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Journal articles on the topic 'Heat induced whey proteins fibrils'

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Published: 10 December 2022

Last updated: 28 January 2023

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1

Raman, Bakthisaran, Tadato Ban, Miyo Sakai, Saloni Y. Pasta, Tangirala Ramakrishna, Hironobu Naiki, Yuji Goto, and Ch Mohan Rao. "αB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid β-peptide and β2-microglobulin." Biochemical Journal 392, no. 3 (December 6, 2005): 573–81. http://dx.doi.org/10.1042/bj20050339.

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αB-crystallin, a small heat-shock protein, exhibits molecular chaperone activity. We have studied the effect of αB-crystallin on the fibril growth of the Aβ (amyloid β)-peptides Aβ-(1–40) and Aβ-(1–42). αB-crystallin, but not BSA or hen egg-white lysozyme, prevented the fibril growth of Aβ-(1–40), as revealed by thioflavin T binding, total internal reflection fluorescence microscopy and CD spectroscopy. Comparison of the activity of some mutants and chimaeric α-crystallins in preventing Aβ-(1–40) fibril growth with their previously reported chaperone ability in preventing dithiothreitol-induced aggregation of insulin suggests that there might be both common and distinct sites of interaction on α-crystallin involved in the prevention of amorphous aggregation of insulin and fibril growth of Aβ-(1–40). αB-crystallin also prevents the spontaneous fibril formation (without externally added seeds) of Aβ-(1–42), as well as the fibril growth of Aβ-(1–40) when seeded with the Aβ-(1–42) fibril seed. Sedimentation velocity measurements show that αB-crystallin does not form a stable complex with Aβ-(1–40). The mechanism by which it prevents the fibril growth differs from the known mechanism by which it prevents the amorphous aggregation of proteins. αB-crystallin binds to the amyloid fibrils of Aβ-(1–40), indicating that the preferential interaction of the chaperone with the fibril nucleus, which inhibits nucleation-dependent polymerization of amyloid fibrils, is the mechanism that is predominantly involved. We found that αB-crystallin prevents the fibril growth of β2-microglobulin under acidic conditions. It also retards the depolymerization of β2-microglobulin fibrils, indicating that it can interact with the fibrils. Our study sheds light on the role of small heat-shock proteins in protein conformational diseases, particularly in Alzheimer's disease.

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2

Rothbard, Jonathan B., Jesse J. Rothbard, Luis Soares, C. Garrison Fathman, and Lawrence Steinman. "Identification of a common immune regulatory pathway induced by small heat shock proteins, amyloid fibrils, and nicotine." Proceedings of the National Academy of Sciences 115, no. 27 (June 18, 2018): 7081–86. http://dx.doi.org/10.1073/pnas.1804599115.

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Although certain dogma portrays amyloid fibrils as drivers of neurodegenerative disease and neuroinflammation, we have found, paradoxically, that amyloid fibrils and small heat shock proteins (sHsps) are therapeutic in experimental autoimmune encephalomyelitis (EAE). They reduce clinical paralysis and induce immunosuppressive pathways, diminishing inflammation. A key question was the identification of the target for these molecules. When sHsps and amyloid fibrils were chemically cross-linked to immune cells, a limited number of proteins were precipitated, including the α7 nicotinic acetylcholine receptor (α7 NAChR). The α7 NAChR is noteworthy among the over 20 known receptors for amyloid fibrils, because it plays a central role in a well-defined immune-suppressive pathway. Competitive binding between amyloid fibrils and α-bungarotoxin to peritoneal macrophages (MΦs) confirmed the involvement of α7 NAChR. The mechanism of immune suppression was explored, and, similar to nicotine, amyloid fibrils inhibited LPS induction of a common set of inflammatory cytokines while inducing Stat3 signaling and autophagy. Consistent with this, previous studies have established that nicotine, sHsps, and amyloid fibrils all were effective therapeutics in EAE. Interestingly, B lymphocytes were needed for the therapeutic effect. These results suggest that agonists of α7 NAChR might have therapeutic benefit for a variety of inflammatory diseases.

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3

Stepanenko, Olga V., M. I. Sulatsky, E. V. Mikhailova, Olesya V. Stepanenko, O. I. Povarova, I. M. Kuznetsova, K. K. Turoverov, and A. I. Sulatskaya. "Alpha-B-Crystallin Effect on Mature Amyloid Fibrils: Different Degradation Mechanisms and Changes in Cytotoxicity." International Journal of Molecular Sciences 21, no. 20 (October 16, 2020): 7659. http://dx.doi.org/10.3390/ijms21207659.

