TGase酶法交联改善低温花生粕分离蛋白功能特性的研究

利用转谷氨酰胺酶(TGase)对低温花生粕分离蛋白(PPI)进行交联改性,对比不同交联时间(30,90,240min)对PPI功能特性的影响.结果表明:TGase可促使PPI亚基发生改变并形成高分子聚合物,随着交联程度的上升,PPI溶解性逐渐降低.TGases限制性交联(37℃交联90min)可明显提高PPI乳状液的稳定性,但交联时间过长将导致其制备的乳状液乳化活性及稳定性显著降低.DSC分析表明,TGase适度交联使PPI变性温度(Td)增加,变性焓值(ΔH)降低,表明TGase交联可使PPI热稳定性提高.

Effect of TGase Cross-linking on Functional Properties of Peanut Protein Isolate

Transglutaminase（TGase） was used to modify peanut protein isolate（PPI） and the effect of different incubation time（30min,90min and 240min） on the functional properties of PPI was studied.The results showed that TGase cross-linking induced the change of PPI subunits and the formation of high-molecular-weight polymers.when the incubation time of TGase cross-linking was increased,the decrease in solubility of PPI was observed.It was found that limited TGase cross-linking（37 ℃,90 min） could obviously improve the emulsion stability of PPI but overtreatment could result in the decrease of emulsion activity and stability.The increase of Td and the decrease of ΔH showed by DSC analysis further proved that TGase cross-linking could increase the thermal stability of PPI.