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The Effect On The Casein Micelle Size And Plasmin Activity When Using A Microfluidizer For Homogenising Skim Milk
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Book Synopsis The Effect on the Casein Micelle Size and Plasmin Activity when Using a Microfluidizer for Homogenising Skim Milk by : Louise Knutsson
Download or read book The Effect on the Casein Micelle Size and Plasmin Activity when Using a Microfluidizer for Homogenising Skim Milk written by Louise Knutsson and published by . This book was released on 2006 with total page 92 pages. Available in PDF, EPUB and Kindle. Book excerpt:
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.
Book Synopsis The Effect of Casein to Whey Protein Ratio on the Heat Stability of Skim Milk by : Mandeep Kaur Jeswan Singh
Download or read book The Effect of Casein to Whey Protein Ratio on the Heat Stability of Skim Milk written by Mandeep Kaur Jeswan Singh and published by . This book was released on 2011 with total page 628 pages. Available in PDF, EPUB and Kindle. Book excerpt: Heating is an integral part of processing milk and the response of milks to heating dictates the processability and functionality of the milks. This thesis examines the effects of changing the ratio of the caseins to whey proteins on the behaviour of skim milk on heating. Modified skim milks with similar serum mineral compositions but with different casein to whey protein ratios (0.03, 1.74, 3.97, 5.27, 7.25) were prepared by blending casein rich and whey protein rich fractions in appropriate amounts and dialyzing against 9% total solids skim milk (pH6.7). These modified milks were freeze dried and used for preparation of 9% total solids milks at various pH (6.2, 6.7 and 7.2).Viscometry and Diffusing Wave Spectroscopy (DWS), both prior to and after heating as well as in situ, were used to investigate the effects of the casein to whey protein ratios on the heat stability of the milks. The pH in situ at the time of heating and Ca activity at 25°C were used to gain insights into changes in the mineral equilibria. The heat-induced changes to protein distribution between the serum and colloidal phases and the type of protein complexes formed after heating were followed using HPLC-SEC and gel electrophoresis.On heating (90°C/10min), milks (pH6.2) with the lowest ratios of casein to whey protein (0.03 and 1.74) gelled while the viscosities of the other milks increased. At pH6.7 and 7.2, the viscosity decreased for all milks except that with the lowest casein to whey protein ratio (0.03) where viscosity was increased. The viscosity increase at the lower pH was attributed to complex formation between the denatured whey proteins and the casein micelles. The decrease in viscosity for the higher pH milks after heating was due to the dissociation of caseins from the micelle and the formation of increased amounts of soluble aggregates as confirmed by the HPLC-SEC and gel electrophoresis. Characterization of the serum protein concentration and gel electrophoresis analysis of the modified milks showed that iIn the presence of casein micelles, the serum protein concentration of the milks increased on heating as a function of pH and increasing casein to whey protein ratio as a result of more dissociation of caseins and the formation of soluble aggregates at higher pH. HPLC-SEC analysis showed that the size of the soluble aggregates decreases as the casein to whey protein ratio increases.The pH in situ decreased during heating (90oC/10min), the magnitude of which was increased with increasing initial milk pH. The changes in pH in situ were independent of the casein to whey protein ratio and were similar for all milks, clearly demonstrating that pH changes are solely governed by the serum mineral composition. The pH and Ca activity after heating werewas largely restored to the initial values for most milks except for the milks with lower casein to whey protein ratios (0.03, 1.74) at high pH (7.2). This demonstrates that in the absence of casein micelles, there were changes to the calcium phosphate equilibria that were not reflected in the overall pH change.DWS measurements as a function of temperature (25-120°C) enabled an in-situ study of (a) the heat-induced changes to the milk proteins and the serum as manifested by the changes to the casein micelles and (b) the temperature of the onset of gelation. Changes to the interactions of the casein micelles as shown by changes in their diffusion coefficients were most pronounced at pH 6.2 where significant changes to the mobility of the casein micelles occurred between 80 to 120oC due to the aggregation of the denatured whey proteins on the casein micelles surface. At pH 6.7 and 7.2, changes to the mobility of the casein micelles were minimal except at high temperatures (105-120oC) due to the decrease in size as a result of increased soluble aggregate formation. At 120oC, with the exception of the milk with the highest casein to whey protein ratio, all pH6.2 milks gelled on heating. The reduction in the low whey protein concentration for the milk with the highest casein to whey protein ratio (7.25) improved heat stability at low pH.Overall, the results showed that the pH and temperature of heating have major effects on the aggregation behavior of the proteins and that the susceptibility of the milks to aggregation was strongly influenced by the casein to whey protein ratio. Heat stability increased with increasing ratio of caseins to whey proteins, especially at low pH. The results of this work have demonstrated that the heat stability of milks can be manipulated by careful control of the protein composition and the pH prior to heating.
