Journal articles on the topic 'Β-lactoglobulin fibrils'
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Gowda, Vasantha, Michal Biler, Andrei Filippov, Malisa V. Mantonico, Eirini Ornithopoulou, Mathieu Linares, Oleg N. Antzutkin, and Christofer Lendel. "Structural characterisation of amyloid-like fibrils formed by an amyloidogenic peptide segment of β-lactoglobulin." RSC Advances 11, no. 45 (2021): 27868–79. http://dx.doi.org/10.1039/d1ra03575d.
Full textGosal, Walraj S., Simon B. Ross-Murphy, Paul D. A. Pudney, and Allan H. Clark. "Characterisation of amyloid fibrils formed from β-lactoglobulin." Biochemical Society Transactions 30, no. 3 (June 1, 2002): A83. http://dx.doi.org/10.1042/bst030a083.
Full textJones, Owen G., Stephan Handschin, Jozef Adamcik, Ludger Harnau, Sreenath Bolisetty, and Raffaele Mezzenga. "Complexation of β-Lactoglobulin Fibrils and Sulfated Polysaccharides." Biomacromolecules 12, no. 8 (August 8, 2011): 3056–65. http://dx.doi.org/10.1021/bm200686r.
Full textArnaudov, Luben N., Renko de Vries, Hans Ippel, and Carlo P. M. van Mierlo. "Multiple Steps during the Formation of β-Lactoglobulin Fibrils." Biomacromolecules 4, no. 6 (November 2003): 1614–22. http://dx.doi.org/10.1021/bm034096b.
Full textRabe, Rebecca, Ute Hempel, Laurine Martocq, Julia K. Keppler, Jenny Aveyard, and Timothy E. L. Douglas. "Dairy-Inspired Coatings for Bone Implants from Whey Protein Isolate-Derived Self-Assembled Fibrils." International Journal of Molecular Sciences 21, no. 15 (August 3, 2020): 5544. http://dx.doi.org/10.3390/ijms21155544.
Full textMa, Baoliang, Wen Li, Xudong Zhu, Guiling Liu, Fan Zhang, Fang Wu, Xiping Jiang, and Jinbing Xie. "Folic acid inhibits the amyloid fibrils formation of β-lactoglobulin." European Journal of BioMedical Research 1, no. 1 (February 10, 2017): 22. http://dx.doi.org/10.18088/ejbmr.1.1.2015.pp22-27.
Full textChen, Da, Lorena Silva Pinho, Enrico Federici, Xiaobing Zuo, Jan Ilavsky, Ivan Kuzmenko, Zhi Yang, Owen Griffith Jones, and Osvaldo Campanella. "Heat accelerates degradation of β-lactoglobulin fibrils at neutral pH." Food Hydrocolloids 124 (March 2022): 107291. http://dx.doi.org/10.1016/j.foodhyd.2021.107291.
Full textDunstan, Dave E., Paul Hamilton-Brown, Peter Asimakis, William Ducker, and Joseph Bertolini. "Shear-induced structure and mechanics of β-lactoglobulin amyloid fibrils." Soft Matter 5, no. 24 (2009): 5020. http://dx.doi.org/10.1039/b914089a.
Full textPeng, Dengfeng, Jinchu Yang, Jing Li, Cuie Tang, and Bin Li. "Foams Stabilized by β-Lactoglobulin Amyloid Fibrils: Effect of pH." Journal of Agricultural and Food Chemistry 65, no. 48 (November 28, 2017): 10658–65. http://dx.doi.org/10.1021/acs.jafc.7b03669.
Full textAkkermans, Cynthia, Paul Venema, Atze Jan van der Goot, Remko M. Boom, and Erik van der Linden. "Enzyme-Induced Formation of β-Lactoglobulin Fibrils by AspN Endoproteinase." Food Biophysics 3, no. 4 (August 13, 2008): 390–94. http://dx.doi.org/10.1007/s11483-008-9094-3.
Full textWang, 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.
Full textBateman, Libei, Aiqian Ye, and Harjinder Singh. "Re-formation of Fibrils from Hydrolysates of β-Lactoglobulin Fibrils during in Vitro Gastric Digestion." Journal of Agricultural and Food Chemistry 59, no. 17 (September 14, 2011): 9605–11. http://dx.doi.org/10.1021/jf2020057.
Full textKroes-Nijboer, Ardy, Yvette S. Lubbersen, Paul Venema, and Erik van der Linden. "Thioflavin T fluorescence assay for β-lactoglobulin fibrils hindered by DAPH." Journal of Structural Biology 165, no. 3 (March 2009): 140–45. http://dx.doi.org/10.1016/j.jsb.2008.11.003.
