Characterization of casein micelle precipitation by chitosans

被引:39
作者
Ausar, SF
Bianco, ID
Badini, RG
Castagna, LF
Modesti, NM
Landa, CA
Beltramo, DM
机构
[1] Agencia Cordoba Ciencia SE, CEPROCOR, RA-5164 Santa Maria Punilla, Argentina
[2] Consejo Nacl Invest Cient & Tecn, Cordoba, Argentina
关键词
casein; chitosan; hydrocolloids; casein-chitosan complex;
D O I
10.3168/jds.S0022-0302(01)74485-2
中图分类号
S8 [畜牧、 动物医学、狩猎、蚕、蜂];
学科分类号
0905 ;
摘要
We have found that the addition of chitosan, a cationic polymer, on whole or skim milk produces destabilization and coagulation of casein micelles that takes place without changes in the milk pH or the stability of most whey proteins. The amount of lipids recovered in the chitosan-casein aggregates was similar or higher than that obtained with rennet or acid precipitation. Approximately 70% of milk Ca2+ (similar to 750 mg/L) was found in the chitosan-induced aggregates, which is 10 and 50% higher than the amounts observed with acid or rennet coagulations, respectively. Purified alpha, beta-, and kappa -caseins were extensively precipitated by different molecular weight chitosans at pH 6.8. The phosphate groups of caseins seem not to be relevant in this interaction because dephosphorylated alpha- and beta -caseins were equally precipitated with chitosans. Analysis by optical microscopy of the chitosan-casein complex reveals that the size of the aggregates increase as the molecular weight of chitosans increase. Hydrophobic and electrostatic interactions particpate in the association and coagulation of casein micelles with chitosans of different molecular weights. The phenomenon is observed over a broad range of temperature (4 to 70 degreesC) with a reduction in the concentration of chitosan needed to precipitate the caseins that parallels a reduction in the viscosity of the chitosan solutions. Taken together, the results indicate that the electrostatic interactions may contribute energetically to the association between the two biopolymers, but the hydrophobicity of the complex would be the key determinant in the overall energetics of the reaction.
引用
收藏
页码:361 / 369
页数:9
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