TY - JOUR
T1 - Milk protein hydrolysis by actinidin
T2 - Influence of protein source and hydrolysis conditions
AU - Kaur, S.
AU - Huppertz, T.
AU - Vasiljevic, T.
N1 - Publisher Copyright:
© 2021 Elsevier Ltd
PY - 2021/7
Y1 - 2021/7
N2 - The plant protease actinidin has been frequently used in the food industry, but its application in dairy systems remains largely unassessed. The aim of this research was to establish the effect of temperature (15–60 °C), time (0–5 h) and enzyme-to-substrate ratio on the actinidin-induced hydrolysis of proteins in whey protein isolate (WPI), whey protein concentrate (WPC) and milk protein concentrate (MPC), as monitored through the degree of hydrolysis (DH) and SDS-PAGE. The DH increased with increasing temperature and incubation time for all three protein sources. A lower E:S ratio resulted in a greater DH for WPC and WPI, but not for MPC. SDS-PAGE analysis revealed that actinidin mainly acted on α-lactalbumin and αS-caseins in WPI and MPC, respectively.
AB - The plant protease actinidin has been frequently used in the food industry, but its application in dairy systems remains largely unassessed. The aim of this research was to establish the effect of temperature (15–60 °C), time (0–5 h) and enzyme-to-substrate ratio on the actinidin-induced hydrolysis of proteins in whey protein isolate (WPI), whey protein concentrate (WPC) and milk protein concentrate (MPC), as monitored through the degree of hydrolysis (DH) and SDS-PAGE. The DH increased with increasing temperature and incubation time for all three protein sources. A lower E:S ratio resulted in a greater DH for WPC and WPI, but not for MPC. SDS-PAGE analysis revealed that actinidin mainly acted on α-lactalbumin and αS-caseins in WPI and MPC, respectively.
UR - https://www.scopus.com/pages/publications/85101732313
U2 - 10.1016/j.idairyj.2021.105029
DO - 10.1016/j.idairyj.2021.105029
M3 - Article
AN - SCOPUS:85101732313
SN - 0958-6946
VL - 118
JO - International Dairy Journal
JF - International Dairy Journal
M1 - 105029
ER -