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首页> 外文期刊>International Dairy Journal >Excessive cross-linking of caseins by microbial transglutaminase and its impact on physical properties of acidified milk gels
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Excessive cross-linking of caseins by microbial transglutaminase and its impact on physical properties of acidified milk gels

机译：酪蛋白通过微生物转谷氨酰胺酶的过度交联及其对酸化乳胶物理性质的影响

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摘要

By varying cross-linking intensity, the effect of microbial transglutaminase on acid gels made from casein solution and raw milk was studied. To avoid any impact of heating, N-ethylmaleimide was used for enzyme inactivation after appropriately checking its efficiency. Up to a specific degree of oligomerisation gel stiffness and firmness increased and tan t, time at gelation onset and syneresis decreased. Above approximately 70% and 25% of cross-linked protein in casein solution and raw milk, respectively, these parameters showed an opposite behaviour, and weak gels with high syneresis were obtained. Substrate differences, such as preferred cross-linking of adjoining -caseins on the surface of the micelle enhanced the effect of steric hindrance in raw milk and impaired proper rearrangements upon acidification at a much lower level of oligomerised protein. It is mainly dimeric and trimeric casein that successfully contributed to the enhanced properties of milk protein gels.
机译：通过改变交联强度，研究了微生物转谷氨酰胺酶对酪蛋白溶液和原料乳制成的酸性凝胶的影响。为了避免加热的影响，在适当检查其效率后，将N-乙基马来酰亚胺用于酶灭活。直至特定程度的低聚，凝胶的刚度和硬度增加，并且胶凝开始和脱水收缩的时间缩短。在酪蛋白溶液和生乳中分别超过约70％和25％的交联蛋白，这些参数表现出相反的行为，并且获得具有高脱水收缩性的弱凝胶。底物差异（例如，胶束表面上相邻的酪蛋白的优选交联）增强了原奶中空间位阻的作用，并且在低得多的低聚蛋白质水平下，酸化时损害了适当的重排。主要是二聚和三聚酪蛋白成功地促进了乳蛋白凝胶的增强性能。

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