Physico-chemical properties of different forms of bovine lactoferrin

被引:111
作者
Bokkhim, Huma [1 ]
Bansal, Nidhi [1 ]
Grondahl, Lisbeth [2 ]
Bhandari, Bhesh [1 ]
机构
[1] Univ Queensland, Sch Agr & Food Sci, Brisbane, Qld 4072, Australia
[2] Univ Queensland, Sch Chem & Mol Biosci, Brisbane, Qld 4072, Australia
关键词
Lactoferrin; Molecular confirmation; Physico-chemical properties; Thermal denaturation; Rheological behaviour; Surface tension; INDUCED AGGREGATION; MILK; PROTEINS; IRON; CONFORMATION; DENATURATION; BEHAVIOR; WATER; SALT; PH;
D O I
10.1016/j.foodchem.2013.05.139
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Three forms of bovine lactoferrin (Lf), apo-, native- and holo- with 0.9%, 12.9% and 99.7% iron content, respectively, were characterised for their physico-chemical properties. Colour, surface tension, thermal properties, particle charge and rheological behaviour of Lf were found to be affected by the form of Lf. The surface tension of Lf tends to decrease with decrease in iron content. The Circular Dichroism (CD) spectra confirmed that all forms of Lf had similar secondary structures while the tertiary structure was different for holo-Lf. The Differential Scanning Calorimeter (DSC) analysis showed that the apo- and holo-Lf in aqueous solution displayed thermal denaturation temperatures of 71 +/- 0.2 and 91 +/- 0.5 degrees C, respectively, suggesting that the iron saturation of Lf tends to increase its thermal stability. The study of particle charge properties (zeta-potential) in 1 mM KCl salt solution showed that apo-Lf reached the net charge of zero in the pH range 5.5-6.5 whereas native and holo-Lf in the pH range 8.0-9.0. The apparent viscosity of 1% (wt/wt) solution of the different forms of Lf showed no difference between apo- and native-Lf (approximate to 1.4 mPa s) while the value was significantly higher (2.38 mPa s) for holo-Lf. (C) 2013 Elsevier Ltd. All rights reserved.
引用
收藏
页码:3007 / 3013
页数:7
相关论文
共 36 条
[1]   HEAT-STABILITY OF BOVINE LACTOFERRIN AT ACIDIC PH [J].
ABE, H ;
SAITO, H ;
MIYAKAWA, H ;
TAMURA, Y ;
SHIMAMURA, S ;
NAGAO, E ;
TOMITA, M .
JOURNAL OF DAIRY SCIENCE, 1991, 74 (01) :65-71
[2]   Molecular structure, binding properties and dynamics of lactoferrin [J].
Baker, EN ;
Baker, HM .
CELLULAR AND MOLECULAR LIFE SCIENCES, 2005, 62 (22) :2531-2539
[3]  
BATES GW, 1973, J BIOL CHEM, V248, P3228
[4]   Formation of protein nanoparticles by controlled heat treatment of lactoferrin: Factors affecting particle characteristics [J].
Bengoechea, Carlos ;
Peinado, Irene ;
Julian McClements, David .
FOOD HYDROCOLLOIDS, 2011, 25 (05) :1354-1360
[5]   LACTOFERRIN FROM HUMAN-BREAST MILK AND FROM NEUTROPHIL GRANULOCYTES - COMPARATIVE STUDIES OF ISOLATION, QUANTITATION, CHARACTERIZATION AND IRON-BINDING PROPERTIES [J].
BEZWODA, WR ;
MANSOOR, N .
BIOMEDICAL CHROMATOGRAPHY, 1989, 3 (03) :121-126
[6]  
Bowen W. R., 2010, NANOSCIENCE COLLOIDA, P79
[7]   Heat-induced aggregation of bovine lactoferrin at neutral pH: Effect of iron saturation [J].
Brisson, Guillaume ;
Britten, Michel ;
Pouliot, Yves .
INTERNATIONAL DAIRY JOURNAL, 2007, 17 (06) :617-624
[8]   The physiology of lactoferrin [J].
Brock, JH .
BIOCHEMISTRY AND CELL BIOLOGY, 2002, 80 (01) :1-6
[9]   SPECTROSCOPIC STUDY OF BOVINE LACTOFERRIN [J].
BROWN, EM ;
PARRY, RM .
BIOCHEMISTRY, 1974, 13 (22) :4560-4565
[10]   Isolation of lactoferrin from milk of different species:: Calorimetric and antimicrobial studies [J].
Conesa, Celia ;
Sanchez, Lourdes ;
Rota, Carmen ;
Perez, Maria-Dolores ;
Calvo, Miguel ;
Farnaud, Sebastien ;
Evans, Robert W. .
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 2008, 150 (01) :131-139