首页> 外文期刊>Journal of Agricultural and Food Chemistry >Effect of transglutaminase-catalyzed polymerization of beta-casein on its emulsifying properties.
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Effect of transglutaminase-catalyzed polymerization of beta-casein on its emulsifying properties.

机译:转谷氨酰胺酶催化的β-酪蛋白聚合对其乳化性能的影响。

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beta-Casein was polymerized to various extents by the transglutaminase-catalyzed cross-linking reaction. Under the reaction conditions used, dimer, trimer, and tetramer of beta-casein were produced as predominant species at short reaction times (20-90 min) and large polymers at longer reaction times (3-24 h). Examination of the emulsifying properties of these cross-linked beta-casein polymers showed that although the emulsifying activity index decreased, the storage stability of the emulsions increased with increasing degree of polymerization. Experiments with mixtures of native and polymerized beta-casein also showed that increasing the fraction of polymerized beta-casein in the mixture increased the emulsion stability. This enhancement of emulsion stability might be due either to an enhancement in steric stabilization, attributable to the branched nature of the trasgutaminase-catalyzed polymers, or to stronger cohesive interactions between polymerized beta-casein molecules than between monomeric beta-casein molecules in the film.
机译:β-酪蛋白通过转谷氨酰胺酶催化的交联反应聚合到不同程度。在所使用的反应条件下,β-酪蛋白的二聚体,三聚体和四聚体在较短的反应时间(20-90分钟)以大分子形式生成,而较大的聚合物在较长的反应时间(3-24小时)以大分子形式生成。对这些交联的β-酪蛋白聚合物的乳化性能的研究表明,尽管乳化活性指数降低,但是乳液的储存稳定性随着聚合度的增加而增加。用天然和聚合的β-酪蛋白的混合物进行的实验还表明,增加混合物中聚合的β-酪蛋白的分数会增加乳液的稳定性。乳液稳定性的这种提高可能是由于空间蛋白稳定化的增强,这归因于反铁蛋白酶催化的聚合物的支化性质,或者是由于聚合的β-酪蛋白分子之间比单体β-酪蛋白分子之间更强的内聚相互作用。

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