Studies on Size Characteristics and Reformation of Casein Micelles in Bovine Milk

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ISBN 13 :
Total Pages : 234 pages
Book Rating : 4.:/5 (319 download)

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Book Synopsis Studies on Size Characteristics and Reformation of Casein Micelles in Bovine Milk by : Santa Hui-Cheng Lin

Download or read book Studies on Size Characteristics and Reformation of Casein Micelles in Bovine Milk written by Santa Hui-Cheng Lin and published by . This book was released on 1971 with total page 234 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Casein Micelles and Their Properties

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ISBN 13 :
Total Pages : 250 pages
Book Rating : 4.:/5 (115 download)

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Book Synopsis Casein Micelles and Their Properties by : Maneesha S. Mohan

Download or read book Casein Micelles and Their Properties written by Maneesha S. Mohan and published by . This book was released on 2014 with total page 250 pages. Available in PDF, EPUB and Kindle. Book excerpt: The internal structure of casein micelles is not fully understood. In the present work, we explore some of the basic questions about casein micelles in bovine milk including its size distribution, native binding properties and effect of ultra-high pressure homogenization (ultra-HPH) on technological properties of casein micelles. The size distribution of casein micelles was studied by cryo-TEM using skim milk from four cows. The degree of variation in casein micelle sizes (polydispersity) ranged between 0.39 and 0.47 for a size distribution ranging from 10 to 693 nm. These results indicated high polydispersity of casein micelles in milk from single cows. Casein micelles associated with vitamin A in four pasteurized skim milks (1.6 - 2.5 micro gm/mL of milk; 14 - 40% of the initial quantity detected in milks), while other protein fractions contained negligible vitamin A. Thus, casein micelles can inherently associate with hydrophobic probes like vitamin A in milk. This association of vitamin A to casein micelles in milk provided protection from degradation on exposure to ultraviolet light when compared to apple juice. Further, the effect of ultra-HPH up to 500 MPa on the physicochemical (apparent casein micelle size by dynamic light scattering) and technological characteristics (rennet coagulation - firmness [ 90 min, 1Hz, 0.01% strain]; acid gelation using 3%w/v glucono delta lactone – firmness [22°C, 110 min, 1Hz, 0.01% strain], SDS-PAGE) of casein micelles were studied. Casein micelle size increased from ca. 180 nm at 100 MPa to ca. 280 nm at 500 MPa HPH pressure. With increase in HPH pressure, renneting ability decreased until no coagulation was obtained for 500 MPa HPH milk. The firmness of HPH milk acid gels increased from about 76 Pa to 108 Pa when pressure was increased above 100 MPa (up to 400 MPa) HPH as compared to acid gels made from non-homogenized milk. Overall we elucidated the size distribution, binding ability to vitamin A and changes occurring on ultra-HPH in casein micelles. This information can be utilized by the industry to modify and utilize casein micelles as an ingredient for different end uses.

Association of Low Molecular Weight Hydrophobic Compounds with Native Bovine Casein Micelles

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ISBN 13 :
Total Pages : pages
Book Rating : 4.:/5 (1 download)

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Book Synopsis Association of Low Molecular Weight Hydrophobic Compounds with Native Bovine Casein Micelles by : Manpreet Cheema

Download or read book Association of Low Molecular Weight Hydrophobic Compounds with Native Bovine Casein Micelles written by Manpreet Cheema and published by . This book was released on 2017 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: Bovine milk contains ca.3.3 % proteins and casein proteins (s1-, s2-, - and -casein) account for 80% of the total protein content and exist in the form of colloidal particles known as casein micelles (D11=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.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 g) and PC 16:0/18:1(180.2 20.08 g) 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 -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. 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. 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.

Measurement of Casein Micelle Size in Raw Dairy Cattle Milk by Dynamic Light Scattering

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ISBN 13 :
Total Pages : pages
Book Rating : 4.:/5 (115 download)

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Book Synopsis Measurement of Casein Micelle Size in Raw Dairy Cattle Milk by Dynamic Light Scattering by : Peter Hristov

Download or read book Measurement of Casein Micelle Size in Raw Dairy Cattle Milk by Dynamic Light Scattering written by Peter Hristov and published by . This book was released on 2016 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: The particle size of milk influences its microstructure and defines the qualities of dairy products, such as colloidal stability and texture. Moreover, differences in casein micelle size may affect milk processing, especially cheese making. Hence, the size of casein micelle is an important characteristic of raw milk and determines the yield of dairy products. The aim of the present research is to estimate the casein micelle size in the raw milk of dairy cattle by dynamic light scattering. The obtained results may be used for genetic elaboration of the breed, as well as to increase the competitiveness of the milk industry by selection of animals with higher casein micelle size.

