微波-超声波协同影响菜籽蛋白糖基化改性
作者:
Zhang, Yanpeng
(张燕鹏);Zhang, Manjun;Qi, Yutang;Zhang, Weinong;Zhu, Xianbin
期刊:
食品科学,2017年38(17):114-119 ISSN:1002-6630
通讯作者:
Zhang, Weinong(zhangweinong@163.com)
作者机构:
[Zhang, Yanpeng; Zhang, Weinong; Zhang, Manjun; Qi, Yutang; Zhu, Xianbin] College of Food Science and Engineering, Wuhan Polytechnic University, Wuhan, 430023, China
关键词:
微波-超声波协同作用;糖基化;菜籽蛋白;功能特性;分子结构
摘要:
采用微波-超声波协同作用强化菜籽蛋白的糖基化改性,并对所得糖基化产物进行了功能性质和分子结构的对比分析。结果表明,当改性条件为微波功率500 W、超声波功率300 W、协同作用时间7 min时,菜籽蛋白的接枝度可达67.1%,显著高于湿热法和微波法制备的糖基化产物,有效提高了蛋白质糖基化反应的效率;协同作用可显著改善所得糖基化产物的溶解性、乳化活性、起泡能力、泡沬稳定性,分别提高至55.7%、13.9 m~2/g、50.0%和80.0%:糖基化产物的表面疏水性和圆二色谱结果分析表明,微波和超声波处理使得菜籽蛋白的分子展开,表面疏水性和分子柔性增加,从而促进了糖基化反应的进行,改善了蛋白质糖基化产物的功能特性。
语种:
中文
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Structural characterization and physicochemical properties of protein extracted from soybean meal assisted by steam flash-explosion with dilute acid soaking
作者:
Zhang, Yanpeng
(张燕鹏);Yang, Ruijin
*;Zhang, Weinong;Hu, Zhixiong;Zhao, Wei
期刊:
Food Chemistry,2017年219:48-53 ISSN:0308-8146
通讯作者:
Yang, Ruijin
作者机构:
[Zhang, Yanpeng; Zhang, Weinong; Hu, Zhixiong] Wuhan Polytech Univ, Coll Food Sci & Engn, Wuhan 430023, Hubei, Peoples R China.;[Zhao, Wei; Yang, Ruijin] Jiangnan Univ, State Key Lab Food Sci & Technol, Wuxi 214122, Jiangsu, Peoples R China.
通讯机构:
[Yang, Ruijin] J;Jiangnan Univ, State Key Lab Food Sci & Technol, Wuxi 214122, Jiangsu, Peoples R China.
关键词:
Dilute acid soaking;Physicochemical properties;Soybean protein isolate;Steam flash-explosion;Structural characterization
摘要:
The aim of this work was to analyze the influence of steam flash-explosion (SFE) with dilute acid soaking pretreatment on the structural characteristics and physiochemical properties of protein from soybean meal (SBM). The pretreatment led to depolymerisation of soy protein isolate (SPI) and formation of new protein aggregation through non-disulfide covalent bonds, which resulted in broader MW distribution of SPI. The analysis of CD spectroscopy showed that the SFE treatment induced minor changes in secondary structure, however, the intrinsic tryptophan fluorescence revealed that acid soaking and SFE treatment pronouncedly altered the tertiary structure of SPI. The protein zeta potential was shown to be increased after SFE treatment attributed to the changes in protein structure and the covalent coupling between carbohydrate and protein. These results contribute to clarifying the mechanisms of the effect of pretreatment on SPI structure, thus moving further toward implementing SFE in the processing chain of SPI. © 2016 Elsevier Ltd
语种:
英文
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