Film-forming mechanism and heat denaturation effects on the physical and chemical properties of pea-protein-isolate edible films

被引:71
作者
Choi, WS
Han, JH [1 ]
机构
[1] Univ Manitoba, Dept Food Sci, Winnipeg, MB R3T 2N2, Canada
[2] Chung Ju Natl Univ, Dept Food Sci & Technol, Chungju, Chungbuk, South Korea
关键词
yellow-field-peas (Pisum sativum L. Miranda); edible film; tensile property; wettability; surface energy; electrophoresis; FTIR;
D O I
10.1111/j.1365-2621.2002.tb10297.x
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Pea-protein isolate solutions were heat-denatured and dried to form stand-alone edible films. Heat treatment at 90 degreesC over 5 min increased tensile strength and elongation-at-break, and decreased the elastic modulus. No significant differences were found in the initial contact angle of water and surface energies of heat-denatured films from those of nonheated films except for the 20 min heat-treated film. Additionally, heat denaturation reduced the water absorption rate of the films to 19 to 40% of the nonheated film. FTIR spectroscopy showed that more water existed in the nonheated films as compared to the heat-denatured films. Electrophoresis studies suggested that intermolecular disulfide bonds were created during heat denaturation, which resulted in increased film integrity.
引用
收藏
页码:1399 / 1406
页数:8
相关论文
共 26 条
[1]   Effects of bound water on FTIR spectra of glycinin [J].
Abbott, TP ;
Nabetani, H ;
Sessa, DJ ;
Wolf, WJ ;
Liebman, MN ;
Dukor, RK .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 1996, 44 (08) :2220-2224
[2]  
*AOAC, 1990, OFF METH AN, V1, P342
[3]  
*ASTM, 1987, ANN BOOK AM SOC TEST, P42
[4]  
ASTM, 1991, Annual book of American standard testing methods, P313
[5]  
BLACK J, 1992, BIOL PERFORMANCE MAT, P73
[6]  
CHANG R, 1981, PHYSICAL CHEM APPL B, P505
[7]  
CHERIAN G, 1995, CEREAL CHEM, V72, P1
[8]   Physical and mechanical properties of pea-protein-based edible films [J].
Choi, WS ;
Han, JH .
JOURNAL OF FOOD SCIENCE, 2001, 66 (02) :319-322
[9]   Changes in the secondary structure of bovine casein by Fourier transform infrared spectroscopy: Effects of calcium and temperature [J].
Curley, DM ;
Kumosinski, TF ;
Unruh, JJ ;
Farrell, HM .
JOURNAL OF DAIRY SCIENCE, 1998, 81 (12) :3154-3162
[10]   The conformation of α-lactalbumin as a function of pH, heat treatment and adsorption at hydrophobic surfaces studied by FTIR [J].
Fang, Y ;
Dalgleish, DG .
FOOD HYDROCOLLOIDS, 1998, 12 (02) :121-126