Full textBolder, Suzanne G., Hanneke Hendrickx, Leonard M. C. Sagis, and Erik van der Linden. "Ca2+-Induced Cold-Set Gelation of Whey Protein Isolate Fibrils." Applied Rheology 16, no. 5 (October 1, 2006): 258–64. http://dx.doi.org/10.1515/arh-2006-0018.
Full textBolisetty, Sreenath, Jozef Adamcik, and Raffaele Mezzenga. "Snapshots of fibrillation and aggregation kinetics in multistranded amyloid β-lactoglobulin fibrils." Soft Matter 7, no. 2 (2011): 493–99. http://dx.doi.org/10.1039/c0sm00502a.
Full textGilbert, Jay, Osvaldo Campanella, and Owen G. Jones. "Electrostatic Stabilization of β-lactoglobulin Fibrils at Increased pH with Cationic Polymers." Biomacromolecules 15, no. 8 (July 22, 2014): 3119–27. http://dx.doi.org/10.1021/bm500762u.
Full textWu, Xiaoli, Katsuyoshi Nishinari, Zhiming Gao, Meng Zhao, Ke Zhang, Yapeng Fang, Glyn O. Phillips, and Fatang Jiang. "Gelation of β-lactoglobulin and its fibrils in the presence of transglutaminase." Food Hydrocolloids 52 (January 2016): 942–51. http://dx.doi.org/10.1016/j.foodhyd.2015.09.012.
Full textCarbonaro, M., A. Di Venere, A. Filabozzi, P. Maselli, V. Minicozzi, S. Morante, E. Nicolai, A. Nucara, E. Placidi, and F. Stellato. "Role of dietary antioxidant (−)-epicatechin in the development of β-lactoglobulin fibrils." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1864, no. 7 (July 2016): 766–72. http://dx.doi.org/10.1016/j.bbapap.2016.03.017.
Full textRaynes, Jared K., Li Day, Pauline Crepin, Mathew H. Horrocks, and John A. Carver. "Coaggregation of κ-Casein and β-Lactoglobulin Produces Morphologically Distinct Amyloid Fibrils." Small 13, no. 14 (February 1, 2017): 1603591. http://dx.doi.org/10.1002/smll.201603591.
Full textBolisetty, Sreenath, Jijo J. Vallooran, Jozef Adamcik, and Raffaele Mezzenga. "Magnetic-Responsive Hybrids of Fe3O4 Nanoparticles with β-Lactoglobulin Amyloid Fibrils and Nanoclusters." ACS Nano 7, no. 7 (June 14, 2013): 6146–55. http://dx.doi.org/10.1021/nn401988m.
Full textJurado, Rocío, and Natividad Gálvez. "Apoferritin Amyloid-Fibril Directed the In Situ Assembly and/or Synthesis of Optical and Magnetic Nanoparticles." Nanomaterials 11, no. 1 (January 8, 2021): 146. http://dx.doi.org/10.3390/nano11010146.
Full textJurado, Rocío, and Natividad Gálvez. "Apoferritin Amyloid-Fibril Directed the In Situ Assembly and/or Synthesis of Optical and Magnetic Nanoparticles." Nanomaterials 11, no. 1 (January 8, 2021): 146. http://dx.doi.org/10.3390/nano11010146.
Full textPan, Shiyu, Zhihui Zhai, Kai Yang, Yao Xiang, Shoufeng Tang, Yating Zhang, Tifeng Jiao, Qingrui Zhang, and Deling Yuan. "β-Lactoglobulin amyloid fibrils supported Fe(III) to activate peroxydisulfate for organic pollutants elimination." Separation and Purification Technology 289 (May 2022): 120806. http://dx.doi.org/10.1016/j.seppur.2022.120806.
Full textDave, Anant C., Simon M. Loveday, Skelte G. Anema, Trevor S. Loo, Gillian E. Norris, Geoffrey B. Jameson, and Harjinder Singh. "β-Lactoglobulin Self-Assembly: Structural Changes in Early Stages and Disulfide Bonding in Fibrils." Journal of Agricultural and Food Chemistry 61, no. 32 (August 5, 2013): 7817–28. http://dx.doi.org/10.1021/jf401084f.
Full textBateman, Libei, Aiqian Ye, and Harjinder Singh. "In Vitro Digestion of β-Lactoglobulin Fibrils Formed by Heat Treatment at Low pH." Journal of Agricultural and Food Chemistry 58, no. 17 (September 8, 2010): 9800–9808. http://dx.doi.org/10.1021/jf101722t.
Full textRogers, S. S., P. Venema, J. P. M. van der Ploeg, E. van der Linden, L. M. C. Sagis, and A. M. Donald. "Investigating the permanent electric dipole moment of β-lactoglobulin fibrils, using transient electric birefringence." Biopolymers 82, no. 3 (June 15, 2006): 241–52. http://dx.doi.org/10.1002/bip.20483.
