β-1,3-1,4-glucanase (BG) is an industrially important enzyme owing to its stringent specificity for β-glucan cleavage. In this study, poly-γ-glutamic acid (γ-PGA) was added to BG to investigate its effect on improving the activity and stability of the enzyme. The effect of γ-PGA was investigated by analyzing kinetic and thermodynamic parameters. Compared to control, significant differences (P < .05) in enzyme activity were observed when 1.0 %, 1.5 %, and 2.0 % γ-PGA was added, and the activities were increased 1.23 ± 0.05, 1.23 ± 0.07, and 1.31 ± 0.07-fold, respectively. Regarding thermostability, residual BG activity after a 1 h incubation at 60 °C was 12.53 ± 0.06 % without γ-PGA and 79.02 ± 5.76 % with 1% γ-PGA. The storage stability at 25 °C and 50 °C also increased when γ-PGA was present. The kinetics and thermodynamic investigations indicated that the increased activity and stability of BG when γ-PGA was added were due to increased values of the Vmax, Kcat, and activation energy for denaturation. The findings of this study suggest that adding γ-PGA to BG increases the application value of this enzyme in the food and feed industries.

中文翻译：

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芽孢杆菌产生的聚-γ-谷氨酸提高β-1,3-1,4-葡聚糖酶的酶活性、热稳定性和储存稳定性。SJ-10

β-1,3-1,4-葡聚糖酶 (BG) 是一种工业上重要的酶，因为它对 β-葡聚糖裂解具有严格的特异性。在本研究中，将聚-γ-谷氨酸 (γ-PGA) 添加到 BG 中以研究其对提高酶活性和稳定性的影响。通过分析动力学和热力学参数研究了γ-PGA的影响。与对照相比，添加 1.0 %、1.5 % 和 2.0 % γ-PGA 时，酶活性有显着差异（P < .05），活性分别增加 1.23 ± 0.05、1.23 ± 0.07 和 1.31 ± 0.07 -折叠，分别。关于热稳定性，在 60 °C 下孵育 1 小时后的残余 BG 活性为 12.53 ± 0.06 %，不含 γ-PGA，79.02 ± 5.76 %，含 1% γ-PGA。当存在 γ-PGA 时，25 °C 和 50 °C 的储存稳定性也增加。动力学和热力学研究表明，添加 γ-PGA 时 BG 的活性和稳定性增加是由于 Vmax、Kcat 和变性活化能的值增加。本研究的结果表明，在 BG 中添加 γ-PGA 增加了这种酶在食品和饲料行业的应用价值。