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Given the ability of molecular chaperones and chaperone-like proteins to inhibit the formation of pathological amyloid fibrils, the chaperone-based therapy of amyloidosis has recently been proposed. However, since these diseases are often diagnosed at the stages when a large amount of amyloids is already accumulated in the patient’s body, in this work we pay attention to the undeservedly poorly studied problem of chaperone and chaperone-like proteins’ effect on mature amyloid fibrils. We showed that a heat shock protein alpha-B-crystallin, which is capable of inhibiting fibrillogenesis and is found in large quantities as a part of amyloid plaques, can induce degradation of mature amyloids by two different mechanisms. Under physiological conditions, alpha-B-crystallin induces fluffing and unweaving of amyloid fibrils, which leads to a partial decrease in their structural ordering without lowering their stability and can increase their cytotoxicity. We found a higher correlation between the rate and effectiveness of amyloids degradation with the size of fibrils clusters rather than with amino acid sequence of amyloidogenic protein. Some external effects (such as an increase in medium acidity) can lead to a change in the mechanism of fibrils degradation induced by alpha-B-crystallin: amyloid fibers are fragmented without changing their secondary structure and properties. According to recent data, fibrils cutting can lead to the generation of seeds for new bona fide amyloid fibrils and accelerate the accumulation of amyloids, as well as enhance the ability of fibrils to disrupt membranes and to reduce cell viability. Our results emphasize the need to test the chaperone effect not only on fibrillogenesis, but also on the mature amyloid fibrils, including stress conditions, in order to avoid undesirable disease progression during chaperone-based therapy.

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4

Kulig, Melissa, and Heath Ecroyd. "The small heat-shock protein αB-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of α-lactalbumin." Biochemical Journal 448, no. 3 (November 21, 2012): 343–52. http://dx.doi.org/10.1042/bj20121187.

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Stress conditions can destabilize proteins, promoting them to unfold and adopt intermediately folded states. Partially folded protein intermediates are unstable and prone to aggregation down off-folding pathways leading to the formation of either amorphous or amyloid fibril aggregates. The sHsp (small heat-shock protein) αB-crystallin acts as a molecular chaperone to prevent both amorphous and fibrillar protein aggregation; however, the precise molecular mechanisms behind its chaperone action are incompletely understood. To investigate whether the chaperone activity of αB-crystallin is dependent upon the form of aggregation (amorphous compared with fibrillar), bovine α-lactalbumin was developed as a model target protein that could be induced to aggregate down either off-folding pathway using comparable buffer conditions. Thus when α-lactalbumin was reduced it aggregated amorphously, whereas a reduced and carboxymethylated form aggregated to form amyloid fibrils. Using this model, αB-crystallin was shown to be a more efficient chaperone against amorphously aggregating α-lactalbumin than when it aggregated to form fibrils. Moreover, αB-crystallin forms high molecular mass complexes with α-lactalbumin to prevent its amorphous aggregation, but prevents fibril formation via weak transient interactions. Thus, the conformational stability of the protein intermediate, which is a precursor to aggregation, plays a critical role in modulating the chaperone mechanism of αB-crystallin.

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5

Winkler, Juliane, Jens Tyedmers, Bernd Bukau, and Axel Mogk. "Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation." Journal of Cell Biology 198, no. 3 (August 6, 2012): 387–404. http://dx.doi.org/10.1083/jcb.201201074.

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Hsp100 and Hsp70 chaperones in bacteria, yeast, and plants cooperate to reactivate aggregated proteins. Disaggregation relies on Hsp70 function and on ATP-dependent threading of aggregated polypeptides through the pore of the Hsp100 AAA+ hexamer. In yeast, both chaperones also promote propagation of prions by fibril fragmentation, but their functional interplay is controversial. Here, we demonstrate that Hsp70 chaperones were essential for species-specific targeting of their Hsp100 partner chaperones ClpB and Hsp104, respectively, to heat-induced protein aggregates in vivo. Hsp70 inactivation in yeast also abrogated Hsp104 targeting to almost all prions tested and reduced fibril mobility, which indicates that fibril fragmentation by Hsp104 requires Hsp70. The Sup35 prion was unique in allowing Hsp70-independent association of Hsp104 via its N-terminal domain, which, however, was nonproductive. Hsp104 overproduction even outcompeted Hsp70 for Sup35 prion binding, which explains why this condition prevented Sup35 fragmentation and caused prion curing. Our findings indicate a conserved mechanism of Hsp70–Hsp100 cooperation at the surface of protein aggregates and prion fibrils.

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6

Xu, Hong-Hua, Jing Wang, Shi-Rong Dong, Wen Cheng, Bao-Hua Kong, and Jun-Yan Tan. "Acid-responsive properties of fibrils from heat-induced whey protein concentrate." Journal of Dairy Science 99, no. 8 (August 2016): 6052–60. http://dx.doi.org/10.3168/jds.2015-10823.