Casein Micelles from Bovine Milk

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ISBN 13 :
Total Pages : 73 pages
Book Rating : 4.:/5 (586 download)

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Book Synopsis Casein Micelles from Bovine Milk by : Raymundo Trejo

Download or read book Casein Micelles from Bovine Milk written by Raymundo Trejo and published by . This book was released on 2009 with total page 73 pages. Available in PDF, EPUB and Kindle. Book excerpt: Caseins, in the form of micelles, are the most abundant milk protein. The nature of these micelles is still not fully understood and several models have been proposed. The first chapter discusses this topic, along with the importance of milk proteins to the food industry, and their allergenic properties. In the second chapter the changes in the hydrophobicity of dissociated casein micelles are explored. As new applications for milk proteins are discovered, it becomes more important to understand their physicochemical properties when subjected to different treatments. It has been reported that casein micelles disassociate when heated in the presence of ethanol. The changes to the hydrophobicity of milk proteins during that process were evaluated by utilizing the fluorescent hydrophobic probe 1-anilinonaphthalene-8-sulfonic acid (ANS). The results showed that the fluorescence intensity of ANS decreased when the samples were heated. Using the information obtained from the fluorescence spectroscopy it was possible to infer that the hydrophobicity of the milk proteins also decreased when the casein micelles disassociate in the presence of ethanol. The third chapter deals with the association of native casein micelles and whey proteins. This association was thought to only be consequence of whey protein denaturation and interaction with k-casein through S-S linkages. Size exclusion chromatography (SEC) was used to isolate native casein micelles from raw skim milk samples with a pH value of 6.8, 6.0, and 5.5. In a separate experiment, casein micelles were precipitated by lowering the pH of milk to ~4.6, and the whey was removed and substituted with protein free serum (PFS). Then, the casein micelles were re-suspended in PFS at a native pH. SDS-PAGE was conducted on the samples utilizing silver staining of total proteins for higher sensitivity of detection. Whey proteins were found in association with the casein micelles at all pH values. Samples of both native pH and re-suspended casein micelles were tested with gel electrophoresis under native and reducing conditions. The bands for the whey proteins were only visible under the reducing conditions. These findings demonstrate that whey proteins are also part of the native casein micelle structure.

Casein Micelles from Bovine Milk

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ISBN 13 :
Total Pages : 149 pages
Book Rating : 4.:/5 (842 download)

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Book Synopsis Casein Micelles from Bovine Milk by : Raymundo Trejo

Download or read book Casein Micelles from Bovine Milk written by Raymundo Trejo and published by . This book was released on 2012 with total page 149 pages. Available in PDF, EPUB and Kindle. Book excerpt: A definitive structure of the native casein micelle structure continues to elude researchers. Data and images obtained via cryo - transmission electron microscopy of isolated native casein micelles allowed for the reconstruction of a three dimensional model of the micelle; which contains water filled cavities (ca. 20 to 30 nm diameter), channels (diameter larger than ca. 5 nm), and several hundred high density nanoclusters (6-12 nm diameter) within the interior of the micelles. Analysis of isolated casein micelles by SDS polyacrylamide gel electrophoresis (pH 6.8, 5.0) showed that whey proteins were found associated with the isolated micelles regardless of the pH of the milk sample. However, the introduction of the hydrophobic peptide valinomycin (MW= 1111.32; LogP=5.92) into raw skim milk did not result on the peptide being found associated with isolated casein micelles. Taking advantage of the heat, ethanol, and pH mediated micelle disassociation, it was possible to improve the solubility of caseins in fluid milk via esterification. The esterification of casein resulted in a shift on its isoelectric point; which in turn resulted in a better solubility at low pH values. Caseins esterified at a pH 3 and 4 had a higher solubility than those esterified at other pH values and non-modified skim milk powder in acidified juice with a pH equal or below 3.5. By adding a chilling step (3-5°C/pH ~5.2) to the processing of non-fat yogurt, it was possible to improve the whey holding capacity of the product while also producing a firm product without the need for added stabilizers or gums. In the conditions of the chilling step, beta casein and calcium migrated out of the micelles. This resulted in a reduction on the size of the micelles. A possible explanation for these results would be that once the temperature returned to 47°C, the liberated caseins self-associated into small micelles and together with the smaller original micelles formed a tight gel matrix. Casein is fundamentally important to the dairy industry. By gaining an understanding of its structure and properties, it is possible to develop new applications and enhance its performance in dairy products.

