为改善油莎豆蛋白(Cyperus esculentus L.protein,CEP)乳化性扩大其在食品加工领域中应用,考察酶水解、酶水解结合酶促糖基化对CEP乳化特性的影响。首先使用木瓜蛋白酶水解CEP,以乳化稳定性为指标进行单因素试验,制备得到油莎豆蛋白水解物(Cyperus esculentus L.protein hydrolysate,CEPH);再使用谷氨酰胺转氨酶(transglutaminase,TG酶)将CEPH、壳聚糖(chitosan,CTS)交联,以接枝度为指标,通过单因素试验确定CEPH、CTS共价结合最适条件,制备CEPH-CTS。结果表明,水解降低了CEP表面疏水性并提高其溶解度,使得CEP乳化性大幅提升。由于CTS的引入,CEPH-CTS结构更加灵活,溶解度再次提升。傅里叶变换红外光谱显示CEPH-CTS具有较多的无规则卷曲结构,与CEP、CEPH相比分别增加了40.65%和32.39%。差示扫描量热仪结果显示,CEPH-CTS具有复杂且有序的结构,热稳定性优于CEPH。CEPH-CTS的乳化稳定性较CEP、CEPH分别提高了390.53%和40.79%。综上,酶水解结合酶促糖基化提升了CEP乳化稳定性,可为食品及饮料乳化剂的开发提供新选择。
To improve the emulsifying properties of Cyperus esculentus L.protein (CEP) and expand its application in the food processing field, the effects of enzymatic hydrolysis and enzymatic hydrolysis combined with enzymatic glycosylation on the emulsifying characteristics of CEP were investigated.First, CEP was hydrolyzed using papain, and a single-factor experiment was conducted with emulsifying stability as the indicator to prepare Cyperus esculentus L.protein hydrolysate (CEPH).CEPH and chitosan (CTS) were cross-linked with transglutaminase (TGase), and the degree of grafting was used as an indicator.The optimal conditions for the covalent binding of CEPH and CTS were determined through single-factor experiments, and CEPH-CTS was prepared.The results indicated that hydrolysis reduced the hydrophobicity of CEP surface and increased its solubility, which significantly enhanced the emulsifying property of CEP.The results indicated that hydrolysis reduced the hydrophobicity of CEP surface and increased its solubility, which significantly enhanced the emulsifying property of CEP.Due to the introduction of CTS, the CEPH-CTS structure is more flexible and its solubility has been further improved.Fourier transform infrared spectroscopy shows that CEPH-CTS has a significantly higher degree of irregular coiling, increasing by 40.65% compared to CEP and by 32.39% compared to CEPH.The results of differential scanning calorimetry show that CEPH-CTS has a complex and ordered structure, and its thermal stability is superior to that of CEPH.The emulsification stability of CEPH-CTS was increased by 390.53% and 40.79% compared with that of CEP and CEPH, respectively.In conclusion, the combination of enzymatic hydrolysis and TGase-induced glycation enhances the emulsifying stability of CEP, which can provide a new option for the development of emulsifiers in food and beverages.
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