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7

Wang, Jing, Hong Hua Xu, and Yan Xu. "Nanofibril Formation of Whey Protein Concentrate and their Properties of Fibril Dispersions." Advanced Materials Research 634-638 (January 2013): 1268–73. http://dx.doi.org/10.4028/www.scientific.net/amr.634-638.1268.

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Compared with β-lactoglobulin or WPI, the complex compositions for whey protein concentrate (WPC) impacted the nano-fibrils formation, the heat-induced conversion of WPC into fibrils needed alternative methods with lower pH and higher heating temperature. 3wt% WPC could form long semi-flexible fibrils with diameters from 24nm to 28nm by heating at 90°C, pH 1.8 for 10h. The major driving forces both fibrils (pH 1.8) and particulate aggregates (pH 6.5) from WPC were studied using transmission electron microscopy (TEM), turbidity, surface hydrophobicity and free sulfydryl group (-SH). The results indicated that surface hydrophobicity interaction played a dominant role in the formation of fibrils aggregates, while the disulphide bonds after heating to form fibrils aggregates at the acidic pH 1.8 was weaker than that of formation particulate aggregates at pH 6.5.

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8

Čurda, L., L. Belháčová, M. Uhrová, J. Štětina, and L. Fukal. "Assessment of heat-induced denaturation of whey proteins." Journal of Chromatography A 772, no. 1-2 (June 1997): 231–34. http://dx.doi.org/10.1016/s0021-9673(97)00100-3.

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9

Bolder, Suzanne G., Astrid J. Vasbinder, Leonard M. C. Sagis, and Erik van der Linden. "Heat-induced whey protein isolate fibrils: Conversion, hydrolysis, and disulphide bond formation." International Dairy Journal 17, no. 7 (July 2007): 846–53. http://dx.doi.org/10.1016/j.idairyj.2006.10.002.

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10

Zhang, Lina, Ruoya Zhou, Jinyue Zhang, and Peng Zhou. "Heat-induced denaturation and bioactivity changes of whey proteins." International Dairy Journal 123 (December 2021): 105175. http://dx.doi.org/10.1016/j.idairyj.2021.105175.

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11

Li, Quanyang, and Zhengtao Zhao. "Interaction between lactoferrin and whey proteins and its influence on the heat-induced gelation of whey proteins." Food Chemistry 252 (June 2018): 92–98. http://dx.doi.org/10.1016/j.foodchem.2018.01.114.

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12

Asaduzzaman, Md, Md Sultan Mahomud, and Mohammod Enamul Haque. "Heat-Induced Interaction of Milk Proteins: Impact on Yoghurt Structure." International Journal of Food Science 2021 (September 22, 2021): 1–10. http://dx.doi.org/10.1155/2021/5569917.

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Heating milk for yoghurt preparation has a significant effect on the structural properties of yoghurt. Milk heated at elevated temperature causes denaturation of whey protein, aggregation, and some case gelation. It is important to understand the mechanism involved in each state of stabilization for tailoring the final product. We review the formation of these complexes and their consequence on the physical, rheological, and microstructural properties of acid milk gels. To investigate the interactions between denatured whey protein and casein, the formation of covalent and noncovalent bonds, localization of the complexes, and their impact on ultimate gelation and final yoghurt texture are reviewed. The information regarding this fundamental mechanism will be beneficial to develop uniform quality yoghurt texture and potential interest of future research.

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13

O'Kennedy, Brendan T., and John S. Mounsey. "Control of Heat-Induced Aggregation of Whey Proteins Using Casein." Journal of Agricultural and Food Chemistry 54, no. 15 (July 2006): 5637–42. http://dx.doi.org/10.1021/jf0607866.

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14

Corredig, Milena, Edita Verespej, and Douglas G. Dalgleish. "Heat-Induced Changes in the Ultrasonic Properties of Whey Proteins." Journal of Agricultural and Food Chemistry 52, no. 14 (July 2004): 4465–71. http://dx.doi.org/10.1021/jf0354390.

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15

Chính Nghia, Nguyen, Vu Thu Trang, and Do Van Duong. "WHEY PROTEIN ADDITION TO FACILITATE ACCELERATION OF YOGHURT FERMENTATION." Vietnam Journal of Science and Technology 57, no. 3B (November 12, 2019): 69. http://dx.doi.org/10.15625/2525-2518/57/3b/14346.

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Whey proteins were present in appropriate proportion in milk, during heat-treatment at pasteurization temperatures; whey proteins and casein have the ability to form firm gel of uniform porosity through heat-induced protein-protein interactions. In this study, the addition of whey proteins in fresh milk were carry out to investigate whether whey protein would accelerate yoghurt fermentation time and facilitate the yoghurt structure. The results indicated that the addition of whey concentrate 80 increased the water retention capacity of the final product. Whey protein concentrate 80 supplement at the content of 0.8% shortened fermentation time for the product 12.5%. The addition of whey protein also improved the properties of water retention until 26%, viscosity and structure of yoghurt products.