Food Biochemistry and Food Processing

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Publisher : John Wiley & Sons
ISBN 13 : 0470276347
Total Pages : 786 pages
Book Rating : 4.4/5 (72 download)

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Book Synopsis Food Biochemistry and Food Processing by : Y. H. Hui

Download or read book Food Biochemistry and Food Processing written by Y. H. Hui and published by John Wiley & Sons. This book was released on 2008-02-15 with total page 786 pages. Available in PDF, EPUB and Kindle. Book excerpt: The biochemistry of food is the foundation on which the research and development advances in food biotechnology are built. In Food Biochemistry and Food Processing, lead editor Y.H. Hui has assembled over fifty acclaimed academicians and industry professionals to create this indispensable reference and text on food biochemistry and the ever-increasing development in the biotechnology of food processing. While biochemistry may be covered in a chapter or two in standard reference books on the chemistry, enzymes, or fermentation of food, and may be addressed in greater depth by commodity-specific texts (e.g., the biotechnology of meat, seafood, or cereal), books on the general coverage of food biochemistry are not so common. Food Biochemistry and Food Processing effectively fills this void. Beginning with sections on the essential principles of food biochemistry, enzymology and food processing, the book then takes the reader on commodity-by-commodity discussions of biochemistry of raw materials and product processing. Later sections address the biochemistry and processing aspects of food fermentation, microbiology, and food safety. As an invaluable reference tool or as a state-of-the-industry text, Food Biochemistry and Food Processing fully develops and explains the biochemical aspects of food processing for scientist and student alike.

Reduction of Membrane Fouling During Ultrafiltration of Cottage Cheese Whey

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ISBN 13 :
Total Pages : 380 pages
Book Rating : 4.:/5 (31 download)

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Book Synopsis Reduction of Membrane Fouling During Ultrafiltration of Cottage Cheese Whey by : Doretta Ngah-chun Lee

Download or read book Reduction of Membrane Fouling During Ultrafiltration of Cottage Cheese Whey written by Doretta Ngah-chun Lee and published by . This book was released on 1973 with total page 380 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Separation of Functional Molecules in Food by Membrane Technology

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Publisher : Academic Press
ISBN 13 : 0128150572
Total Pages : 435 pages
Book Rating : 4.1/5 (281 download)

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Book Synopsis Separation of Functional Molecules in Food by Membrane Technology by : Charis M. Galanakis

Download or read book Separation of Functional Molecules in Food by Membrane Technology written by Charis M. Galanakis and published by Academic Press. This book was released on 2018-11-14 with total page 435 pages. Available in PDF, EPUB and Kindle. Book excerpt: Separation of Functional Molecules in Food by Membrane Technology deals with an issue that is becoming a new research trend in the field of food and bioproducts processing. The book fills in the gap of transfer knowledge between academia and industry by highlighting membrane techniques and applications for the separation of food components in bioresources, discussing separation mechanisms, balancing advantages and disadvantages, and providing relevant applications. Edited by Charis Galanakis, the book is divided in 13 chapters written by experts from the meat science, food technology and engineering industries. - Covers the 13 most relevant topics of functional macro and micro molecules separation using membrane technology in the food industry - Brings the most recent advances in the field of membrane processing - Presents the sustainability principles of the food industry and the modern bioeconomy frame of our times

Casein

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Publisher : Elsevier
ISBN 13 : 0443132143
Total Pages : 427 pages
Book Rating : 4.4/5 (431 download)

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Book Synopsis Casein by : Mamdouh El-Bakry

