Optimization of heat stabilizer of transglutaminase

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  • 1 (Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University, Wuxi 214122, China) 2(School of Biotechnology, Jiangnan University, Wuxi 214122, China)

Online published: 2018-02-02

Abstract

Transglutaminase (EC 2.3.2.13, TGase) can catalyze the cross-linking of protein molecules, and it has been widely used in the fields of food, biology, medicine, textile and so on. In order to improve the thermal stability, the effects of carbohydrates, salts and alcohols on the half-life of TGase at 55oC ((t1/2(55oC)) were studied. The results showed that the addition of sorbitol, wheat protein, NaCl and glucose could effectively prolong the half-life of TGase. On this basis, orthogonal experiments were carried out to obtain the best compound stabilizer: 50 g/L sorbitol, 50 g/L wheat protein, 50 g/L NaCl, and 50 g/L glucose. Under the protection of the compound stabilizer, thet1/2(55oC) value and the optimum reaction temperature of TGase were increased by 59.73-fold and 10oC respectively compared with the control (no stabilizer), and the residual enzyme activity rate after storage at room temperature (25oC) for 80 days was 73.84%, 62.79% higher than the control. The results of this study will facilitate the improvement of TGase production and application development.


Cite this article

REN Li-jun et al . Optimization of heat stabilizer of transglutaminase[J]. Food and Fermentation Industries, 2018 , 44(1) : 1 . DOI: 10.13995/j.cnki.11-1802/ts.015351

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