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16

Regester, Geoffrey O., R. John Pearce, Victor W. K. Lee, and Michael E. Mangino. "Heat-related changes to the hydrophobicity of cheese whey correlate with levels of native β-lactoglobulin and α-lactalbumin." Journal of Dairy Research 59, no. 4 (November 1992): 527–32. http://dx.doi.org/10.1017/s0022029900027199.

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SummaryCorrelations were identified between levels of the native whey proteins, β-lactoglobulin and α-lactalbumin and the surface and total hydrophobicities of cheese whey in response to different heat treatments. Heat-induced changes in the native βlactoglobulin content and surface hydrophobicity of whey exhibited the most significant linear relationship while correlations between total hydrophobicity and the native proteins were less significant because of an atypical rise in the n−heptane-binding capacity of whey after high-temperature treatment. The content of native β-lactoglobulin in whey was more sensitive to heating than the content of native α-lactalbumin, while heat-related changes in the total hydrophobicity of whey were generally greater than similar changes in surface hydrophobicity.

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17

SCHORSCH, CATHERINE, DEBORAH K. WILKINS, MALCOLM G. JONES, and IAN T. NORTON. "Gelation of casein-whey mixtures: effects of heating whey proteins alone or in the presence of casein micelles." Journal of Dairy Research 68, no. 3 (August 2001): 471–81. http://dx.doi.org/10.1017/s0022029901004915.

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The aim of the present work was to investigate the role of whey protein denaturation on the acid induced gelation of casein. This was studied by determining the effect of whey protein denaturation both in the presence and absence of casein micelles. The study showed that milk gelation kinetics and gel properties are greatly influenced by the heat treatment sequence. When the whey proteins are denatured separately and subsequently added to casein micelles, acid-induced gelation occurs more rapidly and leads to gels with a more particulated microstructure than gels made from co-heated systems. The gels resulting from heat-treatment of a mixture of pre-denatured whey protein with casein micelles are heterogeneous in nature due to particulates formed from casein micelles which are complexed with denatured whey proteins and also from separate whey protein aggregates. Whey proteins thus offer an opportunity not only to control casein gelation but also to control the level of syneresis, which can occur.

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18

PAULSSON, MARIE, PER-OLOF HEGG, and HELGE B. CASTBERG. "Heat-Induced Gelation of Individual Whey Proteins A Dynamic Rheological Study." Journal of Food Science 51, no. 1 (January 1986): 87–90. http://dx.doi.org/10.1111/j.1365-2621.1986.tb10842.x.

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19

Surel, Olivier, and Marie-Hélène Famelart. "Heat induced gelation of acid milk: balance between weak and covalent bonds." Journal of Dairy Research 70, no. 2 (May 2003): 253–56. http://dx.doi.org/10.1017/s0022029903006174.

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Gelation of acidified milk at pH[ges ]5, after heat treatments is a well known phenomenon, due to the precipitation of whey proteins, and especially β-lactoglobulin onto κ-casein (Sawyer, 1969). High heat treatments cause denaturation of whey proteins which associate with κ-casein through disulphide interchange reactions (Hill, 1989). Since their charge is reduced, the denatured proteins associated with casein micelles become susceptible to aggregation when milk is then acidified, which promotes enhanced protein–protein interactions (Lucey et al. 1997). The gelation phenomenon involves disulphide bonds (Hashizume & Sato, 1988; Goddard, 1996) which are responsible for the gel firmness (Goddard, 1996). However, other interactions between proteins can occur, such as hydrogen and hydrophobic bonds, especially at the initial stage of interactions (Haque et al. 1987; Haque & Kinsella, 1988; Jang & Swaisgood, 1990). It is therefore relevant to investigate a possible contribution of weak linkages to the gel structure and firmness.

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20

Oldfield, David J., Harjinder Singh, and Mike W. Taylor. "Kinetics of heat-induced whey protein denaturation and aggregation in skim milks with adjusted whey protein concentration." Journal of Dairy Research 72, no. 3 (May 23, 2005): 369–78. http://dx.doi.org/10.1017/s002202990500107x.

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Microfiltration and ultrafiltration were used to manufacture skim milks with an increased or reduced concentration of whey proteins, while keeping the casein and milk salts concentrations constant. The skim milks were heated on a pilot-scale UHT plant at 80, 90 and 120 °C. The heat-induced denaturation and aggregation of β-lactoglobulin (β-lg), α-lactalbumin (α-la) and bovine serum albumin (BSA) were quantified by polyacrylamide gel electrophoresis. Apparent rate constants and reaction orders were calculated for β-lg, α-la and BSA denaturation. Rates of β-lg, α-la and BSA denaturation increased with increasing whey protein concentration. The rate of α-la and BSA denaturation was affected to a greater extent than β-lg by the change in whey protein concentration. After heating at 120 °C for 160 s, the concentration of β-lg and α-la associated with the casein micelles increased as the initial concentration of whey proteins increased.

