作　　者： ; ; ; ; ;

机构地区： 东北农业大学食品学院

出　　处： 《现代食品科技》 2015年第10期203-209,共7页

摘　　要： 卵白蛋白是蛋清中的主要蛋白质,利用卵白蛋白制备ACE抑制肽可为其高值利用提供参考。本文采用离子交换色谱对卵白蛋白的粗酶解物进行脱盐处理,确定了室温25℃、20 m L进样量、8 BV/h的脱盐工艺条件。在上述条件下,酶解物脱盐率达到83.6%,氮回收率和ACE(血管紧张素转换酶)抑制率分别为87.71%和80.31%。再采用截留分子量为10 ku和3 ku的两种超滤膜将脱盐酶解物分离成>10 ku、3~10 ku和<3 ku三个组分,最佳操作条件:超滤时间40 min、操作压力1.5 bar、温度35℃(10 ku)和30℃(3 ku)。超滤所得三个组分均具有ACE抑制活性,其中分子量<3 ku的超滤物活性最高,该组分与粗酶解物相比较,总巯基和表面巯基含量显著降低(p<0.05),同时表面疏水性显著提高(p<0.05),热稳定性增加。因此,卵白蛋白的粗酶解物经脱盐、超滤处理,可以明显去除其中的盐分,并得到ACE抑制活性较高的分离组分。 The preparation of angiotensin converting enzyme(ACE) inhibitory peptides from ovalbumin, the main protein in egg whites, can provide a reference for their value-added application. The desalination of crude enzymatic hydrolysates from ovalbumin in this paper was performed by ion exchange chromatography, using the following desalting conditions: room temperature(25 ℃), sample load of 20 m L, and flow rate of 8 BV/h. Under these conditions, the desalination rate of hydrolysates, nitrogen recovery rate, and ACE inhibition rate were 83.6%, 87.71%, and 80.31%, respectively. Two ultrafiltration membranes with molecular weight cut-offs of 10 ku and 3 ku were employed to separate the desalinated hydrolysates into three fractions: >10 ku, 3~10 ku, and <3 ku. The optimal operating conditions were as follows: ultrafiltration time of 40 min, operating pressure of 1.5 bar, and temperature of 35 for 10 ℃ ku or 30 ℃ for 3 ku. All three fractions showed ACE inhibitory activity, and the highest activity was found in the <3 ku fraction. Compared to crude hydrolysates, the total and surface hydrosulfuryl contents of the <3 ku fraction were significantly decreased(p < 0.05), the surface hydrophobicity was increased(p < 0.05), and thermal stability was improved. Therefore, desalination and ultrafiltration treatments can effectively reduce the salt content of crude enzymatic hydrolysates of ovalbumin and produce a fraction with high ACE inhibitory activity.

关 键 词： 卵白蛋白 抑制肽 脱盐 超滤

领　　域： [轻工技术与工程] [轻工技术与工程]