Effects of preheating treatment on thermal property and adhesion performance of soy protein isolates

被引:18
作者
Wang, Ying [1 ]
Sun, Xiuzhi Susan [2 ]
Wang, Donghai [1 ]
机构
[1] Kansas State Univ, Dept Biol & Agr Engn, Manhattan, KS 66506 USA
[2] Kansas State Univ, Dept Grain Sci & Ind, Biomat & Technol Lab, Manhattan, KS 66506 USA
关键词
adhesion strength; esterification; protein modification; SDS-PAGE; solubility; soy protein; thermal property; water resistance;
D O I
10.1163/156856107782844756
中图分类号
TQ [化学工业];
学科分类号
0817 ;
摘要
The objective of this research was to study the effects of preheating treatment and thermal-setting temperature on the thermal properties and adhesion performance of esterified and cross-linked soy protein isolates. Preheating treatment was achieved by heating a soy protein isolate suspension (5% solid) for 20 min at 60, 80, 110 or 130 degrees C. Thermal-setting temperatures of 130, 160, 190 and 220 degrees C were achieved by adjusting the temperature of the hot press. Differential scanning calorimetry and sodium dodecyl sulfate-polyacrylamide gel electrophoresis were used to determine changes in the protein structure before and after preheating treatment. Preheating treatment had a significant effect on protein structure and adhesion performance. Adhesion strength of control and esterified soy protein isolates reached maximum at 80 degrees C preheating temperature. Severe preheating (over 110 degrees C) caused complete denaturation of proteins and loss of their native structure and was, therefore, detrimental to adhesion performance. Thermal-setting temperature also had a significant effect on protein structure and wet strength of the soy protein isolates. Wet adhesion strength of unmodified, esterified, and cross-linked soy protein isolates increased by 170%, 128% and 80%, respectively, as the thermal-setting temperature increased from 130 to 220 degrees C.
引用
收藏
页码:1469 / 1481
页数:13
相关论文
共 22 条
[1]   Emulsifying behaviour of 11S globulin Vicia faba in mixtures with sulphated polysaccharides:: comparison of thermal and high-pressure treatments [J].
Galazka, VB ;
Dickinson, E ;
Ledward, DA .
FOOD HYDROCOLLOIDS, 1999, 13 (05) :425-435
[2]   Alkali-modified soy protein with improved adhesive and hydrophobic properties [J].
Hettiarachchy, NS ;
Kalapathy, U ;
Myers, DJ .
JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY, 1995, 72 (12) :1461-1464
[3]  
HIRANO H, 1987, PHYTOCHEMISTRY, V26, P41, DOI 10.1016/S0031-9422(00)81477-6
[4]   Adhesive properties of soy proteins modified by sodium dodecyl sulfate and sodium dodecylbenzene sulfonate [J].
Huang, WN ;
Sun, XZ .
JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY, 2000, 77 (07) :705-708
[5]   Adhesive properties of soy proteins modified by urea and guanidine hydrochloride [J].
Huang, WN ;
Sun, XZ .
JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY, 2000, 77 (01) :101-104
[6]   CHANGES IN THE EMULSIFYING AND FOAMING PROPERTIES OF PROTEINS DURING HEAT DENATURATION [J].
KATO, A ;
OSAKO, Y ;
MATSUDOMI, N ;
KOBAYASHI, K .
AGRICULTURAL AND BIOLOGICAL CHEMISTRY, 1983, 47 (01) :33-37
[7]   Enzymatically-modified soy protein part 2: adhesion behaviour [J].
Kumar, R ;
Choudhary, V ;
Mishra, S ;
Varma, IK .
JOURNAL OF ADHESION SCIENCE AND TECHNOLOGY, 2004, 18 (02) :261-273
[8]  
LAEMMLI UK, 1985, NATURE, V227, P680
[9]   Thermal properties and adhesion strength of modified soybean storage proteins [J].
Mo, XQ ;
Sun, XZ ;
Wang, DH .
JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY, 2004, 81 (04) :395-400
[10]  
Mo XQ, 1999, J APPL POLYM SCI, V73, P2595, DOI 10.1002/(SICI)1097-4628(19990923)73:13<2595::AID-APP6>3.0.CO