Relevant bibliographies by topics / Heat induced whey proteins fibrils

Academic literature 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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Journal articles on the topic "Heat induced whey proteins fibrils"

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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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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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Heat induced whey proteins fibrils"

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Lin, Yu-Min, and 林裕閔. "Studies on the Heat-Induced Interaction of Chicken Breast Muscle Salt-Soluble Proteins and Whey Proteins." Thesis, 2003. http://ndltd.ncl.edu.tw/handle/89051839748483490792.

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碩士
靜宜大學
食品營養研究所
91
The interactions between chicken breast muscle salt-soluble proteins (SSP) and whey protein concentrate (WPC) in 0.6M NaCl/0.05M sodium phosphate buffer (pH 7.0) under various protein concentrations (30mg/ml, 10mg/ml, 5mg/ml), mixed ratios (3:1, 1:1, 1:3) and heat treatments (unheated and 30-100℃, 20min) were investigated. SDS-Polyacrylamide gel electrophoresis technique was used to study the change of protein composition and formation of high molecular weight aggregates. When SSP and WPC were separately heated alone, the results revealted that obvious protein-protein interactions occurred at 50℃for SSP, while 80℃ for WPC. In the mixture of 30 mg/ml SSP and WPC at 1:3 ratio, the above proteins showed remarkable interactions at 90℃; and the phenomena were similar to the results of SSP and WPC heated alone. For the 1:1 mixtures of different protein concentrations, the degree of interactions and formation of large aggregate precipitates increased as protein concentration increased. Most of soluble high molecular weight aggregates formed via inter-molecular interactions could be dissociated with SDS and β-ME. Thus the interactions between proteins involved noncovalent bonds and disulfide bonds. Because the precipitates could be solubilized with urea and dissociated with SDS and β-ME, noncovalent bonds and disulfide bond were involved in the interactions between chicken breast muscle SSP and WPC. In addition, some of precipitates could not be dissociated, indicating the existence of covalent bonds.
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Liyanaarachchi, Winston. "Microparticulation of Dairy Proteins." Thesis, 2017. https://vuir.vu.edu.au/33172/.

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The formation of soluble, heat stable whey protein (WP) particles could be achieved via the inclusion of caseins. The aim of this study was to establish the effects of caseins on the properties of heat-induced WP aggregates.
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Patel, Hasmukh Ambalal. "Studies on heat- and pressure-induced interactions of milk proteins : a thesis presented in partial fulfilment of the requirements for the degree of Doctor of Philosophy in Food Technology at Massey University, Palmerston North, New Zealand." 2007. http://hdl.handle.net/10179/1606.

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The present study was aimed at understanding the high pressure (HP) processing-induced interactions of milk proteins in whey protein concentrate (WPC) solutions, in skim milk and in pure protein systems. The changes in milk proteins induced by heat treatments in the same systems under selected conditions were also evaluated. The main approach taken was to elucidate changes in the whey proteins in heat- and pressure-treated samples from common aliquots, under identical conditions, using various one-dimensional (1D) and two-dimensional (2D) polyacrylamide gel electrophoresis (PAGE) techniques in the absence or presence of a disulphide bond reducing agent. In some instances, the samples were also analysed using small deformation rheology, size exclusion chromatography (SEC) and transmission electron microscopy (TEM). The results of the present study indicated that, in general terms, heat treatment and HP treatment had common effects, i.e. denaturation and subsequent aggregation of whey proteins. Both heat treatment and HP treatment generated disulphide-bonded and hydrophobically bonded aggregates of whey proteins. However, the sensitivities of each of the whey proteins to heat treatment [immunoglobulin (Ig) > lactoferrin (LF) > bovine serum albumin (BSA) > β-laetoglobulin B (β-LG B) > β-LG A > α-lactalbumin (α-LA)] and pressure treatment (β-LG B > β-LG A > IgG > LF > BSA > α-LA) were considerably different. Also, HP treatment generated a comparatively greater proportion of smaller aggregates than did heat treatment. The effects of protein concentration, intensity of pressure treatment, holding time and pressurising temperature on whey protein aggregation in WPC solutions were investigated. The rate of aggregation of whey proteins increased with an increase in the concentration of protein in the WPC solution and the pressurising temperature. The combination of low protein concentration, mild pressure treatment (200 MPa) and low pressurising temperature (20°C) led to minimal loss of native-like and SDS-monomeric β-LG, whereas the combination of high protein concentration, severe pressure treatment (600 MPa) and higher pressuring temperature (40°C and higher) led to significant loss of both native-like and SDS-monomeric β-LG. The sensitivity of pressure-resistant whey proteins, such as α-LA and BSA, to the aggregation was significantly increased at pressurising temperatures of 40°C and higher. Self-supporting gels were formed when 8 or 12% (w/v) WPC solutions were pressure treated at 600-800 MPa. 20°C. Detailed analysis of the behaviour of the proteins during the formation of these gels revealed a novel pathway, suggesting that intermolecular disulphide bond formation occurred at high pressure but that hydrophobic association became important after the HP treatment. In the later part of the study, heat- and HP-induced interactions of caseins and whey proteins were studied in a more complex system, i.e. skim milk. With the application of modified PAGE techniques, it was possible to show that the high molecular weight disulphide-bonded aggregates that were formed by HP treatment of skim milk contained disulphide-linked complexes consisting of αS2-casein (αS2-CN) as well as κ-CN, β-LG and other whey proteins. The results showed that the effects of heat treatment and HP on the interactions of the caseins and whey proteins in milk were significantly different. The accessibility of αS2-CN and the formation of complexes involving αS2-CN, κ-CN and whey proteins in the HP-treated milk, as demonstrated using the modified 2D PAGE technique, and as explained by possible proposed reactions of the caseins and whey proteins in pressure-treated milk, was an important finding of the present study. Finally, a study on the effects of HP treatment in model systems using pure proteins in solution, both singly or in binary and ternary combinations, generated very useful information and clarified the role of each protein in pressure-induced aggregation and interactions of milk proteins in complex systems such as WPC and milk. It was found that the reactions of β-LG were not significantly affected by other proteins such as α-LA or BSA, but that the presence of β-LG in the system catalysed the reactions of other proteins such as α-LA or BSA.
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Book chapters on the topic "Heat induced whey proteins fibrils"