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21

Norwood, Eve-Anne, Marie Chevallier, Cécile Le Floch-Fouéré, Pierre Schuck, Romain Jeantet, and Thomas Croguennec. "Heat-Induced Aggregation Properties of Whey Proteins as Affected by Storage Conditions of Whey Protein Isolate Powders." Food and Bioprocess Technology 9, no. 6 (February 4, 2016): 993–1001. http://dx.doi.org/10.1007/s11947-016-1686-1.

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22

Ainis, William Nicholas, Carsten Ersch, and Richard Ipsen. "Partial replacement of whey proteins by rapeseed proteins in heat-induced gelled systems: Effect of pH." Food Hydrocolloids 77 (April 2018): 397–406. http://dx.doi.org/10.1016/j.foodhyd.2017.10.016.

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23

Guralnick, Jacob R., Ram R. Panthi, Valeria L. Cenini, Vinay S. N. Mishra, Barry M. G. O’Hagan, Shane V. Crowley, and James A. O’Mahony. "Rehydration Properties of Whey Protein Isolate Powders Containing Nanoparticulated Proteins." Dairy 2, no. 4 (October 27, 2021): 602–16. http://dx.doi.org/10.3390/dairy2040047.

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The rehydration properties of original whey protein isolate (WPIC) powder and spray-dried WPI prepared from either unheated (WPIUH) or nanoparticulated WPI solutions were investigated. Nanoparticulation of whey proteins was achieved by subjecting reconstituted WPIC solutions (10% protein, w/w, pH 7.0) to heat treatment at 90 °C for 30 s with no added calcium (WPIH) or with 2.5 mM added calcium (WPIHCa). Powder surface nanostructure and elemental composition were investigated using atomic force microscopy and X-ray photoelectron spectroscopy, followed by dynamic visualisation of wetting and dissolution characteristics using environmental scanning electron microscopy. The surface of powder particles for both WPIUH and WPIC samples generally appeared smooth, while WPIH and WPIHCa displayed micro-wrinkles with more significant deposition of nitrogen and calcium elements. WPIH and WPIHCa exhibited lower wettability and solubility performance than WPIUH and WPIC during microscopic observation. This study demonstrated that heat-induced aggregation of whey proteins, in the presence or absence of added calcium, before drying increases aggregate size, alters the powder surface properties, consequently impairing their wetting characteristics. This study also developed a fundamental understanding of WPI powder obtained from nanoparticulated whey proteins, which could be applied for the development of functional whey-based ingredients in food formulations, such as nanospacers to modulate protein–protein interactions in dairy concentrates.

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24

Cornacchia, Leonardo, Cécile Forquenot de la Fortelle, and Paul Venema. "Heat-Induced Aggregation of Whey Proteins in Aqueous Solutions below Their Isoelectric Point." Journal of Agricultural and Food Chemistry 62, no. 3 (January 8, 2014): 733–41. http://dx.doi.org/10.1021/jf404456q.

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25

Roesch, Rodrigo R., and Milena Corredig. "Heat-Induced Soy−Whey Proteins Interactions: Formation of Soluble and Insoluble Protein Complexes." Journal of Agricultural and Food Chemistry 53, no. 9 (May 2005): 3476–82. http://dx.doi.org/10.1021/jf048870d.

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26

Gao, Feng, Xuefei Zhang, Jiaqi Wang, Xiaomeng Sun, and Cuina Wang. "Systematical characterization of functional and antioxidative properties of heat-induced polymerized whey proteins." Food Science and Biotechnology 27, no. 6 (June 1, 2018): 1619–26. http://dx.doi.org/10.1007/s10068-018-0402-5.

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27

Gulzar, Muhammad, and Jean Christophe Jacquier. "Impact of Residual Lactose on Dry Heat-Induced Pre-texturization of Whey Proteins." Food and Bioprocess Technology 11, no. 11 (August 8, 2018): 1985–94. http://dx.doi.org/10.1007/s11947-018-2162-x.

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28

Calvo, Marta M., Jeffrey Leaver, and Jean M. Banks. "Influence of other whey proteins on the heat-induced aggregation of α-lactalbumin." International Dairy Journal 3, no. 8 (January 1993): 719–27. http://dx.doi.org/10.1016/0958-6946(93)90085-e.

