TY - JOUR
T1 - Formation of nanotubes and gels at a broad pH range upon partial hydrolysis of bovine α-lactalbumin
AU - Geng, Xiaolu
AU - Bjerrum, Morten Jannik
AU - Arleth, Lise
AU - Otte, Jeanette
AU - Ipsen, Richard
PY - 2016/1/1
Y1 - 2016/1/1
N2 - The influence of pH (from 7.5 to 4.0) on the hydrolysis and self-assembly process of nanotubes formed from partially hydrolysed bovine α-lactalbumin was studied. The results showed that the pH had no influence on the products resulting from hydrolysis, but a decrease in pH dramatically reduced the hydrolysis rate. In contrast, the self-assembly process was favoured by decreased pH due to the reduced electrostatic repulsion between the fragments making up the nanotubes. Initially, upon adding a protease, a rapid change in conformation was indicated by circular dichroism spectroscopy. Subsequently no further change was observed. Due to slower hydrolysis and faster self-assembly at pH 6.5 and 4.0, the main building fragments were integrated quickly into nanotubes, and hence avoided further hydrolysis. Self-assembly of protease-induced α-lactalbumin nanotubes can thus be extended over a broad range of pH values. These findings might be useful for future applications in both food and pharmaceutical industries.
AB - The influence of pH (from 7.5 to 4.0) on the hydrolysis and self-assembly process of nanotubes formed from partially hydrolysed bovine α-lactalbumin was studied. The results showed that the pH had no influence on the products resulting from hydrolysis, but a decrease in pH dramatically reduced the hydrolysis rate. In contrast, the self-assembly process was favoured by decreased pH due to the reduced electrostatic repulsion between the fragments making up the nanotubes. Initially, upon adding a protease, a rapid change in conformation was indicated by circular dichroism spectroscopy. Subsequently no further change was observed. Due to slower hydrolysis and faster self-assembly at pH 6.5 and 4.0, the main building fragments were integrated quickly into nanotubes, and hence avoided further hydrolysis. Self-assembly of protease-induced α-lactalbumin nanotubes can thus be extended over a broad range of pH values. These findings might be useful for future applications in both food and pharmaceutical industries.
U2 - 10.1016/j.idairyj.2015.08.005
DO - 10.1016/j.idairyj.2015.08.005
M3 - Journal article
SN - 0958-6946
VL - 52
SP - 72
EP - 81
JO - International Dairy Journal
JF - International Dairy Journal
ER -