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首页> 外文期刊>Food Science & Nutrition >Rheological and structural properties of enzyme‐induced gelation of milk proteins by ficin and Polyporus badius
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Rheological and structural properties of enzyme‐induced gelation of milk proteins by ficin and Polyporus badius

机译：丝蛋白和猪Poly的酶促乳蛋白凝胶化的流变和结构特性

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The rheological and microstructural characteristics of ewes’ milk curd obtained by coagulating with milk‐clotting enzymes, including ficin extract and Polyporus badius were evaluated. The gelation of milk was examined by small amplitude oscillatory shear measurements (SAOS). Different concentrations of ficin and P. badius extracts (1, 3, and 5%) were utilized to coagulate milk proteins. The ewes’ samples containing ficin and mushroom enzymes were heated from 25 to 45°C at a heating rate 1°C/min and kept for 30?min. Then, the curds were cooled down to 25°C with the same heating rate. The ficin extract could induce stronger gels at 45°C and 5% ficin. Similar results were also found for 5% P. badius extract and incubation at 45°C. However, P.badius gels achieved a network with more viscous characteristics and had a softer texture than ficin gels. Therefore, it may be concluded the induced gels with mushroom had higher moisture and lower protein contents, which related to the high proteolytic activity of P. badius . The microstructure survey showed that the mushroom‐induced gel had a more compact structure. By increasing enzyme concentration, both gels showed a coarser and more compact protein network. Whereas, the P. badius gels had more fusions and folds which indicate the greater proteolysis occurred during gelation and there was greater breakdown of protein. Our findings suggest the application of ficin and P. badius enzymes to develop a novel procedure to coagulate milk proteins and providing new structures in food systems.
机译：评价了通过凝集酶凝结而获得的母乳凝乳的流变学和微观结构特征，凝乳酶包括ficin提取物和猪Poly（Polyporus badius）。通过小振幅振荡剪切测量（SAOS）检查牛奶的凝胶化。利用不同浓度的丝氨酸​​和恶臭假单胞菌提取物（1、3和5％）来凝结乳蛋白。将含有藻蛋白和蘑菇酶的母羊样品以1℃/ min的加热速率从25℃加热至45℃，并保持30分钟。然后，以相同的加热速率将凝乳冷却至25℃。丝蛋白提取物可在45°C和5％丝蛋白诱导更强的凝胶。对于5％P. badius提取物和在45°C下孵育，也发现了相似的结果。然而，巴德毕氏菌凝胶获得的网络比黏蛋白凝胶具有更高的粘性，并且质地更柔软。因此，可以推断出蘑菇诱导的凝胶具有较高的水分和较低的蛋白质含量，这与P. badius的高蛋白水解活性有关。显微组织调查显示，蘑菇诱导的凝胶具有更致密的结构。通过增加酶的浓度，两种凝胶均显示出更粗糙，更紧密的蛋白质网络。而P. badius凝胶具有更多的融合和折叠，这表明在凝胶化过程中发生了更大的蛋白水解作用，并且蛋白质的分解也更大。我们的发现表明，ficin和恶性疟原虫酶的应用将开发一种新的程序来凝结牛奶蛋白，并在食品系统中提供新的结构。

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