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29

Gulzar, Muhammad, Saïd Bouhallab, Romain Jeantet, Pierre Schuck, and Thomas Croguennec. "Influence of pH on the dry heat-induced denaturation/aggregation of whey proteins." Food Chemistry 129, no. 1 (November 2011): 110–16. http://dx.doi.org/10.1016/j.foodchem.2011.04.037.

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30

Anema, Skelte G., and Yuming Li. "Association of denatured whey proteins with casein micelles in heated reconstituted skim milk and its effect on casein micelle size." Journal of Dairy Research 70, no. 1 (February 2003): 73–83. http://dx.doi.org/10.1017/s0022029902005903.

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When skim milk at pH 6·55 was heated (75 to 100 °C for up to 60 min), the casein micelle size, as monitored by photon correlation spectroscopy, was found to increase during the initial stages of heating and tended to plateau on prolonged heating. At any particular temperature, the casein micelle size increased with longer holding times, and, at any particular holding time, the casein micelle size increased with increasing temperature. The maximum increase in casein micelle size was about 30–35 nm. The changes in casein micelle size were poorly correlated with the level of whey protein denaturation. However, the changes in casein micelle size were highly correlated with the levels of denatured whey proteins that were associated with the casein micelles. The rate of association of the denatured whey proteins with the casein micelles was considerably slower than the rate of denaturation of the whey proteins. Removal of the whey proteins from the skim milk resulted in only small changes in casein micelle size during heating. Re-addition of β-lactoglobulin to the whey-protein-depleted milk caused the casein micelle size to increase markedly on heat treatment. The changes in casein micelle size induced by the heat treatment of skim milk may be a consequence of the whey proteins associating with the casein micelles. However, these associated whey proteins would need to occlude a large amount of serum to account for the particle size changes. Separate experiments showed that the viscosity changes of heated milk and the estimated volume fraction changes were consistent with the particle size changes observed. Further studies are needed to determine whether the changes in size are due to the specific association of whey proteins with the micelles or whether a low level of aggregation of the casein micelles accompanies this association behaviour. Preliminary studies indicated lower levels of denatured whey proteins associated with the casein micelles and smaller changes in casein micelle size occurred as the pH of the milk was increased from pH 6·5 to pH 6·7.

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31

Xu, Weiyi, Shenghua He, Ying Ma, Yixin Zhang, and Rongchun Wang. "Effect of the heat-induced whey proteins/κ-casein complex on the acid gelation of yak milk." RSC Advances 5, no. 12 (2015): 8952–56. http://dx.doi.org/10.1039/c4ra14432e.

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32

Mottar, J., A. Bassier, M. Joniau, and J. Baert. "Effect of Heat-Induced Association of Whey Proteins and Casein Micelles on Yogurt Texture." Journal of Dairy Science 72, no. 9 (September 1989): 2247–56. http://dx.doi.org/10.3168/jds.s0022-0302(89)79355-3.

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33

Anema, Skelte G. "Heat-induced changes in caseins and casein micelles, including interactions with denatured whey proteins." International Dairy Journal 122 (November 2021): 105136. http://dx.doi.org/10.1016/j.idairyj.2021.105136.

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34

Stevenson, E. M., A. J. R. Law, and J. Leaver. "Heat-Induced Aggregation of Whey Proteins Is Enhanced by Addition of Thiolated β-Casein." Journal of Agricultural and Food Chemistry 44, no. 9 (January 1996): 2825–28. http://dx.doi.org/10.1021/jf950798j.

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35

de la Fuente, Miguel Angel, Harjinder Singh, and Yacine Hemar. "Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins." Trends in Food Science & Technology 13, no. 8 (August 2002): 262–74. http://dx.doi.org/10.1016/s0924-2244(02)00133-4.

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36

Liyanaarachchi, W. S., L. Ramchandran, and T. Vasiljevic. "Controlling heat induced aggregation of whey proteins by casein inclusion in concentrated protein dispersions." International Dairy Journal 44 (May 2015): 21–30. http://dx.doi.org/10.1016/j.idairyj.2014.12.010.

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37

Dannenberg, Frank, and Heinz G. Kessler. "Quantitative densitometry of heat-induced changes in whey proteins following ultrathin-layer isoelectric focusing." Electrophoresis 7, no. 2 (1986): 67–72. http://dx.doi.org/10.1002/elps.1150070203.

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38

WARD, BRENT R., SIMON J. GODDARD, MARY-ANN AUGUSTIN, and IAN R. McKINNON. "EDTA-induced dissociation of casein micelles and its effect on foaming properties of milk." Journal of Dairy Research 64, no. 4 (November 1997): 495–504. http://dx.doi.org/10.1017/s0022029997002367.

