School of Life Science and Technology, Wuhan Polytechnic University, Wuhan 430023, China.
State Key Laboratory of Biocatalysis and Enzyme Engineering, College of Life Science, Hubei University, Wuhan 430062, China.
Int J Mol Sci. 2023 Jun 30;24(13):10901. doi: 10.3390/ijms241310901.
Laccases are widely used in industrial production due to their broad substrate availability and environmentally friendly nature. However, the pursuit of laccases with superior stability and increased heterogeneous expression to meet industry demands appears to be an ongoing challenge. To address this challenge, we resurrected five ancestral sequences of laccase BsCotA and their homologues. All five variants were successfully expressed in soluble and functional forms with improved expression levels in . Among the five variants, three exhibited higher catalytic rates, thermal stabilities, and acidic stabilities. Notably, AncCotA2, the best-performing variant, displayed a / of 7.5 × 10 M·s, 5.2-fold higher than that of the wild-type BsCotA, an improved thermo- and acidic stability, and better dye decolorization ability. This study provides a laccase variant with high application potential and presents a new starting point for future enzyme engineering.
漆酶由于其广泛的底物可用性和环境友好性，在工业生产中得到了广泛的应用。然而，为了满足工业需求，追求稳定性更高、异源表达增加的漆酶似乎是一个持续的挑战。为了解决这个挑战，我们复活了漆酶 BsCotA 的五个祖先序列及其同源物。所有五个变体都以可溶性和功能性形式成功表达，在 中的表达水平得到了提高。在这五个变体中，有三个表现出更高的催化速率、热稳定性和酸性稳定性。值得注意的是，表现最好的变体 AncCotA2 的 / 值为 7.5×10 M·s，比野生型 BsCotA 高 5.2 倍，热稳定性和酸性稳定性得到了提高，并且具有更好的染料脱色能力。本研究提供了一种具有高应用潜力的漆酶变体，并为未来的酶工程提供了一个新的起点。
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