利用转谷氨酰胺酶（TGase）将花生分离蛋白（PPI）与蓝园碜酶解物（DPH）进行酶法交联，并经高压均质制成O／W型乳状液，研究TGase的交联作用对乳状液粒度分布、表面积平均粒径、显微结构及离心乳析率等的影响．结果表明：TGase可促使PPI与不同水解度的DPH交联，与交联前的电泳图相比，低分子质量亚基条带（14～31ku）消褪，高分子质量亚基条带（大于97ku）生成；DPH的水解程度对交联物的乳化性有重要影响，水解度为5．5％时所得交联物具有较好的乳化特性；交联作用提高了PPI-DPH异源蛋白的乳化活性与乳化稳定性．

Peanut protein isolate （PPI） was cross-linked with Decapterus maruadsi protein hydralysate （DPH） under the catalyzing of transglutaminase （TGase）, and oil-in-water emulsions of the samples were prepared via the high-pressure homogenization. Then, the effects of the cross-linking on the particle size distribution, the mean diameter per particle surface area, the microstructure and the centrifugal creaming rate of the emulsions were analyzed. The results indicate that （1） TGase accelerates the linkage between PPI and DPH with different hydrolysis degrees; （2） in the electrophoretograms of the cross-linked samples, the subunit bands with low molecular mass （ 14 -31 ku） disappear while the bands with high molecular mass （ more than 97 ku） appear; （3） the hydrolysis degree of DPH greatly improves the emulsifying properties of PPI-DPH, especially at a value of 5.5% ; and （4） the TGase cross-linking improves the emulsifying activity and emulsion stability of the cross-linked PPI-DPH.