Abstract
Thermal denaturation of recombinant human lysozyme from rice has been studied by differential scanning calorimetry at acidic (4.2), neutral (7.2) and basic (9.2) pH levels at various heating rates, and it has been compared with thermal denaturation of human lysozyme isolated from milk at the same pH levels at a heating rate of 10 °C/min. Data obtained from heat-induced unfolding and subsequent refolding after heating indicate that thermal denaturation of both lysozymes undergoes a two-state process. The maximum temperature of the endothermic peaks and the enthalpy change of denaturation indicate that recombinant and milk lysozymes possess similar thermostability, which is higher at acidic than at neutral pH. On the other hand, both proteins are more thermolabile at basic pH. Lysozyme from human milk shows a higher tendency to aggregate than recombinant human lysozyme from rice during the thermal denaturation process.
Similar content being viewed by others
References
Olsen OM, Nilsen IW, Sletten K, Myrnes B (2003) Comp Biochem Phys B 136:107–115
Ibrahim HR, Higashiguchi S, Juneja LR, Kim M, Yamamoto T (1996) J Agric Food Chem 44:1416–1423
Braun OH, Sandkühler H (1985) J Pediatr Gastr Nutr 4:583–586
Parry RM, Chandan RC, Shahani KM (1968) J Dairy Sci 51:606–607
Piccini R, Binda E, Belotti M, Casirani G, Zecconi A (2005) Vet Res 36:747–757
Li N, Yu Z, Meng Q, Yu H, Fan B, Yu S, Fei J, Wang L, Dai Y (2006) J Dairy Sci 89:2911–2918
Eitenmiller RR, Friend BA, Shahani KM, Ball EM (1974) J Food Sci 39:930–933
Hanson LA, Winberg J (1972) Arch Dis Child 47:845–848
Modler HW (1994) Int Dairy J 4:383–407
Dewey KG, Heinig MJ, Nommsen-Rivers LA (1995) J Pediatr 126:696–702
Proctor VA, Cunningham FE (1988) Crit Rev Food Sci 26:359–395
Carlsson B, Cruz JR, García B, Hanson LA, Urrutia JJ (1979) Immune factors in human milk. In: Visser HKA (ed) Nutrition and metabolismus of the fetus and infants. The Hague, The Netherlands, pp 263–271
Wang CS, Kloer HU (1984) Anal Biochem 139:224–227
Lollike K, Kjeldsen L, Sengeløv H, Borregaard N (1995) Leukemia 9:206–209
Takai I, Oda O, Shinzato T, Ohbayashi K, Yamanaka N, Maeda K (1996) J Chromatogr B Biomed Appl 685:21–25
Yang B, Wang J, Tang B, Liu Y, Guo C, Yang P, Yu T, Li R, Zhao J, Zhang L, Dai Y, Li N (2011) PLoS One 16:e17593
Xiong R, Chen J (2008) Biotechnol Appl Biochem 51:129–134
Goldstein DA, Thomas JA (2004) Q J Med 97:705–716
Twyman RM, Stoger E, Schillberg S, Christou P, Fischer R (2003) Trends Biotechnol 21:570–578
Gastañaduy A, Cordano A, Graham GG (1990) J Pediatr Gastroenterol Nutr 11:240–246
Llabrés M, Cueto M, Dorta MJ, Munguía O (2003) Int J Pharm 252:159–166
Kissinger HE (1957) Anal Chem 29:1702–1706
Jollès P, Jollès J (1984) Mol Cell Biochem 63:165–189
Privalov PL, Griko YV, Freire E, Privalov G, van Dael H (1995) J Mol Biol 252:447–459
Makki F, Durance TD (1996) Food Res Int 29:635–645
Harwalkar VR, Ma CY, Maurice TJ (1990) Instrumentation and techniques of thermal analysis in food research. In: Harwalkar VR, Ma CY (eds) Thermal analysis of foods. Elsevier, Essex, pp 1–15
Dobson CM, Hooke SD, Radford SE (1994) Biochemistry 33:5867–5876
Koshiba T, Tsumoto K, Masaki K, Kawano K, Nitta K, Kumagai I (1998) Protein Eng 11:683–690
Kuroki R, Kawakita S, Nakamura H, Yutani K (1992) Proc Natl Acad Sci USA 89:6803–6807
Imoto T, Hashimoto Y, Munemura O, Masumoto K, Ueda T (2001) Biol Pharm Bull 24:1102–1107
Yutani K, Takano K, Ogasahara K, Kaneda H, Yagamata Y, Fujii S, Kanaya E, Kikuchi M, Oobatake M (1995) J Mol Biol 254:62–76
Yutani K, Takano K, Tsuchimori K, Yagamata Y (1999) Eur J Biochem 266:675–682
Clark EDB (1998) Curr Opin Biotechnol 9:157–163
Boothe J, Nykiforuk C, Shen Y, Zaplachinski S, Szarka S, Kuhlman P, Murray E, Morck D, Moloney MM (2010) Plant Biotechnol J 8:588–606
Acknowledgments
This research has been carried out supported by the European Social Fund and by a research fellow grant from the Ministerio de Educación y Ciencia of Spanish Government.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Castillo, E., Franco, I., Pérez, M.D. et al. Thermal denaturation of recombinant human lysozyme from rice: effect of pH and comparison with human milk lysozyme. Eur Food Res Technol 233, 1067–1073 (2011). https://doi.org/10.1007/s00217-011-1612-8
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s00217-011-1612-8