微生物转谷氨酰胺酶催化酪蛋白酸钠聚合物的功能特性研究

Study on Functional Properties of Sodium Casemate Polymer Catalyzed by Microbial Transglutaminase

研究了微生物转谷氨酰胺酶(TGase)催化酪蛋白酸钠聚合对其功能特性的影响。结果显示,随着催化时间的增加,其各组份含量不断减少,同时生成的聚合物含量不断增加,比较了TGase催化不同酪蛋白的聚合速率,结果显示转谷氨酰胺酶较易催化α-和β-酪蛋白,而不易催化κ-酪蛋白TGase催化聚合酪蛋白酸钠能明显改善其乳化性能,聚合时间越长,乳化指数越高,而乳化稳定性随聚合时间先升后降,4h时最高TGase催化酪蛋白酸钠还可提高其热稳定性。

Effect on functional properties of sodium eascinate catalyzed In microbial transglutaminase (TGase) was studied. The results indicated that different casein components declined and its biopolymers increased with the reaction time. The rate of polymerization of different casein by TGase was compared. It indicated that α- and β-casein were more easily polymerized by TGase than k-casein. The polymerization of TGase could improve the emulsifying activity of sodium caseinate.The emulsifying activity index ( EAI) became high as the polymerization time went on. and the emulsifying stability increased at initial time and declined at more than 4h. The heat stability of sodium caseinate was also improved by TGase. The foaming properties of sodium caseinate was not affected by TGase.