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Paulsson, M., and P. Dejmek. "Rheological Properties of Heat-Induced Whey Protein Gels." In Milk Proteins, 174–77. Heidelberg: Steinkopff, 1989. http://dx.doi.org/10.1007/978-3-642-85373-9_28.

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Brodkorb, André, Thomas Croguennec, Said Bouhallab, and Joseph J. Kehoe. "Heat-Induced Denaturation, Aggregation and Gelation of Whey Proteins." In Advanced Dairy Chemistry, 155–78. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-2800-2_6.

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Matsudomi, N., and T. Oshita. "The Role of α-Lactalbumin in Heat-Induced Gelation of Whey Proteins." In ACS Symposium Series, 93–103. Washington, DC: American Chemical Society, 1996. http://dx.doi.org/10.1021/bk-1996-0650.ch007.

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Gunasekaran, Sundaram, and Oscar Solar. "Heat-Induced Casein–Whey Protein Interactions." In Food Proteins and Peptides, 199–228. CRC Press, 2012. http://dx.doi.org/10.1201/b11768-9.

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Conference papers on the topic "Heat induced whey proteins fibrils"

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Lammers, Steven, Tosin Feyintola, Kendall Hunter, Emily Gibson, Tim Lei, Phil Kao, H. Jerry Qi, Craig Lanning, Robin Shandas, and Kurt Stenmark. "Microstructural Changes in Collagen and Elastin and Their Impact on the Mechanics of the Pulmonary Artery in Hypertension." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53958.

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In pulmonary arteries (PA), mechanical function is largely driven by the underlying microstructure of the structural proteins collagen and elastin, which reside within the extracellular matrix (ECM) of the arterial tissue. It has long been established that much of the mechanical non-linearity associated with arterial tissue is the result of collagen mechanics. Arterial collagen is arranged within the vascular wall as tortuous fibrils with a bulk fiber orientation of roughly helical configuration. When arterial tissue is deformed, these collagen fibers become straightened in the direction of applied load. At some critical deformation, termed the transition stretch (λTrans), collagen fibers begin to carry load, thus significantly altering material stiffness. This in turn gives rise to the non-linear force-stretch (F-λ) response typical of these tissues, Figure 1. We have recently found that λTrans is significantly reduced in the hypoxia-induced pulmonary hypertensive (PH) rat model. We therefore propose that this model constitutes an ideal system to study the effect of collagen microstructure on the mechanics of arterial tissues in response to PH vascular remodeling. We hypothesize that quantitative characterization of collagen microstructure will predict pulmonary artery (PA) λTrans within this model system. By directly relating collagen microstructural changes to bulk tissue mechanics in response to PH-induced vascular remodeling we can better understand how changes in collagen structure impact pulmonary hemodynamic capacitance, a major component of cardiac load and contributing factor to right heart failure.
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