Download or read book Casein written by Mamdouh El-Bakry and published by Elsevier. This book was released on 2024-06-24 with total page 427 pages. Available in PDF, EPUB and Kindle. Book excerpt: Casein: Structural Properties, Uses, Health Benefits and Nutraceutical Applications investigates casein properties, uses, and applications in food and non-food products, in addition to exploring its health benefits and uses in manufacturing, such as in cheese products, along with an in-depth discussion on the future scope, challenges, and market trends of this protein. Casein: Structural Properties, Uses, Health Benefits and Nutraceutical Applications is an excellent reference for food scientists, dairy researchers, pharmaceutical scientists, students and researchers studying related fields. - Provides comprehensive coverage of casein, the main milk protein that has many applications and uses - Includes suggested reading for further information - Addresses a wide-range of related topics, including non-food applications of casein

Studies on the Casein Micelles of Buffalo Milk in Relation to Rennet Action

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ISBN 13 :
Total Pages : pages
Book Rating : 4.:/5 (697 download)

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Book Synopsis Studies on the Casein Micelles of Buffalo Milk in Relation to Rennet Action by : S. Oommen

Download or read book Studies on the Casein Micelles of Buffalo Milk in Relation to Rennet Action written by S. Oommen and published by . This book was released on 1973 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: Micellar casein of buffalo milk differed from that of cow milk in the chemiccal composition namely sialic acid, hexose, nitrogen, calcium and phosphorus. Chemical omposition was also affected by the stage of lactation and particle size of casein micelle. Casein from cow milk and buffalo milk was also shown to differ in their proteolytic action by trypsin andrennin Buffalo micellar casein showed faster turbidity development by rennet a compared o cow micellar aein.

The Role of [alpha]s1-casein in the Formation of the Casein Micelle

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ISBN 13 :
Total Pages : 114 pages
Book Rating : 4.:/5 (376 download)

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Book Synopsis The Role of [alpha]s1-casein in the Formation of the Casein Micelle by : Chinchi C. Chen

Download or read book The Role of [alpha]s1-casein in the Formation of the Casein Micelle written by Chinchi C. Chen and published by . This book was released on 1997 with total page 114 pages. Available in PDF, EPUB and Kindle. Book excerpt: "Caseins are the major protein components of milk. Bovine caseins have been the most thoroughly studied and serve as the principal area of research for the dairy industry. Bovine caseins are composed of several major polypeptide families, (alpha)s1-, (alpha)s1-, (beta)- and K-caseins. The (alpha)s1-caseins constitute 30.6% of bovine milk protein. The distribution of polar and apolar amino acids within each (alpha)s1 -casein molecule tends to be asymmetric, yielding protein molecules with hydrophobic and hydrophilic domains that give the caseins excellent functional properties. Moreover, the phosphoserine groups of (alpha)s1 -casein associate with calcium phosphate complexes in milk to form loosely ordered aggregates, termed casein micelles. This conformational feature renders (alpha)s1 -casein with great capacity fkor the delivery of a highly nutritious solution of protein, carbohydrate, phosphate, calcium and other minerals. In this study, we have investigated the physical properties of (alpha)s1casein under different pHs and/or various concentration of calcium. The fluorescence studies suggested that a decrease in pH and an increase of calcium concentration switch the surrounding environment of Trp 164 from hydrophilic to hydrophobic. The results, obtained from the studies of viscosity, phase separation and isoelectric point calculations, suggested that phosphorylated (alpha)s1 -casein forms micelles at a pH of -5.5. This is consistent with the pH where milk micelles form and; therefore, lends evidence to the hypothesis that the main component of the micelle framework in milk is (alpha)s1 -casein. In conjunction and our results with the predicted secondary structure, we proposed that, at a pH -5.5, the negative charges in the hydrophobic domain of (alpha)s1 -casein are neutralized and the electrostatic repulsion of the hydrophilic domain is reduced. Therefore, the protein-protein interaction is promoted and micelle formation is favored."--Abstract.

