Ionic regulation whey protein composition on membrane fouling during ultrafiltration process analyzed by HPLC.

In order to meet the market demand and avoid the increase of operation amount and cleaning cost in the process of ultrafiltration, it is particularly important to find more practical and efficient methods to control and improve membrane fouling. In this study, the ions in the ultrafiltration process were regulated to affect membrane surface proteins composition (lactoferrin, α-lactalbumin, ß-lactoglobulin A and ß-lactoglobulin B) and delay membrane fouling. It was found that Na+ (21 mmol/L), Zn2+ (0.25 mmol/L) and K+ (44 mmol/L) was added at 4 min, 8 min and 12 min, respectively during ultrafiltration process. The continuous regulation slowed down the decline rate of membrane flux and reduced the content of α-lactalbumin, ß-lactoglobulin A and ß-lactoglobulin B on the membrane surface analyzed by HPLC. This could reduce the irreversible membrane fouling of proteins cake resistance. Furthermore, the ions concentration was also investigated after filtration. The concentration of K+ was increased significantly and other ions concentration was not significantly changed after continuous regulation such Na+, Mg2+, Zn2+ and Ca2+ compared to control. Therefore, dynamic ionic regulation of whey protein ultrafiltration process is a simple and effective method, which provides technical theoretical basis for optimizing and improving membrane technology.

The effect of ion environment changes on retention protein behavior during whey ultrafiltration process.

The factors affecting membrane fouling are very complex. In this study, the membrane fouling process was revealed from the perspective of ion environment changes, which affected the whey protein structure during ultrafiltration. It was found that the concentrations of Ca2+ and Na+ were overall increased and the concentrations of K+, Mg2+ and Zn2+ were decreased at an ultrafiltration time of 11 min, which made more hydrophilic groups buried inside and increased the content of α-helix, leading to more protein aggregation. The relatively higher K+ ratio in retention could lead to an antiparallel ß-sheet configuration, aspartic acid, glutamic acid and tryptophan increased, which resulted in more protein aggregation and deposition on the membrane surface at 17 min. When the ion concentration and ratio restored the balance and were close to the initial state in retention, the protein surface tension decreased, and the hydrophilic ability increased at 21-24 min.