TY - JOUR
T1 - Rehydration and water sorption behaviour of bovine milk protein isolate and its associated enzymatic hydrolysates
AU - Ryan, Ger
AU - O'Regan, Jonathan
AU - FitzGerald, Richard J.
N1 - Publisher Copyright:
© 2022 Elsevier Ltd
PY - 2022/5
Y1 - 2022/5
N2 - The glass transition temperature (Tg), moisture sorption and rehydration properties of bovine milk protein isolate (MPI) and MPI hydrolysates generated with Flavourzyme™, Neutrase™ and Protamex™ [degree of hydrolysis (DH) ranging from 15.6 to 37.1%] were evaluated. MPI hydrolysates displayed reduced water droplet contact angles (<50°) compared with intact MPI (∼90°), indicating increased wettability. The aqueous solubility of the hydrolysates was increased (72–100%) compared with intact MPI (∼30%) at 25 °C. The hydrolysates had higher moisture contents (40–50%) than intact MPI (∼27%) at water activity (ɑw) values between 0.80 and 0.90. MPI hydrolysates displayed reduced Tg (48.5–67.3 °C) compared with intact MPI (∼121 °C), indicating reduced stability. Overall, enzymatic hydrolysis enhanced the properties of MPI; this improvement was enzyme dependent and increased with increasing DH. Manufacture of hydrolysate ingredients with a controlled moisture content and storage at controlled ambient temperatures is proposed to maintain the improved rehydration properties.
AB - The glass transition temperature (Tg), moisture sorption and rehydration properties of bovine milk protein isolate (MPI) and MPI hydrolysates generated with Flavourzyme™, Neutrase™ and Protamex™ [degree of hydrolysis (DH) ranging from 15.6 to 37.1%] were evaluated. MPI hydrolysates displayed reduced water droplet contact angles (<50°) compared with intact MPI (∼90°), indicating increased wettability. The aqueous solubility of the hydrolysates was increased (72–100%) compared with intact MPI (∼30%) at 25 °C. The hydrolysates had higher moisture contents (40–50%) than intact MPI (∼27%) at water activity (ɑw) values between 0.80 and 0.90. MPI hydrolysates displayed reduced Tg (48.5–67.3 °C) compared with intact MPI (∼121 °C), indicating reduced stability. Overall, enzymatic hydrolysis enhanced the properties of MPI; this improvement was enzyme dependent and increased with increasing DH. Manufacture of hydrolysate ingredients with a controlled moisture content and storage at controlled ambient temperatures is proposed to maintain the improved rehydration properties.
UR - http://www.scopus.com/inward/record.url?scp=85123735166&partnerID=8YFLogxK
U2 - 10.1016/j.idairyj.2022.105323
DO - 10.1016/j.idairyj.2022.105323
M3 - Article
AN - SCOPUS:85123735166
SN - 0958-6946
VL - 128
JO - International Dairy Journal
JF - International Dairy Journal
M1 - 105323
ER -