Transglutaminases (TGases) are enzymes that catalyze transfer of acyl group and covalent crosslinks formation between peptide-bound glutaminyl residues and amino groups. TGases have many industrial applications and have been purified from various sources. TGase was purified from the bovine liver extract by gel filtration on Sephacryl S-200 HR column. TGase activity was measured using CBZ-l-glutaminylglycine & hydroxylamine and the enzyme was characterized with respect to its response to different temperatures, pHs and salt concentrations. TGase was purified by yield 36.7%, had a weight 74 kDa, a high pH (pH = 8) and temperature (45 °C) optimum. The enzyme was observed to be stable at temperatures below 55 °C and was stable within a narrow pH range of 6.5–8.0. Purified TGase showed Ca2+ dependent characteristics and tended to retain activity at a high NaCl concentration. These results revealed that purified TGase can be used as a potential alternative to other sources.

中文翻译：

---

凝胶过滤法纯化牛肝转谷氨酰胺酶

转谷氨酰胺酶（TGase）是催化酰基转移和肽结合的谷氨酰胺残基与氨基之间共价交联形成的酶。TGase具有许多工业应用，并已从各种来源纯化。通过在Sephacryl S-200 HR柱上进行凝胶过滤，从牛肝提取物中纯化出TGase。使用CBZ-1-谷氨酰胺基甘氨酸和羟胺测量TGase活性，并就其对不同温度，pH和盐浓度的响应来表征该酶。TGase的提纯率为36.7％，重74 kDa，pH高（pH = 8），温度最佳（45°C）。观察到该酶在低于55°C的温度下稳定，并且在6.5–8.0的窄pH范围内稳定。纯化的TGase显示出Ca2 +依赖性特征，并倾向于在高NaCl浓度下保留活性。这些结果表明，纯化的TGase可以用作其他来源的潜在替代品。