Physicochemical properties of peanut protein isolate-glucomannan conjugates prepared by ultrasonic treatment

被引:152
|
作者
Li, Chen [1 ,2 ]
Huang, Xingjian [3 ]
Peng, Qiang [1 ]
Shan, Yuanyuan [1 ]
Xue, Feng [1 ]
机构
[1] Northwest A&F Univ, Coll Food Sci & Engn, Yangling 712100, Shaanxi, Peoples R China
[2] Jiangnan Univ, Sch Food Sci & Technol, State Key Lab Food Sci & Technol, Wuxi 214122, Jiangsu, Peoples R China
[3] Huazhong Agr Univ, Dept Food Sci & Technol, Wuhan 430070, Peoples R China
基金
中国国家自然科学基金;
关键词
Peanut protein isolate; Glucomannan; Classical heating; Ultrasonic treatment; BETA-LACTOGLOBULIN; FUNCTIONAL-PROPERTIES; SOY PROTEIN; MAILLARD REACTION; POLYSACCHARIDE CONJUGATE; CARBOXYMETHYL DEXTRAN; KONJAC GLUCOMANNAN; IMPROVEMENT; STABILITY; INTENSIFICATION;
D O I
10.1016/j.ultsonch.2014.03.018
中图分类号
O42 [声学];
学科分类号
070206 ; 082403 ;
摘要
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 alpha-helix, more beta-structures and random coil, higher surface hydrophobicity and less compact tertiary structure as compared to those obtained by classical heating and native PPI. (C) 2014 Elsevier B.V. All rights reserved.
引用
收藏
页码:1722 / 1727
页数:6
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