Engineering Research Center of Bio-process, Ministry of Education, Hefei University of Technology, 193 Tunxi Road, Hefei, Anhui 230009, PR China; School of Food Science and Engineering, Hefei University of Technology, Hefei, Anhui 230009, PR China.
Engineering Research Center of Bio-process, Ministry of Education, Hefei University of Technology, 193 Tunxi Road, Hefei, Anhui 230009, PR China.
Food Chem. 2025 Feb 1;464(Pt 2):141681. doi: 10.1016/j.foodchem.2024.141681. Epub 2024 Oct 16.
Although frozen dough technology has demonstrated significant benefits, the mechanisms underlying dough deterioration during freezing remain unclear. To overcome this obstacle, the effect of freezing-induced deteriorations of wheat starch granular surface proteins (SGSPs)-high/low molecular weight (HMW/LMW) glutenins complexes were analyzed from the molecular to macroscopic scales. After 7 cycles of freezing/thawing treatment, SGSPs-LMW complex showed a higher antifreeze stability than SGSPs-HMW complex. The freezable water content of SGSPs-HMW increased from 32 % to 39 %, indicating a marked migration and recrystallization of ice. In this situation, the interactions of SGSPs-HMW complex were affected and destabilized, leading to partially denatured and depolymerized molecular structures. Furthermore, the bulk protein aggregation network was also dissociated under the ice tearing and splitting, which irreversibly collapsed to small molecular protein particles. In comparison, the resistance of SGSPs-LMW complex on continued network disruption appear to be the key to maintain the quality of frozen dough.
尽管冷冻面团技术已经显示出显著的优势，但面团在冷冻过程中劣化的机制仍不清楚。为了克服这一障碍，本研究从分子到宏观尺度分析了冷冻诱导的小麦淀粉颗粒表面蛋白（SGSPs）-高分子量/低分子量（HMW/LMW）谷蛋白复合物劣化的影响。经过 7 次冻融处理后，SGSPs-LMW 复合物表现出比 SGSPs-HMW 复合物更高的抗冻稳定性。SGSPs-HMW 的可冻结水含量从 32%增加到 39%，表明冰的明显迁移和重结晶。在这种情况下，SGSPs-HMW 复合物的相互作用受到影响并失稳，导致部分变性和分子结构解聚。此外，在冰的撕裂和分裂下，大量蛋白质聚集网络也发生解离，不可逆地坍塌成小分子蛋白质颗粒。相比之下，SGSPs-LMW 复合物对持续网络破坏的抵抗力似乎是保持冷冻面团质量的关键。