Food Science and Technology Abstracts

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ISBN 13 :
Total Pages : 1058 pages
Book Rating : 4.3/5 (91 download)

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Book Synopsis Food Science and Technology Abstracts by :

Download or read book Food Science and Technology Abstracts written by and published by . This book was released on 1972-10 with total page 1058 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Dairy Chemistry and Biochemistry

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Publisher : Springer
ISBN 13 : 3319148923
Total Pages : 598 pages
Book Rating : 4.3/5 (191 download)

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Book Synopsis Dairy Chemistry and Biochemistry by : P. F. Fox

Download or read book Dairy Chemistry and Biochemistry written by P. F. Fox and published by Springer. This book was released on 2015-06-19 with total page 598 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book is the most comprehensive introductory text on the chemistry and biochemistry of milk. It provides a comprehensive description of the principal constituents of milk (water, lipids, proteins, lactose, salts, vitamins, indigenous enzymes) and of the chemical aspects of cheese and fermented milks and of various dairy processing operations. It also covers heat-induced changes in milk, the use of exogenous enzymes in dairy processing, principal physical properties of milk, bioactive compounds in milk and comparison of milk of different species. This book is designed to meet the needs of senior students and dairy scientists in general.

Milk Proteins

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Publisher : Academic Press
ISBN 13 : 0080920683
Total Pages : 562 pages
Book Rating : 4.0/5 (89 download)

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Book Synopsis Milk Proteins by : Mike Boland

Download or read book Milk Proteins written by Mike Boland and published by Academic Press. This book was released on 2009-02-07 with total page 562 pages. Available in PDF, EPUB and Kindle. Book excerpt: In recent years, there has been a great deal of progress in the understanding and management of milk proteins across the production chain. Milk Proteins takes a uniquely comprehensive look at those developments and presents them in a one-source overview. By providing a brief overview of each topic area, and then describing the most important recent advances therein, the "field-to-table" approach of this book provides specialists with new and directly relevant information in their own areas, along with information from complementary research fields, allowing them to contextualize their work within the larger pictures. At the same time it provides generalists with a complete overview and offers insights into topics for more in-depth reading. Covering areas that are receiving attention from people of many fields -- genomics, functional foods -- and including the latest research and developments in milk-protein phenomenon and interactions, this book will be an ideal resource for professionals and students alike. - A fresh look at recent developments across the entire production chain -- from animal genetics to nutritional and nutrigenomic needs of the customer - Up-to-date information from internationally-recognised authors from both academic and commercial resources

Caseins

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Publisher : Nova Science Publishers
ISBN 13 : 9781634853378
Total Pages : 145 pages
Book Rating : 4.8/5 (533 download)

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Book Synopsis Caseins by : Laurence Mendoza

Download or read book Caseins written by Laurence Mendoza and published by Nova Science Publishers. This book was released on 2016 with total page 145 pages. Available in PDF, EPUB and Kindle. Book excerpt: Casein, one of the major proteins found in milk sources, can be associated with many health benefits. This book discusses the properties, functions and health implications of casein. Chapter One reviews the scientific evidence around health promoting effects of casein hydrolysates and (bioactive) peptides thereof from an infant nutrition perspective. Chapter Two studies the physicochemical and functional properties of native and trypsin-treated caprine casein micelles. Chapter Three focuses on the molecular characteristics of caseins from equid and from human milk compared also to those of bovine milk. Chapter Four discusses molecular properties of caseins and allergenicity. The last chapter compares and discusses food regulations of different nations with an important winemaking tradition.

Milk Proteins V2

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Publisher : Elsevier
ISBN 13 : 0323145779
Total Pages : 567 pages
Book Rating : 4.3/5 (231 download)

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Book Synopsis Milk Proteins V2 by : Hugh McKenzie

Download or read book Milk Proteins V2 written by Hugh McKenzie and published by Elsevier. This book was released on 2012-12-02 with total page 567 pages. Available in PDF, EPUB and Kindle. Book excerpt: Milk Proteins: Chemistry and Molecular Biology, Volume II provides an extensive and detailed discussion on individual milk proteins. This volume focuses on caseins, which constitute the major group of milk proteins, and provides an understanding of the formation and structure of casein micelles. The topics discussed include the formation and structure of casein micelles; isolation, properties, and zone electrophoresis of whole casein; casein and its attack by rennin (chymosin); biochemistry of prorennin (prochymosin) and rennin (chymosin); minor milk proteins and enzymes; milk protein research and milk technology; and milk proteins in prospect. This book is a good reference for students majoring in protein chemistry, as well as protein chemists and biochemists conducting research on milk proteins.