In this study, the heterologous expression of an engineered thermostablle glucose oxidase from Aspergillus heteromophus CBS 117.55 was achieved in P. pastoris. This recombinant GoxAh was thermostable, with an optimal temperature range 25 °C-65 °C, and it was capable of retaining greater than 90% of its initial activity following a 10-min incubation at 75 °C. This enzyme had an optimum pH of 6.0, and it could retain above 80% of its initial activity following a 2-h incubation at a broad pH range (2.0–8.0). Moreover, GoxAh displayed excellent pepsin and trypsin resistance, and highly resistant to a range of tested metal ions and chemical reagents. These good properties make GoxAh a promising candidate for feed additive. The K_m and k_cat/K_m values of GoxAh were 187 mM and 1.09/mM/s, which limited its widespread application to some degree. However, due to its excellent characteristics, GoxAh is still of potential economic value for high value-added areas, as well as a good initial enzyme for developing applicable feed enzyme by protein engineering.

在这项研究中，在巴斯德毕赤酵母中获得了来自异曲霉CBS 117.55的工程热稳定葡萄糖氧化酶的异源表达。该重组GoxAh具有热稳定性，最适温度范围为25°C至65°C，在75°C孵育10分钟后，它能够保留超过其初始活性的90％。该酶的最适pH为6.0，在较宽的pH范围（2.0–8.0）下孵育2小时后，可以保留其初始活性的80％以上。此外，GoxAh表现出出色的胃蛋白酶和胰蛋白酶抵抗力，并且对一系列经测试的金属离子和化学试剂具有高度抵抗力。这些良好的特性使GoxAh成为饲料添加剂的有前途的候选者。K _m和k_猫GoxAh的/ K _m值为187 mM和1.09 / mM / s，这在一定程度上限制了它的广泛应用。然而，由于其优异的特性，GoxAh对于高附加值领域仍然具有潜在的经济价值，并且是通过蛋白质工程开发适用的饲料酶的良好初始酶。