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[ subject:"Agriculture." ]
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Association of Low Molecular Weight ...
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Cheema, Manpreet Kaur.
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Association of Low Molecular Weight Hydrophobic Compounds with Native Bovine Casein Micelles.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
Association of Low Molecular Weight Hydrophobic Compounds with Native Bovine Casein Micelles./
作者:
Cheema, Manpreet Kaur.
出版者:
Ann Arbor : ProQuest Dissertations & Theses, : 2017,
面頁冊數:
175 p.
附註:
Source: Dissertation Abstracts International, Volume: 79-04(E), Section: B.
Contained By:
Dissertation Abstracts International79-04B(E).
標題:
Agriculture. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10666449
ISBN:
9780355329919
Association of Low Molecular Weight Hydrophobic Compounds with Native Bovine Casein Micelles.
Cheema, Manpreet Kaur.
Association of Low Molecular Weight Hydrophobic Compounds with Native Bovine Casein Micelles.
- Ann Arbor : ProQuest Dissertations & Theses, 2017 - 175 p.
Source: Dissertation Abstracts International, Volume: 79-04(E), Section: B.
Thesis (Ph.D.)--The Pennsylvania State University, 2017.
Bovine milk contains ca.3.3 % proteins and casein proteins (alphas1-, alphas2-, beta- and kappa-casein) account for 80% of the total protein content and exist in the form of colloidal particles known as casein micelles (D¯11=130 nm, ca. 1015 micelles /mL). Modified casein micelles are extensively investigated as encapsulating and delivery agents for various hydrophobic low molecular weight probes. The ability of modified casein micelles to bind hydrophobic probes may derive from the binding affinity of native casein micelles. The objective of the present work is to evaluate the binding properties of native casein micelles by evaluating their association with lipophilic phospholipids including sphingomyelins (SM) and phosphatidylcholines (PC) and active pharmaceutical ingredients (API) appearing in bovine milk. SM and PC are the major source of choline needed for growth and development in newborns. On the contrary, partitioning of undesired hydrophobic API, appearing in dosed dairy animal, to casein proteins can result in accumulation of these API residues in dairy products making them unsafe for human consumption.
ISBN: 9780355329919Subjects--Topical Terms:
518588
Agriculture.
Association of Low Molecular Weight Hydrophobic Compounds with Native Bovine Casein Micelles.
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Bovine milk contains ca.3.3 % proteins and casein proteins (alphas1-, alphas2-, beta- and kappa-casein) account for 80% of the total protein content and exist in the form of colloidal particles known as casein micelles (D¯11=130 nm, ca. 1015 micelles /mL). Modified casein micelles are extensively investigated as encapsulating and delivery agents for various hydrophobic low molecular weight probes. The ability of modified casein micelles to bind hydrophobic probes may derive from the binding affinity of native casein micelles. The objective of the present work is to evaluate the binding properties of native casein micelles by evaluating their association with lipophilic phospholipids including sphingomyelins (SM) and phosphatidylcholines (PC) and active pharmaceutical ingredients (API) appearing in bovine milk. SM and PC are the major source of choline needed for growth and development in newborns. On the contrary, partitioning of undesired hydrophobic API, appearing in dosed dairy animal, to casein proteins can result in accumulation of these API residues in dairy products making them unsafe for human consumption.
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Native casein micelles were separated from raw skim milk of cows (mid lactation) by using size exclusion chromatography (SEC). The extractions of casein micelle fractions for hydrophobic and hydrophilic compounds followed by LC/MS analysis found 18 candidates including PC and SM showing at least 1000 times stronger peak areas associated with native casein micelles as compared to whey proteins and milk serum. Further analysis to characterize and quantify the association of PC and SM with native casein micelles of varying sizes separated from milk of cows in early, mid and late lactations was performed. LC/MS/MS analysis of extracted native casein micelles (diameters; 149 nm -- 87 nm) showed that the highest concentrations of the SM d18:1/22:0 (341.1 +/- 17.36 mug) and PC 16:0/18:1(180.2 +/- 20.08 mug) per gram of casein protein were found associated with the largest casein micelles (149 nm) isolated from late lactation milk and decreased as the casein micelle size decreased. A strong positive correlation was found between the distribution of SM, PC in raw whole milk, raw skim milk and casein micelle fraction. A decreased concentration of lipophilic SM, PC with decreasing casein micelle size was positively correlated to previously report decreasing proportions of beta-casein in smaller casein micelles due to decrease in hydrophobic domains available for interacting with hydrophobic compounds. Overall, contrary to the belief that lipophilic phospholipids such as SM and PC are present in significant amount in milk fat globule membrane in whole milk , 21-50% of most abundant SM and 16-25% of most abundant PC initially present in whole milk were found to appear in skim milk . Out of the total amount of most abundant SM and PC found in raw skim milk, 35-46% SM and 22-29% of PC were found associated with casein micelles.
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Another study to evaluate the association of hydrophobic API with native casein micelles was performed using in vivo and in vitro approach. The in vitro study conducted by spiking the raw bovine milk with hydrophobic API showed ca.66 % meloxicam, ca.30% flunixin, ca.34% of metabolite 5-hydroxy flunixin, ca. 50% thiabendazole and ca.33% of metabolite 5-hydroxy thiabendazole partitioned into casein micelles. The in vivo distribution of the API meloxicam, 5- hydroxy flunixin and 5-hydroxy thiabendazole in milk collected from dosed Holstein cows (mid lactation) showed ca.30% API associated with the casein micelles. Although, the fat fraction of the bovine milk is considered to be a suitable carrier for lipophilic compounds, less than ca. 5.0% of the recovered hydrophobic API were found in fat fraction. No linear relationship between the hydrophobicities of API and their partition into casein micelles was found.
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The present work supports the hypothesis that native casein micelles act as carriers for hydrophobic compounds appearing in bovine milk. The binding abilities of native casein micelles can be potentially used for increasing solubility of hydrophobic nutraceuticals in low fat foods. The significance of SM and PC for neurological development in infants, provide avenues for utilizing larger casein micelles in late lactation milk for fortification of infant formulas. Conversely, association of undesirable API with casein micelles in dairy milk needs to be taken into account for analysis of their residues in dairy products.
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