Crystallization behavior and crystal properties of lactose as affected by lactic, citric, or phosphoric acid.

The presence of acids in a lactose-containing system can affect its crystallization. The crystallization kinetics of lactose solutions were investigated as affected by lactic, citric, or phosphoric acid at a concentration of 0.05, 1, or 4% (wt/wt) as compared with that of pure lactose. The crystallization behavior of lactose was affected differently by the presence of all 3 acids and was mostly concentration dependent. The presence of 1 and 4% citric or phosphoric acid reduced the crystal yield significantly (≥18%) as compared with that of pure lactose (∼82%). Thermographic analysis of lactose crystals showed that the presence of 1% lactic, 0.05 and 1% citric, and 4% phosphoric acids in the lactose solutions induced the formation of amorphous lactose. X-Ray diffraction analysis revealed that the lactose crystallized mainly into α-lactose monohydrate, stable anhydrous α-lactose, and anhydrous crystals containing α-lactose and ß-lactose in a molar ratio of 5:3 and 4:1. Average size of the lactose particles, comprising of several crystallites, declined depending on the type of the acids and their concentration, but size of a single crystallite was not altered. The findings suggested that the lactose crystallization and crystal properties are governed by the lactose-water interactions, which can be influenced by the presence of acids in a concentration-dependent manner.

The effect of ultrasound on casein micelle integrity.

Samples of fresh skim milk, reconstituted micellar casein, and casein powder were sonicated at 20 kHz to investigate the effect of ultrasonication. For fresh skim milk, the average size of the remaining fat globules was reduced by approximately 10 nm after 60 min of sonication; however, the size of the casein micelles was determined to be unchanged. A small increase in soluble whey protein and a corresponding decrease in viscosity also occurred within the first few minutes of sonication, which could be attributed to the breakup of casein-whey protein aggregates. No measurable changes in free casein content could be detected in ultracentrifuged skim milk samples sonicated for up to 60 min. A small, temporary decrease in pH resulted from sonication; however, no measurable change in soluble calcium concentration was observed. Therefore, casein micelles in fresh skim milk were stable during the exposure to ultrasonication. Similar results were obtained for reconstituted micellar casein, whereas larger viscosity changes were observed as whey protein content was increased. Controlled application of ultrasound can be usefully applied to reverse process-induced protein aggregation without affecting the native state of casein micelles.