles in MCC increased with increasing casein concentration of the MCC and with decreasing temperature. Casein as a percent of true protein at 4°C in the liquid phase around casein micelles increased from about 16% for skim milk to about 78% for an MCC containing 10.5% protein. AV of MCC solutions in the range of 6 to 13% casein increased with increasing casein concentration and decreasing temperature. There was a strong temperature by protein concentration interaction for viscosity with AV increasing non-linearly with decreasing temperature at high protein concentration. MCC containing 16 and 18% casein gelled upon cooling to form a gel that was likely a particle jamming gel. These gels increased in strength over 10 days of storage at 4oC, likely due to migration of casein out of the micelles and interaction of the non-micellar casein to form a network that further strengthened the random loose particle jamming gel structure. With an increased understanding of the mechanism of cold thickening of MCC, there may be potential to replace hydrocolloids for thickening and stabilizing beverages with a clean label ingredient and also to provide a high level of protein with superior flavor and color.

ISBN: 9798522940812Subjects--Topical Terms:

532476
Behavior.

Viscosity and Gel Formation of Micellar Casein Concentrates.
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520 $a Milk protein products have gained widespread use in the food and sports nutrition industries. Processing techniques, such as micro and ultrafiltration (UF), have led to the development of novel protein ingredients, particularly micellar casein concentrate (MCC). Liquid MCC has unique rheological properties, specifically that it will form a thermo-reversible gel at colder temperatures. The mechanisms responsible for the rheological properties of MCC are not completely understood but are thought to be related to jamming of the micelles and to the dissociation of β-casein from the micelle at colder temperatures. This thesis determined the basis for viscosity increase and cold gelation of liquid MCC at protein concentrations from 6 to 20% during refrigerated storage. Skim milk (ca 350 kg) was pasteurized (72°C for 16 sec) and filtered through a ceramic MF system to make micellar casein concentrate (MCC). The liquid MCC was immediately concentrated via a plate ultrafiltration (UF) system to 18% protein (w/w). The MCC was then diluted to various concentrations (6 to 18%, w/w). Apparent viscosity readings were collected from liquid MCC samples (6, 8, 10, 12% protein w/w) at 4, 20, and 37°C. Instron compression force of MCC gels (14, 16, 18% protein w/w) was collected over a period of 2 weeks at 4°C. The maximum compressive load was compared at each time point to assess the changes in gel strength over time. Supernatants from MCC of 6.5 and 10.5% protein were collected after ultracentrifugation (100,605 x g for 2 h at 4, 20 and 37°C) and the nitrogen distribution (total, noncasein, casein, and nonprotein nitrogen) was determined. The entire experiment was replicated 3 times. The highest protein concentrations of MCC formed gels almost immediately on cooling to 4°C, while lower concentrations of MCC were viscous liquids. The protein, casein, and casein as a percent of true protein in the liquid phase around casein micelles in MCC increased with increasing casein concentration of the MCC and with decreasing temperature. Casein as a percent of true protein at 4°C in the liquid phase around casein micelles increased from about 16% for skim milk to about 78% for an MCC containing 10.5% protein. AV of MCC solutions in the range of 6 to 13% casein increased with increasing casein concentration and decreasing temperature. There was a strong temperature by protein concentration interaction for viscosity with AV increasing non-linearly with decreasing temperature at high protein concentration. MCC containing 16 and 18% casein gelled upon cooling to form a gel that was likely a particle jamming gel. These gels increased in strength over 10 days of storage at 4oC, likely due to migration of casein out of the micelles and interaction of the non-micellar casein to form a network that further strengthened the random loose particle jamming gel structure. With an increased understanding of the mechanism of cold thickening of MCC, there may be potential to replace hydrocolloids for thickening and stabilizing beverages with a clean label ingredient and also to provide a high level of protein with superior flavor and color.
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