| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 34404 | Process Biochemistry | 2015 | 9 Pages |
•Hydrolysate produced from acid whey using the integrative process showed high ACE-inhibitory activity.•High ionic calcium concentration in acid whey has an inhibition effect on ACE.•Peptides contributing to ACE-inhibitory activity were a mixture of β-lactoglobulin, α-lactalbumin and BSA.
High ionic calcium concentration and the absence of casein macropeptides (CMP) in acid whey could influence the production of angiotensin-I-converting enzyme (ACE)-inhibitory hydrolysate and its bioactivity through the application of the integrative process. Therefore, the aim of the present study was to produce a hydrolysate from acid whey applying the integrative process. Process performance was evaluated based on protein adsorption capacity and conversion in relation to ACE-inhibitory activity (ACEi%) and ionic calcium concentration. Hydrolysates with high potency of their biological activity were produced (IC50 = 206–353 μg mL−1). High ionic calcium concentration in acid whey contributed to ACE-inhibitory activity. However, low β-lactoglobulin adsorption and conversion was observed. Optimisation of the resin volume increased the adsorption of β-lactoglobulin significantly but with lower selectivity. The changes in conversion value were not significant even at higher concentration of enzyme. Several ACE inhibitors derived from β-lactoglobulin that were identified before in sweet whey hydrolysates such as, IIAEKT, IIAE, IVTQ, LIVTQ, LIVTQT, LDAQ and LIVT were found. New peptides such as, SNICNI and ECCHGD derived from α-lactalbumin and BSA respectively were identified.
