咖啡酸-葡聚糖-肌原纤维蛋白酶解物乳液稳定性的研究

Stability of Emulsions Stabilized by Caffeic Acid-glucan-myofibrillar Protein Hydrolysate Complexes

为了探究咖啡酸(Caffeic Acid,CA)、葡聚糖(Dextran,DEX)复合修饰联合胰蛋白酶不完全酶解对于肌原纤维蛋白(Myofibrillar Protein,MP)乳化特性的提升效果,以CA-DEX-MP复合酶解物为乳液稳定剂制备乳液,优化稳定剂的添加剂量,并以原始MP和MP酶解物稳定的乳液为对照,评估乳液在不同环境刺激下的稳定性。结果表明,CA-DEX-MP酶解物添加量为3 wt.%时乳液具有较低的颗粒粒径(390.26 nm)、电位(-23.6 mV)和较高的界面蛋白吸附量(11.22 mg/mL),且均匀分布;流变性研究表明,该乳液体系显示出显著低于原始MP乳液的表观粘度,可有效避免乳液的相分离现象。3 wt.%CA-DEX-MP复合酶解物乳液在不同温度、酸碱、盐离子强度和28 d贮藏期下均表现出较优的稳定性,可实现乳液的稳定。最终结果表明,乳液稳定剂为3 wt.%CA-DEX-MP复合酶解物时,乳液拥有最高的稳定性。该研究可为肌原纤维蛋白在新型食品乳液稳定剂开发中的应用提供理论支撑和方法学指引。

In order to explore the enhancement effects of composite modification by caffeic acid(CA)and dextran(DEX),a type of glucan,combined with incomplete enzymatic digestion by trypsin on the emulsification properties of myofibrillar proteins(MP),a CA-DEX-MP composite hydrolysate was used as an emulsion stabilizer to prepare emulsions and determine the optimal stabilizer addition amount.The stability of CA-DEX-MP-stabilized emulsions under different environmental stimuli was evaluated by using the raw MP-stabilized and MP hydrolysate-stabilized emulsions as controls.The results showed that when the addition rate of a CA-DEX-MP hydrolysate was 3 wt.%,the particle size and potential of the emulsion were smaller(390.26 nm and-23.6 mV,respectively),and the interfacial protein adsorption capacity was higher(11.22 mg/mL),with an even protein distribution.The rheological study demonstrated that the apparent viscosity of the CA-DEX-MP hydrolysate-stabilized emulsion was significantly lower than that of the raw MP-stabilized emulsion.Hence,phase separation can be effectively avoided.The 3 wt.%CA-DEX-MP-stabilized emulsion showed better stability under different temperatures,pH values,and salt ionic strengths after 28 days of storage.These results indicate successful stabilization of the emulsion.The final results demonstrate that when 3 wt.%CA-DEX-MP hydrolysate is used as the stabilizer,the emulsion exhibits the highest stability.The above findings can provide theoretical support and methodological guidance for the application of myofibrillar proteins in the development of novel food emulsion stabilizers.