摘要
研究了手工揉面过程中面团面筋蛋白结构的变化。结果表明:揉面过程中,揉面初期(2 min)面团游离巯基下降10.69%,二硫键增加4.48%,随后缓慢增长或下降;氢键显著增多(P<0.05),疏水作用力显著下降(P<0.05);二级结构中的无规则卷曲初始骤降56.52%,β-折叠初始增加32.34%,随后小幅增长或下降,α-螺旋和β-转角无明显变化;面筋蛋白、麦醇溶蛋白、麦谷蛋白的SDS可萃取率均有不同程度下降;B/C-LMW-GS峰面积分别增加4.56%,2.61%,4.11%,6.73%,3.18%,0.81%,α-麦醇溶蛋白亚基峰面积分别降低22.42%,10.87%,11.59%,12.87%,9.22%,4.35%。手工揉面促进了面筋蛋白的交联聚合反应,使其蛋白构象朝着更为有序和稳定方向发展,进而增强了面团的黏弹性。
This experiment investigated the changes of the gluten protein structure of the dough during manual kneading.Results:At the first 2 minutes of kneading,the free sulfhydryl group in the dough was decreased by 10.69%,the disulfide bond was increased by 4.48%,and then was slowly increased or decreased;the hydrogen bonds was increased significantly(P<0.05),and the hydrophobic force was decreased significantly(P<0.05);the random coil in the secondary structure had an initial sharp drop of56.52%,and theβ-sheet had an initial increase of 32.34%,followed by a small increase or decrease,and theα-helix andβ-turn have no significant changes;The SDS extractable rates of glutenin all decreased to varying degrees;the peak area of B/CLMW-GS increased by 4.56%,2.61%,4.11%,6.73%,3.18%,0.81%,and the peak area ofα-gliadins decreased by 22.42%,10.87%,11.59%,12.87%,9.22%,and 4.35%,respectively.Hand kneading promoted the cross-linking polymerization reaction of gluten protein and made its protein conformation develop in a more orderly and stable direction,thereby enhanced the viscoelasticity of the dough.
作者
孟莲
周惠明
朱科学
郭晓娜
MENG Lian;ZHOU Hui-ming;ZHU Ke-xue;GUO Xiao-na(School of Food Science and Technology,Jiangnan University,Wuxi,Jiangsu 214122,China;Jiangsu Collaborative Innovation Center for Modern Grain Circulation and Safety,Nanjing,Jiangsu 210000,China)
出处
《食品与机械》
北大核心
2020年第2期19-24,共6页
Food and Machinery
基金
国家自然科学基金(编号:31772006)。
关键词
小麦面团
分子间作用
蛋白亚基
二级结构
wheat dough
molecular interaction
protein subunit
secondary structure
