Antioxidant activities and functional properties of enzymatic protein hydrolysates from defatted Camellia oleifera seed cake.
Seed cake protein (SCP) from Camellia oleifera was hydrolyzed by five commercial proteases (Flavorzyme, Trypsin, Neutrase, Papain, Alcalase). Amino acid composition, molecular weight distribution, antioxidant activity and functional property of the seed cake protein hydrolysates (SCPH) were investigated. Enzymatic hydrolysis improved protein solubility significantly but impaired the foaming and emulsifying property. Hydrolysate generated by alcalase had the highest hydrolysis degree (DH) and antioxidant activity, and displayed excellent protein solubility over wide range of pH, while hydrolysate prepared by flavorzyme showed better copper chelating capacity and emulsifying stability with low molecular weight distribution. Trypsin-treated SCPH showed better foaming property than original protein. The results indicated that enzyme type greatly influenced the molecular weight, functional property and antioxidant activity of SCPH. It was also found that electing appropriate protease and controlling the DH could be enhanced or reduced functional property according to actual applications.
College of Life Science, Sichuan Agricultural University, Ya'an, Sichuan 625014 China.
Xu
X
Li
College of Life Science, Sichuan Agricultural University, Ya'an, Sichuan 625014 China.
Junlin
J
Deng
College of Life Science, Sichuan Agricultural University, Ya'an, Sichuan 625014 China.
Shian
S
Shen
College of Agronomy, Sichuan Agricultural University, Chengdu, Sichuan 611130 China.
Tian
T
Li
College of Life Science, Sichuan Agricultural University, Ya'an, Sichuan 625014 China.
Ming
M
Yuan
College of Life Science, Sichuan Agricultural University, Ya'an, Sichuan 625014 China.
Ruiwu
R
Yang
College of Life Science, Sichuan Agricultural University, Ya'an, Sichuan 625014 China.
Chunbang
C
Ding
Antioxidant activity; Camellia oleifera; Functional property; Protease type; Protein hydrolysate