Stability of biopolymer particles formed by heat treatment of β-lactoglobulin/beet pectin electrostatic complexes

被引:65
作者
Jones, Owen G. [1 ]
McClements, D. Julian [1 ]
机构
[1] Univ Massachusetts, Dept Food Sci, Biopolymers & Colloids Res Lab, Amherst, MA 01003 USA
关键词
soluble complexes; beta-lactoglobulin; beet pectin; salt; thermal treatment; stability;
D O I
10.1007/s11483-008-9068-5
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The purpose of this study was to examine the stability of biopolymer particles formed by heating electrostatic complexes of beta-lactoglobulin and sugar beet pectin together (pH 5, 80 degrees C for 15 min). The effects of electrostatic interactions on the formation and stability of the particles were investigated by incorporation of different salt levels (0 to 200 mM NaCl) during the preparation procedure. Biopolymer particles were characterized by turbidity, electrophoretic mobility, dynamic light scattering, and visual observance. Salt inclusion (>= 25 mM) prior to heating beta-lactoglobulin/pectin complexes led to the formation of large biopolymer particles (d > 1,000 nm) that rapidly sedimented, but salt inclusion after heating (0 to 200 mM) led to the formation of biopolymer particles that remained relatively small (d < 350 nm) and were stable to sedimentation. The biopolymer particles formed in the absence of salt remained stable over a wide range of pH values (e.g., pH 3 to 7 in the presence of 200 mM NaCl). These biopolymer particles may therefore be suitable for application in a number of food products as delivery systems, clouding agents, or texture modifiers.
引用
收藏
页码:191 / 197
页数:7
相关论文
共 28 条
[1]   Formation of new glucomannan-chitosan nanoparticles and study of their ability to associate and deliver proteins [J].
Alonso-Sande, Maria ;
Cuna, Margarita ;
Remunan-Lopez, Carmen .
MACROMOLECULES, 2006, 39 (12) :4152-4158
[2]  
Benichou A, 2002, J DISPER SCI TECHNOL, V23, P93
[3]   Food protein-based materials as nutraceutical delivery systems [J].
Chen, LY ;
Remondetto, GE ;
Subirade, M .
TRENDS IN FOOD SCIENCE & TECHNOLOGY, 2006, 17 (05) :272-283
[4]   Polyelectrolyte-protein complexes [J].
Cooper, CL ;
Dubin, PL ;
Kayitmazer, AB ;
Turksen, S .
CURRENT OPINION IN COLLOID & INTERFACE SCIENCE, 2005, 10 (1-2) :52-78
[5]   Gelation of globular protein in presence of low methoxyl pectin:: effect of Na+ and/or Ca2+ ions on rheology and microstructure of the systems [J].
Donato, L ;
Garnier, C ;
Novales, B ;
Doublier, JL .
FOOD HYDROCOLLOIDS, 2005, 19 (03) :549-556
[6]   Associative phase separation of β-lactoglobulin/pectin solutions:: a kinetic study by small angle static light scattering [J].
Girard, M ;
Sanchez, C ;
Laneuville, SI ;
Turgeon, SL ;
Gauthier, SE .
COLLOIDS AND SURFACES B-BIOINTERFACES, 2004, 35 (01) :15-22
[7]   Quantification of the interactions between β-lactoglobulin and pectin through capillary electrophoresis analysis [J].
Girard, M ;
Turgeon, SL ;
Gauthier, SF .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2003, 51 (20) :6043-6049
[8]   Thermodynamic parameters of β-lactoglobulin-pectin complexes assessed by isothermal titration calorimetry [J].
Girard, M ;
Turgeon, SL ;
Gauthier, SF .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2003, 51 (15) :4450-4455
[9]   Interbiopolymer complexing between β-lactoglobulin and low- and high-methylated pectin measured by potentiometric titration and ultrafiltration [J].
Girard, M ;
Turgeon, SL ;
Gauthier, SF .
FOOD HYDROCOLLOIDS, 2002, 16 (06) :585-591
[10]   Heat-induced aggregation of β-lactoglobulin as a function of pH [J].
Hoffmann, MAM ;
van Mil, PJJM .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1999, 47 (05) :1898-1905