Book Synopsis Kinetics of Inactivation of Immobilized Pepsin and Its Effect on the Release of Macropeptides from Casein During Pepsin Action by : Hyong Joo Lee
Download or read book Kinetics of Inactivation of Immobilized Pepsin and Its Effect on the Release of Macropeptides from Casein During Pepsin Action written by Hyong Joo Lee and published by . This book was released on 1976 with total page 114 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis The Effect of Emulsifying Salts on Casein Micelle Structure in Response to Varied Environmental Conditions by : Mitchell Culler
Download or read book The Effect of Emulsifying Salts on Casein Micelle Structure in Response to Varied Environmental Conditions written by Mitchell Culler and published by . This book was released on 2018 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: The Code of Federal Regulations (CFR) lists 13 emulsifying salts (ES) to be used in the production of pasteurized process cheese. Although these ES are widely used commercially, their method of action in a cheese system is not completely understood, as evidence has been found that the ES can interact with proteins, and their usage is therefore based on an empirical, trial-and-error approach. Further complicating the matter, current research in this area uses inconsistent methods to study the topic, making it difficult to draw conclusions from previous work. Additionally, the interactions between casein proteins in micelles have been shown to change in response to temperature or pH, thus affecting their interactions with ES. In this investigation, 10 of the ES listed in the CFR were investigated for their effects on casein micelle integrity by means of measuring the turbidity (absorbance at 400 nm) of milk-ES systems in order to determine the effect of an ES on a milk protein-based system and how this effect may change for a given ES under varied temperature and pH.In a first study, ES solutions consisted of a mixture of ES in a 1-in-20 dilution of protein free serum (PFS; permeate from 3 kDa molecular weight cut-off (MWCO) skim milk ultrafiltrate) in water to obtain ES concentrations from 0 to 248 mM. Pasteurized skim milk was added to solutions containing specific ES ranging in concentration from 0 to 248 mM and pH 5, 5.8, 6.8, 7.8, and 8.8. The turbidity of the samples was measured at 400 nm immediately after mixing (time, t = 0), after 30 s (t = 30s), and after 30 min (t = 30 min). The resulting decrease in turbidity was modeled using an exponential decay equation, with parameter C* representing a critical salt concentration used as a benchmark level of dissociation that can be used to compare between the effects of ES at varying conditions of pH and temperature. At pH values 5.8 and 6.8, the ES caused the greatest decrease in turbidity of the diluted milk system. At pH 5, the ES had the least effect on the turbidity of the system. SHMP was found to have the strongest dissociative effect, with C* equal to 0.33 mM for t=0 at pH 6.8. In contrast, the largest C* concentration calculated at pH 6.8 was monosodium phosphate at 278.22 mM. Increased time resulted in lower C* values.Next, an automated device was built consisting of three pumps, a continuous flow UV-VIS cell, light source, spectrometer, and a heat exchanger. The prototype automatically modified salt concentration (0 to 246 mM) and temperature (5 to 50C) while recording the turbidity of a diluted skim-milk system. An aqueous solution with continuously variable salt concentration was achieved by making two solutions; both buffered using 5% PFS and one containing 250 mM of an ES. Their ratio was varied to comprise 96% of the total flow through an in-line UV-VIS flow cell. The remaining 4% of the flow was pasteurized skim milk.Temperature and pH were found to have highly specific effects on a given salts ability to cause dissociation. The C* concentrations for ST and SPT increased with pH, but did not change significantly in response to varied temperature in the 5 to 50C range. By contrast, the C* concentration of SAD was approximately 15 times lower at pH 7.8 and 50C than at pH 5.8 and 5C. The results also suggest the formation of intermediate protein aggregates for several salts at temperature and pH of 50C and 7.8, respectively.