Full textChang, Hon Weng, Tai Boon Tan, Phui Yee Tan, Imededdine Arbi Nehdi, Hassen Mohamed Sbihi, and Chin Ping Tan. "Microencapsulation of fish oil-in-water emulsion using thiol-modified β-lactoglobulin fibrils-chitosan complex." Journal of Food Engineering 264 (January 2020): 109680. http://dx.doi.org/10.1016/j.jfoodeng.2019.07.027.
Full textDave, Anant C., Simon M. Loveday, Skelte G. Anema, Geoffrey B. Jameson, and Harjinder Singh. "Formation of nano-fibrils from the A, B and C variants of bovine β-lactoglobulin." International Dairy Journal 41 (February 2015): 64–67. http://dx.doi.org/10.1016/j.idairyj.2014.09.011.
Full textBolisetty, Sreenath, Ludger Harnau, Jin-mi Jung, and Raffaele Mezzenga. "Gelation, Phase Behavior, and Dynamics of β-Lactoglobulin Amyloid Fibrils at Varying Concentrations and Ionic Strengths." Biomacromolecules 13, no. 10 (September 7, 2012): 3241–52. http://dx.doi.org/10.1021/bm301005w.
Full textSerfert, Y., C. Lamprecht, C. P. Tan, J. K. Keppler, E. Appel, F. J. Rossier-Miranda, K. Schroen, et al. "Characterisation and use of β-lactoglobulin fibrils for microencapsulation of lipophilic ingredients and oxidative stability thereof." Journal of Food Engineering 143 (December 2014): 53–61. http://dx.doi.org/10.1016/j.jfoodeng.2014.06.026.
Full textSasaki, Naoki, Yuna Saitoh, Rajesh Kumar Sharma, and Kazuya Furusawa. "Determination of the elastic modulus of β-lactoglobulin amyloid fibrils by measuring the Debye-Waller factor." International Journal of Biological Macromolecules 92 (November 2016): 240–45. http://dx.doi.org/10.1016/j.ijbiomac.2016.07.011.
Full textRühs, Patrick A., Christine Affolter, Erich J. Windhab, and Peter Fischer. "Shear and dilatational linear and nonlinear subphase controlled interfacial rheology of β-lactoglobulin fibrils and their derivatives." Journal of Rheology 57, no. 3 (May 2013): 1003–22. http://dx.doi.org/10.1122/1.4802051.
Full textRühs, Patrick A., Nathalie Scheuble, Erich J. Windhab, Raffaele Mezzenga, and Peter Fischer. "Simultaneous Control of pH and Ionic Strength during Interfacial Rheology of β-Lactoglobulin Fibrils Adsorbed at Liquid/Liquid Interfaces." Langmuir 28, no. 34 (August 15, 2012): 12536–43. http://dx.doi.org/10.1021/la3026705.
Full textChang, Hon Weng, Tai Boon Tan, Phui Yee Tan, Faridah Abas, Oi Ming Lai, Yong Wang, Yonghua Wang, Imededdine Arbi Nehdi, and Chin Ping Tan. "Physical properties and stability evaluation of fish oil-in-water emulsions stabilized using thiol-modified β-lactoglobulin fibrils-chitosan complex." Food Research International 105 (March 2018): 482–91. http://dx.doi.org/10.1016/j.foodres.2017.11.034.
Full textChang, Hon Weng, Tai Boon Tan, Phui Yee Tan, Faridah Abas, Oi Ming Lai, Yong Wang, Yonghua Wang, Imededdine Arbi Nehdi, and Chin Ping Tan. "Microencapsulation of fish oil using thiol-modified β-lactoglobulin fibrils/chitosan complex: A study on the storage stability and in vitro release." Food Hydrocolloids 80 (July 2018): 186–94. http://dx.doi.org/10.1016/j.foodhyd.2018.02.002.
Full textSuo, Zhiguang, Xialing Hou, Yu Liu, Feifei Xing, Yingying Chen, and Lingyan Feng. "β-Lactoglobulin amyloid fibril-templated gold nanoclusters for cellular multicolor fluorescence imaging and colorimetric blood glucose assay." Analyst 145, no. 21 (2020): 6919–27. http://dx.doi.org/10.1039/d0an01357a.
Full textYe, Xinchen, Mikael S. Hedenqvist, Maud Langton, and Christofer Lendel. "On the role of peptide hydrolysis for fibrillation kinetics and amyloid fibril morphology." RSC Advances 8, no. 13 (2018): 6915–24. http://dx.doi.org/10.1039/c7ra10981d.
