Redox agents and N-ethylmaleimide affect the extractability of gluten proteins during fresh pasta processing
Redox agents and N-ethylmaleimide affect the extractability of gluten proteins during fresh pasta processing
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DOI：
10.1016/j.foodchem.2011.01.048
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发表时间：
2011-08-01
期刊：
影响因子：
8.8
通讯作者：
Delcour, Jan A.
中科院分区：
文献类型：
--
作者：
Bruneel, Charlotte;Lagrain, Bert;Delcour, Jan A.
面筋蛋白网络对面食的烹饪质量具有重要意义。在实验室规模的新鲜面食制作（混合和擀面）和烹饪过程中，氧化还原剂被用作影响蛋白质网络形成的工具。SE-和RP-HPLC数据表明，在新鲜面食烹饪过程中，预先存在的面筋蛋白网络中形成了二硫键，并且在此过程中，面筋蛋白聚合比麦胶蛋白-面筋蛋白共聚发生得更快。硫醇阻断剂n-乙基马来酰亚胺（245ppm，在粗面粉上表达，干基）和氧化剂碘酸钾（70ppm）在较小程度上阻碍了烹饪过程中谷蛋白聚合和麦胶蛋白-谷蛋白共聚。然而，通过添加还原剂谷胱甘肽（100ppm）引入反应性硫醇基团，导致在焦化过程中更快的麦胶蛋白-谷蛋白共聚。(C) 2011 Elsevier Ltd.版权所有。
The gluten protein network is of great importance for pasta cooking quality. Redox agents were used as a tool to impact the protein network formation during laboratory scale fresh pasta making (mixing and sheet rolling) and cooking. SE- and RP-HPLC data showed that disulphide bonds are formed in the preexisting gluten protein network during cooking of fresh pasta and that, in the process, glutenin polymerisation occurs faster than gliadin-glutenin copolymerisation. The thiol blocking agent N-ethylmaleimide (245 ppm, expressed on semolina, dry basis) and, to a lesser extent, the oxidising agent potassium iodate (70 ppm), hindered glutenin polymerisation and gliadin-glutenin copolymerisation during cooking. However, the introduction of reactive thiol groups, by addition of the reducing agent glutathione (100 ppm), resulted in faster gliadin-glutenin copolymerisation during cocking. (C) 2011 Elsevier Ltd. All rights reserved.