Virgibacillus dokdonensis VITP14 produces α-amylase and protease with a broader operational range but with differential thermodynamic stability,Biotechnology and Applied Biochemistry

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Virgibacillus dokdonensis VITP14 produces α-amylase and protease with a broader operational range but with differential thermodynamic stability
Biotechnology and Applied Biochemistry ( IF 3.2 ) Pub Date : 2020-12-02 , DOI: 10.1002/bab.2084
Satabdi Mishra ₁ , Nidhya Nadarajan Joghee ₁ , Gurunathan Jayaraman ₁

Affiliation

Extracellular α-amylase and protease were coproduced from halo tolerant Virgibacillus dokdonensis VITP14 with banana peels (2% w/v) as substrate. The pH optima for α-amylase and protease were 6.5 and 7.0, respectively. The temperature optima of α-amylase and protease were 30 and 50 °C, respectively. Both the enzymes were active in the presence of various metal ions (1 mM of Ni²⁺, Ca²⁺, Ba²⁺, Sr²⁺, and Mg²⁺), detergents (Tween 20, Tween 80, Triton X-100), and other additives (2-mercaptoethanol and urea). Both the enzymes followed Michaelis–Menten type enzyme kinetics with V_max of 121.40 and 4.17 μmol Min⁻¹ mL⁻¹ and K_m of 0.59 and 0.28 mg mL⁻¹ for amylase and protease, respectively. Amylase showed higher activation energy for inactivation (75.55 kJ mol⁻¹ compared to 59.70 kJ mol⁻¹ for protease) and higher thermal stability (reflected by longer half-life 53.23 Min compared to 0.11 Min for protease) at 60 °C. The coexistence of amylase and protease could be attributed to the difference in the optimum temperatures of activity and thermal stability of the two enzymes.

中文翻译：

Virgibacillus dokdonensis VITP14 产生的 α-淀粉酶和蛋白酶具有更广泛的操作范围，但具有不同的热力学稳定性

以香蕉皮（2% w/v）为底物，由耐晕的 Virgibacillus dokdonensis VITP14共同产生细胞外 α-淀粉酶和蛋白酶。α-淀粉酶和蛋白酶的最适 pH 值分别为 6.5 和 7.0。α-淀粉酶和蛋白酶的最适温度分别为 30 和 50 °C。这两种酶在各种金属离子（1 mM Ni ²⁺、Ca ²⁺、Ba ²⁺、Sr ²⁺和 Mg ²⁺）、去污剂（Tween 20、Tween 80、Triton X-100 ) 和其他添加剂（2-巯基乙醇和尿素）。两种酶都遵循 Michaelis-Menten 型酶动力学，V _max为 121.40 和 4.17 μmol Min ^-1 mL^-1和K _m分别为 0.59 和 0.28 mg mL ^-1的淀粉酶和蛋白酶。淀粉酶在 60 °C 下显示出更高的失活活化能（75.55 kJ mol ^{-1与蛋白酶的 59.70 kJ mol}^-1相比）和更高的热稳定性（通过更长的半衰期 53.23 分钟与蛋白酶的 0.11 分钟反映）。淀粉酶和蛋白酶的共存可能是由于两种酶的最适活性温度和热稳定性不同所致。

更新日期：2020-12-02

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