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Effects of microwave heating, steaming, boiling and baking on the structure and functional properties of quinoa (Chenopodium quinoa Willd.) protein isolates
International Journal of Food Science & Technology ( IF 3.3 ) Pub Date : 2020-07-07 , DOI: 10.1111/ijfs.14706
Lei Wang 1 , Ji‐lin Dong 1 , Ying‐ying Zhu 1 , Rui‐ling Shen 1 , Li‐gen Wu 2 , Kang‐yi Zhang 3
Affiliation  

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 β‐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.

中文翻译:

微波加热,蒸煮和烘烤对藜麦(Chenopodium quinoa Willd。)分离蛋白的结构和功能特性的影响

研究了微波加热(MW),蒸煮(SM),沸腾(BL)和烘烤(BK)对藜麦分离蛋白(QPI)的结构和功能特性的影响。SDS-PAGE显示QPI-BL的20–30 kDa带强度得到增强,这表明二硫键断裂且蛋白质分子解离。由于亚基的重组,QPI-SM和QPI-BK的某些大分子量或不溶性聚合物组分无法通过凝胶。微波加热和煮沸对α-螺旋显示出负面影响,对β-折叠显示出正面影响,这意味着分子结构从有序转变为无序,二级结构变得松散。游离SH(巯基)和表面疏水性的降低意味着QPI-SM和QPI-BK蛋白质分子的聚集和交联。QPI,QPI-MW和QPI-BL表现出更好的溶解性,这与保水量(WHC)和乳化有关。对于QPI-SM和QPI-BK,功能特性(包括溶解度,WHC和凝胶形成能力)由于分子聚集而降低。热处理显着影响QPI的结构和功能特性,目前的研究表明,微波加热和煮沸可能是QPI更好的热处理方法,并将有助于藜麦蛋白产品的开发。
更新日期:2020-07-07
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