...
首页> 外文期刊>International journal of food science & technology >Effects of microwave heating, steaming, boiling and baking on the structure and functional properties of quinoa (Chenopodium quinoa Willd.) protein isolates
【24h】

Effects of microwave heating, steaming, boiling and baking on the structure and functional properties of quinoa (Chenopodium quinoa Willd.) protein isolates

机译:微波加热,蒸汽,沸腾和烘烤对藜氨基藜(Chenopopodium藜tmaIld.)蛋白质分离物的结构和功能性能的影响

获取原文
获取原文并翻译 | 示例
   

获取外文期刊封面封底 >>

       

摘要

The effects of microwave heating (MW), steaming (SM), boiling (BL) and baking (BK) on the structure and functional properties of quinoa protein isolates (QPI) were investigated. SDS-PAGE showed the 20-30 kDa band strength of QPI-BL was enhanced, which indicated the disulphide bond was broken and protein molecules dissociated. Due to the recombination of subunits, some large molecular weight or insoluble polymer components of QPI-SM and QPI-BK did not pass through the gel. Microwave heating and boiling showed negative effects for α-helix and positive effects for P-sheet, which implied the molecular structure was transformed from ordered to disordered, the secondary structure became loose. The reduction of free SH (sulfhydryl) and surface hydrophobicity implied that aggregation and cross-linking of protein molecules for QPI-SM and QPI-BK. QPI, QPI-MW and QPI-BL exhibited better solubility, which was related to the water holding capacity (WHC) and emulsification. For QPI-SM and QPI-BK, functional properties (including solubility, WHC and gel-forming ability) decreased due to molecular aggregation. Heat treatments significantly affect the structure and functional properties of QPI, the current research showed that microwave heating and boiling might be better heat treatment methods for QPI and would help the development of quinoa protein products.
机译:研究了微波加热(MW),蒸汽(SM),沸腾(BL)和烘焙(BK)对奎奴亚藜蛋白分离株(QPI)的结构和功能性质的影响。 SDS-PAGE表明,增强了QPI-BL的20-30kDA带强度,表明了二硫键破裂,并解离蛋白质分子。由于亚基的重组,QPI-SM和QPI-BK的一些大分子量或不溶性聚合物组分没有通过凝胶。微波加热和煮沸对α-螺旋的负面影响和对P片的阳性作用,暗示分子结构从有序转化为无序,二次结构变得松动。自由SH(巯基)和表面疏水性的减少暗示蛋白质分子对QPI-SM和QPI-BK的聚集和交联。 QPI,QPI-MW和QPI-BL表现出更好的溶解度,与水持量(WHC)和乳化有关。对于QPI-SM和QPI-BK,由于分子聚集,功能性质(包括溶解度,WHC和凝胶形成能力)降低。热处理显着影响QPI的结构和功能性,目前的研究表明,微波加热和沸腾可能是QPI的更好的热处理方法,并有助于藜麦蛋白质产品的发展。

著录项

  • 来源
  • 作者单位

    College of Food and Biological Engineering Zhengzhou University of Light Industry Zhengzhou 450000 Henan China;

    College of Food and Biological Engineering Zhengzhou University of Light Industry Zhengzhou 450000 Henan China;

    College of Food and Biological Engineering Zhengzhou University of Light Industry Zhengzhou 450000 Henan China;

    College of Food and Biological Engineering Zhengzhou University of Light Industry Zhengzhou 450000 Henan China;

    College of Food Science and Technology Henan University of Technology Zhengzhou 450000 Henan China;

    Institute of Food Science and Technology Henan Academy of Agricultural Sciences Zhengzhou 450000 Henan China;

  • 收录信息
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    Functional properties; heat treatments; quinoa protein isolates; structure;

    机译:功能性质;热处理;藜麦蛋白质分离物;结构体;
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号