Emulsifying and foaming properties of transglutaminase-treated wheat gluten hydrolysate as influenced by pH, temperature and salt

被引:141
作者
Agyare, Kingsley K. [2 ]
Addo, Kwaku [1 ]
Xiong, Youling L. [2 ]
机构
[1] Univ Kentucky, Dept Nutr & Food Sci, Lexington, KY 40506 USA
[2] Univ Kentucky, Dept Anim & Food Sci, Lexington, KY 40546 USA
关键词
hydrolyzed wheat gluten; emulsifying properties; foaming properties; microbial transglutaminase; FUNCTIONAL-PROPERTIES; MICROBIAL TRANSGLUTAMINASE; ENZYMATIC-HYDROLYSIS; SDS-ELECTROPHORESIS; PHYSICAL-PROPERTIES; SURFACE-PROPERTIES; PROTEIN ISOLATE; MEAT-PRODUCTS; DROPLET SIZE; EMULSIONS;
D O I
10.1016/j.foodhyd.2007.11.012
中图分类号
O69 [应用化学];
学科分类号
070301 [无机化学];
摘要
Hydrolyzed wheat gluten (GH, 77-85% protein) was prepared by limited hydrolysis with chymotrypsin at 37 degrees C for 4 h (degree of hydrolysis = 6.4%) and 15 h (degree of hydrolysis = 10.3%). The effect of microbial transglutaminase (MTGase) treatment (55 degrees C for I h, or 5 degrees C for 18h) on the emulsifying and foaming properties of GH was evaluated under selected food processing conditions (pH 4.0 and 6.5, 0 and 0.6 M NaCl, and temperature 20 and 5 degrees C). At pH 4.0 and OM NaCl the MTGase treatment substantially increased foaming capacity (FC) of GH compared with their respective control GH samples, as a result of enhanced peptide adsorption to the air-water interface, but FC was similar for both control and MTGase-treated GH at pH 6.5. In contrast, foam drainage stability (FS) of MTGase-treated GH decreased at pH 4.0, but increased significantly (P<0.05) at pH 6.5 when compared with their respective control GH samples. The FC and FS were affected by 0.6 M NaCl in a pH-dependent manner. The MTGase treatments increased emulsion activity index up to 15-fold at pH 6.5, while emulsion stability index was influenced by emulsion temperature and ionic strength conditions. The MTGase-induced changes in functional properties of GH were attributed to pH-dependent Solubility changes, the amphiphilic nature of gluten peptides and increased electrostatic repulsion resulting from deamidation. Published by Elsevier Ltd.
引用
收藏
页码:72 / 81
页数:10
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