Physicochemical properties of peanut protein isolate-glucomannan conjugates prepared by ultrasonic treatment.
Peanut protein isolate (PPI) was glycated with glucomannan through classical heating or ultrasound treatment in this work. The physicochemical properties of PPI-glucomannan conjugates prepared by ultrasound treatment were compared to those prepared by classical heating. Compared with classical heating, ultrasound treatment could accelerate the graft reaction between PPI and glucomannan and improve the concentration of available free amino groups of PPI. Solubility and emulsifying properties of the conjugates obtained by ultrasound treatment were both improved as compared to those obtained by classical heating and native PPI. Decreases of lysine and arginine contents during the graft reaction indicated that these two amino acid residues attended the covalent linkage between PPI and glucomannan. Structural feature analyses suggested that conjugates obtained by ultrasound treatment had less α-helix, more β-structures and random coil, higher surface hydrophobicity and less compact tertiary structure as compared to those obtained by classical heating and native PPI.
College of Food Science and Engineering, Northwest A&F University, Xinong Road No. 28, Yangling, Shaanxi 712100, China; State Key Laboratory of Food Science and Technology, School of Food Science and Technology, Jiangnan University, 1800 Lihu Road, Wuxi 214122, Jiangsu, China.
Chen
C
Li
Department of Food Science and Technology, Huazhong Agricultural University, Shizishan Road, Wuhan 430070, China.
Xingjian
X
Huang
College of Food Science and Engineering, Northwest A&F University, Xinong Road No. 28, Yangling, Shaanxi 712100, China.
Qiang
Q
Peng
College of Food Science and Engineering, Northwest A&F University, Xinong Road No. 28, Yangling, Shaanxi 712100, China.
Yuanyuan
Y
Shan
College of Food Science and Engineering, Northwest A&F University, Xinong Road No. 28, Yangling, Shaanxi 712100, China. Electronic address: xuefeng@nwsuaf.edu.cn.
Feng
F
Xue
D000596:Amino Acids / Q000737:chemistry / Q000528:radiation effects; D010367:Arachis / Q000737:chemistry* / Q000528:radiation effects*; D001120:Arginine / Q000737:chemistry / Q000528:radiation effects; D002942:Circular Dichroism; D004655:Emulsions; D006358:Hot Temperature; D057927:Hydrophobic and Hydrophilic Interactions / Q000528:radiation effects; D008239:Lysine / Q000737:chemistry / Q000528:radiation effects; D008351:Mannans / Q000737:chemistry* / Q000528:radiation effects*; D010940:Plant Proteins / Q000737:chemistry* / Q000528:radiation effects*; D017433:Protein Structure, Secondary / Q000528:radiation effects; D012995:Solubility / Q000528:radiation effects; D014465:Ultrasonics / Q000379:methods*
D000596:Amino Acids; D004655:Emulsions; D008351:Mannans; D010940:Plant Proteins; C022901:(1-6)-alpha-glucomannan; D001120:Arginine; D008239:Lysine
Classical heating; Glucomannan; Peanut protein isolate; Ultrasonic treatment