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The effects of addition of EDTA on the dissociation of caseins and foaming properties of milks (100 g solids/l) reconstituted from skim milk powders given a low-heat (72°C for 30 s) or high-heat (85°C for 30 min) treatment during powder manufacture were determined. The EDTA-induced dissociation of caseins was independent of heat treatment but in high-heat milk was accompanied by release of denatured whey proteins. EDTA changed the proportions of individual caseins in the supernatant. EDTA addition improved both foam overrun and foam stability of low- and high-heat milks. The increase in serum protein on addition of EDTA contributed to the improvement in foaming properties of milks by increasing the availability of the proteins for formation of the air–water interface.

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39

Elliott, Anthony J., Nivedita Datta, Boka Amenu, and Hilton C. Deeth. "Heat-induced and other chemical changes in commercial UHT milks." Journal of Dairy Research 72, no. 4 (September 15, 2005): 442–46. http://dx.doi.org/10.1017/s002202990500138x.

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The properties of commercial directly and indirectly heated UHT milks, both after heating and during storage at room temperature for 24 weeks, were studied. Thermally induced changes were examined by changes in lactulose, furosine and acid-soluble whey proteins. The results confirmed previous reports that directly heated UHT milks suffer less heat damage than indirectly heated milk. During storage, furosine increased and bovine serum albumin in directly heat-treated milks decreased significantly. The changes in lactulose, α-lactalbumin and β-lactoglobulin were not statistically significant. The data suggest that heat treatment indicators should be measured as soon as possible after processing to avoid any misinterpretations of the intensity of the heat treatment.

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40

Corredig, Milena, and Douglas G. Dalgleish. "The mechanisms of the heat-induced interaction of whey proteins with casein micelles in milk." International Dairy Journal 9, no. 3-6 (March 1999): 233–36. http://dx.doi.org/10.1016/s0958-6946(99)00066-7.

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41

Guyomarc'h, Fanny, Merveille Nono, Taco Nicolai, and Dominique Durand. "Heat-induced aggregation of whey proteins in the presence of κ-casein or sodium caseinate." Food Hydrocolloids 23, no. 4 (June 2009): 1103–10. http://dx.doi.org/10.1016/j.foodhyd.2008.07.001.

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42

Peterson, J. B., J. E. Heuser, and D. L. Nelson. "Dissociation and reassociation of trichocyst proteins: biochemical and ultrastructural studies." Journal of Cell Science 87, no. 1 (February 1, 1987): 3–25. http://dx.doi.org/10.1242/jcs.87.1.3.

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Trichocysts, the crystalline exocytotic organelles in Paramecium tetraurelia, are composed of small, acidic proteins existing primarily as disulphide-linked dimers. We have disaggregated trichocyst proteins with heat, simultaneously observing the changes in morphology and protein composition. The tip matrix was most heat-labile; its subunits progressively broke away from the distal end. During this process, breakdown of the cylindrical shaft began. Shafts first became flattened and torn lengthwise, yielding smaller, interconnected pieces still having the crystalline arrangement of their 5 nm thick fibres. Ultimately this pattern became disordered, and discrete fibrils of the same thickness disengaged from the meshwork. In freeze-etched preparations these fibrils were composed of thinner filaments in side-by-side association. Disaggregation of the tip sheath began from the distal end before shaft dissociation was complete. Trichocysts broke down to thin fibrils, but probably not to monomeric subunits. At least three proteins were preferentially released in the initial phase of dissociation. Disulphide-reducing agent present during heating increased the rate of dissociation without altering the sequence of morphological changes or the order of release of individual proteins. The rate and extent of heat-induced dissociation were strongly dependent on pH and cation concentration. The stabilizing effects of low pH and of cations were additive. A cooled suspension of fully dissociated trichocysts reassociated into sedimentable aggregates with discernible filamentous order, but without the crystalline structure of intact trichocysts. Reassociation was dependent upon time, temperature and protein concentration. All but one of the trichocyst proteins re-entered the sedimentable aggregate during reassociation. Reassociation was faster and more complete at pH 6 than at pH 8 and was stimulated by Ca2+, Mg2+ and La3+. Trichocyst proteins dissociated in the presence of dithiothreitol did not reassociate, even after removal of the reducing agent. Trichocysts from mutants defective to varying degrees in trichocyst formation were subjected to similar experimental protocols. Heat-dissociated trichocysts of the mutants scc6 and ptA1 reassociated at rates similar to those of wild-type; ftA3 showed slower reassociation, and tam38 showed little or no reassociation. Reassociation of wild-type trichocyst proteins was blocked by the addition of an equal amount of tam38 trichocyst proteins.(ABSTRACT TRUNCATED AT 400 WORDS)

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43

Warncke, Malou, Sonja Keienburg, and Ulrich Kulozik. "Cold-Renneted Milk Powders for Cheese Production: Impact of Casein/Whey Protein Ratio and Heat on the Gelling Behavior of Reconstituted Rennet Gels and on the Survival Rate of Integrated Lactic Acid Bacteria." Foods 10, no. 7 (July 11, 2021): 1606. http://dx.doi.org/10.3390/foods10071606.

