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[采用相转化高压液相色谱法分析未处理和热处理面粉中的全醇溶蛋白]

[Analysis of whole gliadin from untreated and heat-treated flour with phase inversion high pressure liquid chromatography].

作者信息

Meier P, Windemann H, Baumgartner E

出版信息

Z Lebensm Unters Forsch. 1985 Jun;180(6):467-73. doi: 10.1007/BF02044296.

Abstract

The gliadins from various wheat flours either untreated or heated (baking, cooking, roller-drying, extrusion-cooking) were extracted with 70% ethanol and analysed by RP-HPLC. When flours are heated below 80 degrees C the chromatograms showed no significant change. At temperatures about 80-90 degrees C a peak appeared in all samples (with the exception of durum wheat) at a retention time of 35 min (peak 35) or, if already present, become more pronounced. A further increase in temperature or treatment time resulted in an increase in this peak whereas the peaks of the more strongly bound gliadins slowly disappeared. In the gliadins of the bread crust the amount of peak 35 decreased again. Similarly, changes were observed in the distribution of the apparent molecular weights of gliadins from heated flours by using gel electrophoresis (SDS-PAGE). At temperatures about 80-90 degrees C the bands between 50-62 kD (under reducing conditions) appeared or become stronger. Their intensity increased with increasing time and treatment temperature whereas the lower molecular weight bands slowly disappeared. Peak 35 may be useful as an indicator of gliadin in heat-treated "gluten-free" foods.

摘要

用70%乙醇提取未处理或经过加热(烘焙、蒸煮、滚筒干燥、挤压蒸煮)的各种小麦粉中的醇溶蛋白,并通过反相高效液相色谱(RP-HPLC)进行分析。当面粉在80℃以下加热时,色谱图没有显著变化。在约80-90℃的温度下,所有样品(除硬质小麦外)在保留时间35分钟时出现一个峰(峰35),或者如果该峰已经存在,则变得更加明显。温度或处理时间进一步增加导致该峰增加,而结合更紧密的醇溶蛋白的峰则慢慢消失。在面包皮的醇溶蛋白中,峰35的量再次减少。同样,通过凝胶电泳(SDS-PAGE)观察到加热面粉中醇溶蛋白的表观分子量分布发生了变化。在约80-90℃的温度下,50-62 kD之间的条带(在还原条件下)出现或变强。它们的强度随着时间和处理温度的增加而增加,而较低分子量的条带则慢慢消失。峰35可作为热处理“无麸质”食品中醇溶蛋白的一个指标。

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