Effects of protein and phosphate buffer concentrations on thermal denaturation of lysozyme analyzed by isoconversional method

References

• Vyazovkin S, Vincent L, Sbirrazzuoli N. Thermal denaturation of collagen analyzed by isoconversional method. Macromol Biosci 2007; 7(11):1181-6; PMID:17876859; http://dx.doi.org/10.1002/mabi.200700162
   PubMed Web of Science ®Google Scholar
• Lindgren M, Sparrman T, Westlund PO. A combined molecular dynamic simulation and urea (14)N NMR relaxation study of the urea-lysozyme system. Spectrochim. Acta: Part A 2010; 75(3):953-9; http://dx.doi.org/10.1016/j.saa.2009.11.054
   PubMed Web of Science ®Google Scholar
• Burovaa TV, Grinberga NV, Grinberga VY, Rariy RV, Klibanov AM. Calorimetric evidence for a native-like conformation of hen egg-white lysozyme dissolved in glycerol. Biochim Biophys Acta 2000; 1478(2):309-17; PMID:10825542; http://dx.doi.org/10.1016/S0167-4838(00)00028-5
   PubMed Web of Science ®Google Scholar
• Petersen SB, Jonson V, Fojan P, Pedersen S. Sorbitol prevents the self-aggregation of unfolded lysozyme leading to and up to 13 degrees C stabilisation of the folded form. J Biotechnol 2004; 114(3):269-78; PMID:15522436; http://dx.doi.org/10.1016/j.jbiotec.2004.07.004
   PubMed Web of Science ®Google Scholar
• Mohamed AA, Duarte PR, Kim S. Effect of starch on the thermal kinetics and transmittance properties of lysozyme. J Sci Food Agric 2005; 85:450-8; http://dx.doi.org/10.1002/jsfa.2001
   Web of Science ®Google Scholar
• Hédoux A, Affouard F, Descamps M, Guinet Y, Paccou L. Microscopic description of protein thermostabilization mechanisms with disaccharides from Raman spectroscopy investigations. J Phys Condens Matter 2007; 19:205142-8; PMID:Can't; http://dx.doi.org/10.1088/0953-8984/19/20/205142
   PubMedGoogle Scholar
• Byrne N, Wang LM, Belieres JP, Angell CA. Reversible folding-unfolding, aggregation protection, and multi-year stabilization, in high concentration protein solutions, using ionic liquids. Chem Commun 2007; 45:2714-6; http://dx.doi.org/10.1039/B618943A
   Web of Science ®Google Scholar
• Li XQ. Microcalorimetry study of lysozyme denaturation induced by the guanidine chloride and urea. Chemistry 2011; 74 (9):834-8.
   Google Scholar
• Alice B, Jennifer JM. Reversible and non-reversible thermal denaturation of lysozyme with varying pH at low ionic strength. Biochimica et Biophysica Acta 2013; 1834:2064-70; http://dx.doi.org/10.1016/j.bbapap.2013.06.001
   PubMed Web of Science ®Google Scholar
• Li SJ, Wei YM, Fang YQ, Zhang W, Zhang B. DSC study on the thermal properties of soybean protein isolates/corn starch mixture. J Therm Anal Calorim 2014; 115:1633-8; http://dx.doi.org/10.1007/s10973-013-3433-4
   Web of Science ®Google Scholar
• Anna M, Zofia D, Ewa SK, Barbara K. Calorimetric monitoring of the effect of endurance training and testosterone treatment on rat serum denaturation transition. J Therm Anal Calorim 2014; 115:2231-7; http://dx.doi.org/10.1007/s10973-013-3611-4
   Web of Science ®Google Scholar
• Mallamace F, Corsaro C, Mallamace D, Cicero N Vasi, S, Dugo G, Stanley HE. Dynamical changes in hydration water accompanying lysozyme thermaldenaturation. Front Phys 2015; 10(5):106104-7; http://dx.doi.org/10.1007/s11467-015-0486-9
   Web of Science ®Google Scholar
• Vyazovkin S, Wight CA. Model-free and model-fitting approaches to kinetic analysis of isothermal and nonisothermal data. Thermochim Acta 1999; 340/341:53-68; http://dx.doi.org/10.1016/S0040-6031(99)00253-1
   Web of Science ®Google Scholar
• Tang, WJ, Wang CX, Chen DH. An investigation of the pyrolytic kinetics of some aliphatic amino acids. J Anal Appl Pyrolysis 2006; 75:49-53; http://dx.doi.org/10.1016/j.jaap.2005.04.003
   Web of Science ®Google Scholar
• Maeda Y, Yamada H, Ueda T, Imoto T. Effect of additives on the renaturation of reduced lysozyme in the presence of 4 M urea. Protein Eng 1996; 9:461-5; PMID:8795046; http://dx.doi.org/10.1093/protein/9.5.461
   PubMedGoogle Scholar
• Baier S, McClements J. Impact of Preferential Interactions on Thermal Stability and Gelation of Bovine Serum Albumin in Aqueous Sucrose Solutions. J Agric Food Chem 2001; 49:2600-8; PMID:11368642; http://dx.doi.org/10.1021/jf001096j
   PubMed Web of Science ®Google Scholar
• Bon CL, Nicolai T, Durand D. Kinetics of aggregation and gelation of globular proteins after heat-induced denaturation. Macromolecules 1999; 32:6120-7; http://dx.doi.org/10.1021/ma9905775
   Web of Science ®Google Scholar
• Biliaderis CG. Differential scanning calorimetry in food research—A review. Food Chem 1983; 10:239-65; http://dx.doi.org/10.1016/0308-8146(83)90081-X
   Web of Science ®Google Scholar
• Nohara D, Mizutani A, Sakai T. Kinetic study on thermal denaturation of hen egg-white lysozyme involving precipitation. J Biosci Bioeng 1999; 87:199-205; PMID:16232451; http://dx.doi.org/10.1016/S1389-1723(99)89013-6
   PubMed Web of Science ®Google Scholar
• Shosheva A, Donchev A, Dimitrov M, Kostov G, Toromanov G, Getov V, Alexov E. Comparative study of the stability of poplar plastocyanin isoforms. Biochim Biophys Acta 2005; 1748:116-27; PMID:15752700; http://dx.doi.org/10.1016/j.bbapap.2004.12.012
   PubMed Web of Science ®Google Scholar
• Ravindra BK, Vinod B. Ionic-strength-dependent transition of hen egg-white lysozyme at low pH to a compact state and its aggregation on thermal denaturation. Eur J Biochem 1997; 245:781-9.
   PubMedGoogle Scholar
• Sanchez-Ruiz JM. Theoretical analysis of Lumry-Eyring models in differential scanning calorimetr. Biophys J 1992; 61(4):921-935; PMID:19431826; http://dx.doi.org/10.1016/S0006-3495(92)81899-4
   PubMed Web of Science ®Google Scholar
• Lumry R, Eyring H. Conformational changes of protein. J Phys Chem 1954; 58:110-20; http://dx.doi.org/10.1021/j150512a005
   Web of Science ®Google Scholar
• Jaenicke R. Folding and association of proteins. Prog Biophys Mol Biol 1987; 49:117-237; PMID:3327098; http://dx.doi.org/10.1016/0079-6107(87)90011-3
   PubMed Web of Science ®Google Scholar