INFLUENCE OF COMPLEXING OF CARBOXIMETHYLCELLULOSE ON THE THERMOSTABILITY AND GELATION OF ALPHA-LACTALBUMIN AND BETA-LACTOGLOBULIN.

CAPITANI, CAROLINE; PÉREZ, OSCAR E; BERTOLDO PACHECO, MARÍA TERESA; PILOSOF, ANA MR.

FOOD HYDROCOLLOIDS

Elsevier Ltd.

Lugar: Amsterdam; Año: 2007 vol. 21 p. 1344 - 1354

0268-005X

Thermostability and gelation of the main proteins of whey, alpha-lactalbumin (a-lac) and beta-lactoglobulin (b-lg) recovered by selective complexation with carboxymethylcellulose (CMC) was studied to evaluate its functionality in food systems. Their behavior was compared to the non-complexed proteins. Both complexes showed a maximum stability at pH 4, that is close to the pH of obtention of blg/CMC coacervate (pH 4) and a-lac/CMC coacervate (pH 3.2). Protein complexation increased the thermostability of b-lg by approximately 6–8 1C and that of a-lac by approximately 26 1C due to immobilization of protein molecules in a complex, mainly byelectrostatic interactions and because of different amounts of bound polysaccharide. The denaturation enthalpy of complexed proteins markedly decreased as compared to free proteins. Storage modulus (G0) and loss modulus (G00) were recorded to reflect the structure development during heating b-lg/CMC and a-lac/CMC complexes at different pH values. b-lg/CMC complex at 20wt% was a viscoelastic liquid at pH values within 2 and 8 but upon heating turned to a particulate viscoelastic gel. However, a-lac/CMC complex formed before heating opaque, large visible white particulate aggregates that sticked together to give a solid viscoelastic structure that was not further modified by thermal processing.Keywords: Protein polysaccharide interactions; Differential scanning calorimetry; Denaturation; Gels; Coacervate