Full textMazaheri, Mansooreh, Ali Akbar Moosavi-Movahedi, Ali Akbar Saboury, Fariba Khodagholi, Fatemeh Shaerzadeh, and Nader Sheibani. "Curcumin Protects β-Lactoglobulin Fibril Formation and Fibril-Induced Neurotoxicity in PC12Cells." PLOS ONE 10, no. 7 (July 17, 2015): e0133206. http://dx.doi.org/10.1371/journal.pone.0133206.
Full textNg, Shy Kai, Kar Lin Nyam, Imededdine Arbi Nehdi, Gun Hean Chong, Oi Ming Lai, and Chin Ping Tan. "Impact of stirring speed on β-lactoglobulin fibril formation." Food Science and Biotechnology 25, S1 (March 2016): 15–21. http://dx.doi.org/10.1007/s10068-016-0093-8.
Full text马, 保亮. "Dithiothreitol Inhibits the Amyloid Fibril Formation of β-Lactoglobulin." Biophysics 02, no. 04 (2014): 39–44. http://dx.doi.org/10.12677/biphy.2014.24005.
Full textMa, Baoliang, Xiong You, and Fujiao Lu. "Inhibitory effects of β-ionone on amyloid fibril formation of β-lactoglobulin." International Journal of Biological Macromolecules 64 (March 2014): 162–67. http://dx.doi.org/10.1016/j.ijbiomac.2013.12.003.
Full textGosal, Walraj S., Allan H. Clark, and Simon B. Ross-Murphy. "Fibrillar β-Lactoglobulin Gels: Part 1. Fibril Formation and Structure." Biomacromolecules 5, no. 6 (November 2004): 2408–19. http://dx.doi.org/10.1021/bm049659d.
Full textKroes-Nijboer, Ardy, Paul Venema, Jacob Bouman, and Erik van der Linden. "The Critical Aggregation Concentration of β-Lactoglobulin-Based Fibril Formation." Food Biophysics 4, no. 2 (January 27, 2009): 59–63. http://dx.doi.org/10.1007/s11483-009-9101-3.
Full textSardar, Subrata, Sampa Pal, Sanhita Maity, Jishnu Chakraborty, and Umesh Chandra Halder. "Amyloid fibril formation by β-lactoglobulin is inhibited by gold nanoparticles." International Journal of Biological Macromolecules 69 (August 2014): 137–45. http://dx.doi.org/10.1016/j.ijbiomac.2014.05.006.
Full textLoveday, S. M., X. L. Wang, M. A. Rao, S. G. Anema, and H. Singh. "β-Lactoglobulin nanofibrils: Effect of temperature on fibril formation kinetics, fibril morphology and the rheological properties of fibril dispersions." Food Hydrocolloids 27, no. 1 (May 2012): 242–49. http://dx.doi.org/10.1016/j.foodhyd.2011.07.001.
Full textHamada, Daizo, and Christopher M. Dobson. "A kinetic study of β-lactoglobulin amyloid fibril formation promoted by urea." Protein Science 11, no. 10 (April 13, 2009): 2417–26. http://dx.doi.org/10.1110/ps.0217702.
Full textMaity, Sanhita, Sampa Pal, Subrata Sardar, Nayim Sepay, Hasan Parvej, Shahnaz Begum, Ramkrishna Dalui, Niloy Das, Anirban Pradhan, and Umesh Chandra Halder. "Inhibition of amyloid fibril formation of β-lactoglobulin by natural and synthetic curcuminoids." New Journal of Chemistry 42, no. 23 (2018): 19260–71. http://dx.doi.org/10.1039/c8nj03194k.
Full textArnaudov, Luben N., Renko de Vries, and Martien A. Cohen Stuart. "Time-resolved small-angle neutron scattering during heat-induced fibril formation from bovine β-lactoglobulin." Journal of Chemical Physics 124, no. 8 (February 28, 2006): 084701. http://dx.doi.org/10.1063/1.2171418.
Full textKrebs, Mark R. H., Glyn L. Devlin, and Athene M. Donald. "Amyloid Fibril-Like Structure Underlies the Aggregate Structure across the pH Range for β-Lactoglobulin." Biophysical Journal 96, no. 12 (June 2009): 5013–19. http://dx.doi.org/10.1016/j.bpj.2009.03.028.
Full textLoveday, S. M., M. A. Rao, L. K. Creamer, and H. Singh. "Factors Affecting Rheological Characteristics of Fibril Gels: The Case of β-Lactoglobulin and α-Lactalbumin." Journal of Food Science 74, no. 3 (April 2009): R47—R55. http://dx.doi.org/10.1111/j.1750-3841.2009.01098.x.
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