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:
Book Synopsis The Manufacture of Casein from Buttermilk Or Skim Milk by : Arnold Orlando Dahlberg
Download or read book The Manufacture of Casein from Buttermilk Or Skim Milk written by Arnold Orlando Dahlberg and published by . This book was released on 1918 with total page 40 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Endogenous Proteases in Bovine Milk and the Effect of Thermal Processing on Their Activity by : Robert Joseph Verdi
Download or read book Endogenous Proteases in Bovine Milk and the Effect of Thermal Processing on Their Activity written by Robert Joseph Verdi and published by . This book was released on 1988 with total page 318 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis The Casein Micelle as an Encapsulation System for Triclosan by : Adrienne Lysandra Roach
Download or read book The Casein Micelle as an Encapsulation System for Triclosan written by Adrienne Lysandra Roach and published by . This book was released on 2009 with total page 167 pages. Available in PDF, EPUB and Kindle. Book excerpt: This dissertation reports on the use of the casein micelle as an encapsulation and potential delivery system for a low molecular weight hydrophobic compound, triclosan. The ability of the casein micelle to serve in this capacity was tested in a series of experiments investigating: 1) micelle dissociation to expose hydrophobic binding sites of interaction, 2) encapsulation of triclosan, 3) the release of triclosan under various conditions, and 4) the intercellular delivery of triclosan to human liver cells in vitro for the inactivation of a malaria-causing parasite. Casein micelle dissociation and reassociaiton was achieved through high pressure homogenization and solvent-mediated pressure-induced dissociation. Triclosan was found to naturally associate to casein micelles in skim milk (up to 70%) and this association is enhanced by 30% at homogenization pressures reaching 300 MPa. The release of triclosan is governed by the disruption of micelle integrity, i.e., the enhancement casein-solvent interactions, where triclosan likely exists as a triclosan-protein complex as opposed to free triclosan. In the presence of milk, the release of triclosan is prevented in simulated gastric solutions but released in a simulated intestinal solution, demonstrating the ability of to milk protect triclosan from the acidic environment of the stomach and promote its release in the intestine, a measure of bioaccessibility. The intercellular delivery of triclosan was most affected by the type of milk protein. Triclosan transported within [beta]-casein isolates where most sufficient in preventing the growth and development of Plasmodium berghei, the rodent malaria parasite, in human liver cells. Triclosan carried within milk digestates were also efficient in delaying parasite growth, whereas triclosan carried within milk serum by serum proteins where completely ineffective. Triclosan in the presence of milk also provided a protective effect on host cells from the acute toxicity of triclosan in free form. These experiments introduced new functional properties of the casein micelle. The casein micelle has the ability to serve as an encapsulation system and casein proteins, as a potential delivery system. This introduces new functional properties of the casein micelle for use novel usage within the food, pharmaceutical, and/or cosmetic industry.
Book Synopsis Methods for Manufacturing Acid-precipitated Casein from Skim Milk by : Earle O. Whittier
Download or read book Methods for Manufacturing Acid-precipitated Casein from Skim Milk written by Earle O. Whittier and published by . This book was released on 1942 with total page 32 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Methods for Manufacturing Acid-precipitated Casein from Skim Milk by : Charles Sterling Trimble
Download or read book Methods for Manufacturing Acid-precipitated Casein from Skim Milk written by Charles Sterling Trimble and published by . This book was released on 1933 with total page 32 pages. Available in PDF, EPUB and Kindle. Book excerpt:
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.
Book Synopsis Plasmin in Milk by : Eric Douglas Bastian
Download or read book Plasmin in Milk written by Eric Douglas Bastian and published by . This book was released on 1989 with total page 182 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis The Effects of Altering Temperature and PH of Skim Milk During Microfiltration on Casein Concentrates by : Jacquelyne R. Koch
Download or read book The Effects of Altering Temperature and PH of Skim Milk During Microfiltration on Casein Concentrates written by Jacquelyne R. Koch and published by . This book was released on 2011 with total page 258 pages. Available in PDF, EPUB and Kindle. Book excerpt:
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.
Book Synopsis The Contribution of Skim Milk and Cream Components to Thermally Induced Lipolysis in Cow's Milk by : Kay Burnette Fountain
Download or read book The Contribution of Skim Milk and Cream Components to Thermally Induced Lipolysis in Cow's Milk written by Kay Burnette Fountain and published by . This book was released on 1978 with total page 130 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Book Synopsis Microfiltration of Skim Milk to Separate Micellar Casein from Serum Protein by : Emily Elizabeth Hurt
Download or read book Microfiltration of Skim Milk to Separate Micellar Casein from Serum Protein written by Emily Elizabeth Hurt and published by . This book was released on 2010 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt:
