减轻淀粉衍生物对谷蛋白冷变性的影响:水合能力和构象行为的启示。

IF 5.7 1区 农林科学 Q1 AGRICULTURE, MULTIDISCIPLINARY
Journal of Agricultural and Food Chemistry Pub Date : 2024-11-27 Epub Date: 2024-11-18 DOI:10.1021/acs.jafc.4c08121
Yang Li, Haocun Kong, Caiming Li, Xiaofeng Ban, Zhengbiao Gu, Yujie Lu, Zhaofeng Li
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引用次数: 0

摘要

减轻面筋蛋白在冷冻储存过程中的冷变性对提高冷冻谷物产品的质量至关重要。我们之前的研究发现,淀粉衍生物,尤其是短簇麦芽糊精(SCMD),可以显著改善冷冻面团的质量,缓解面筋网络结构的恶化。为了进一步揭示短簇麦芽糊精在冷冻贮藏期间对面筋蛋白的低温保护机制,研究人员将短簇麦芽糊精与 DE2 麦芽糊精(MD)和预糊化淀粉(PGS)进行了比较,探讨了短簇麦芽糊精对面筋蛋白水合能力和构象行为的调节作用。结果表明,经过 8 周的冷冻储存后,SCMD 显著促进了结合水的保留,并降低了面筋蛋白的表面疏水性。观察发现,SCMD 对稳定面筋蛋白的二级结构和芳香族氨基酸的微环境有明显作用。进一步的机理研究表明,当温度从 300 K 降到 250 K 时,短簇结构通过与水的氢键和立体阻碍效应,而不是直接与蛋白质结合,比线性结构更明显地稳定了 α-螺旋。我们的发现将为谷蛋白的低温变性提供新的见解,并为选择最佳结构来抑制这种变性提供有用的指导,从而提高冷冻谷物产品的质量。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Mitigating the Effects of Starch Derivatives on Cold Denaturation of Gluten Protein: Insights from Hydration Capacity and Conformation Behavior.

Mitigating the Effects of Starch Derivatives on Cold Denaturation of Gluten Protein: Insights from Hydration Capacity and Conformation Behavior.

Mitigating the cold denaturation of gluten protein during frozen storage is crucial for the quality improvement of frozen cereal products. Our previous study observed that starch derivatives, especially short-clustered maltodextrin (SCMD), could significantly improve frozen dough quality, alleviating the deterioration of gluten-network structure. To further reveal the cryoprotection mechanism of SCMD on gluten protein during frozen storage, the modulatory roles of SCMD in the hydration capacity and conformation behavior of gluten protein were explored, in comparison with DE2 maltodextrin (MD) and pregelatinized starch (PGS). Results demonstrated that SCMD significantly facilitated the reservation of bound water and decreased the surface hydrophobicity of gluten protein after 8 weeks of frozen storage. Remarkable effects of SCMD on stabilizing the secondary structure and microenvironment of aromatic amino acids of gluten protein were observed. Further mechanistic investigation showed that when the temperature dropped from 300 to 250 K, the short-clustered structure could stabilize the α-helixes more evidently than linear structures through hydrogen bonds with water and steric hindrance effect, rather than directly with protein. Our findings will provide novel insights into the cold denaturation of gluten protein and useful guidance in selecting the optimum structure to suppress this denaturation, improving the quality of frozen cereal products.

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来源期刊
Journal of Agricultural and Food Chemistry
Journal of Agricultural and Food Chemistry 农林科学-农业综合
CiteScore
9.90
自引率
8.20%
发文量
1375
审稿时长
2.3 months
期刊介绍: The Journal of Agricultural and Food Chemistry publishes high-quality, cutting edge original research representing complete studies and research advances dealing with the chemistry and biochemistry of agriculture and food. The Journal also encourages papers with chemistry and/or biochemistry as a major component combined with biological/sensory/nutritional/toxicological evaluation related to agriculture and/or food.
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