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The idea was to develop powders for fresh/hard cheese or quark production comprising milk proteins in optimal composition and functional properties for manufacturing each of those cheese types. The aim was to avoid whey protein drainage by their prior removal or by their heat-induced structural integration in the curd. The pre-renneted powders already contain additives such as starter cultures and calcium chloride to instantaneously form homogeneous curds upon reconstitution. The impact of the casein/whey protein ratio (86:14 by ultrafiltration and 98:2 by microfiltration) and upfront heat treatment (80 °C/30 min) on the gelling behavior of reconstituted rennet gels and on the survival rate of integrated Lactobacillus paracasei ssp. paracasei F19 was investigated. The assessment criteria for the rennet gelation were curd firming rate, gel strength, and whey drainage. Furthermore, the amount of integrated whey proteins and the resulting cheese yield were evaluated. It could be shown that heating had a positive effect on the viable cell count of the bacteria after spray drying and on the gelation behavior of the reconstituted ultrafiltration concentrates. The curd firming rate and the gel strength could be increased to higher values than the reconstituted microfiltration concentrate at 25% total solids.

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44

Ikeda, Shinya. "Heat-induced gelation of whey proteins observed by rheology, atomic force microscopy, and Raman scattering spectroscopy." Food Hydrocolloids 17, no. 4 (July 2003): 399–406. http://dx.doi.org/10.1016/s0268-005x(03)00033-x.

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45

Abd El-Fattah, Alaa, Samia El-Dieb, and Hany Elkashef. "Development of functional egg-free flan using whey proteins and evaluation of heat-induced gel properties." Journal of Food Measurement and Characterization 13, no. 4 (June 28, 2019): 2828–36. http://dx.doi.org/10.1007/s11694-019-00203-7.

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46

Dominguez, Angella Velazquez, and Taco Nicolai. "Heat induced gelation of micellar casein with and without whey proteins in the presence of polyphosphate." International Dairy Journal 104 (May 2020): 104640. http://dx.doi.org/10.1016/j.idairyj.2020.104640.

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47

Rodríguez Arzuaga, Mariana, Alejandra Bosch, María Cristina Añón, and Analía Graciela Abraham. "Heat induced conformational changes of whey proteins in model infant formulae: Effect of casein and inulin." International Dairy Journal 105 (June 2020): 104695. http://dx.doi.org/10.1016/j.idairyj.2020.104695.

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48

Stănciuc, Nicoleta, Loredana Dumitraşcu, Alina Ardelean, Silvius Stanciu, and Gabriela Râpeanu. "A Kinetic Study on the Heat-Induced Changes of Whey Proteins Concentrate at Two pH Values." Food and Bioprocess Technology 5, no. 6 (May 11, 2011): 2160–71. http://dx.doi.org/10.1007/s11947-011-0590-y.

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49

Corredig, Milena, and Douglas G. Dalgleish. "Effect of different heat treatments on the strong binding interactions between whey proteins and milk fat globules in whole milk." Journal of Dairy Research 63, no. 3 (August 1996): 441–49. http://dx.doi.org/10.1017/s0022029900031940.

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SummaryThe heat-induced binding of whey proteins to milk fat globule membranes in whole milk was investigated by quantitative electrophoresis and laser scanning densitometry. Both α-lactalbumin and β-lactoglobulin bound to the surfaces of fat globules when milk was heated in a water bath in the temperature range 65–85 °C. The interaction behaviour of α-lactalbumin did not seem to change with temperature, and the total amount of protein bound was ∼ 0·2 mg/g fat contained in the cream. The quantity of βlactoglobulin interacting with the milk fat globules increased with temperature from 02 to 0·7 mg/g fat between 65° and 85 °C. Even in whole milk heated at batch pasteurization temperatures (60–65 °C), α-lactalbumin and β-lactoglobulin were found attached to the fat globules. The interactions of the whey proteins with intact fat globule membranes were also investigated in milk heated in an industrial system (a pilot scale UHT and high temperature short time module), and the results were compared with those from the laboratory treatment (simple batch heating). The binding of the whey proteins to fat globules differed between milk heated by UHT using indirect steam heating or direct steam injection (DSI). However, the surface load in milk treated by DSI was not comparable to that of milk treated by batch heating or indirect steam heating, because of the changes in fat globule size and membrane composition caused by the DSI process.

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50

Singh, Tanoj K., Sofia K. Øiseth, Leif Lundin, and Li Day. "Influence of heat and shear induced protein aggregation on the in vitro digestion rate of whey proteins." Food Funct. 5, no. 11 (2014): 2686–98. http://dx.doi.org/10.1039/c4fo00454j.

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