The formation of inclusion bodies (IBs) without enzyme activity in bacterial research is generally undesirable. Researchers have attempted to recovery the enzyme activities of IBs, which are commonly known as active IBs. Tyrosine phenol-lyase (TPL) is an important enzyme that can convert pyruvate and phenol into 3,4-dihydroxyphenyl-l-alanine (L-DOPA) and IBs of TPL can commonly occur. To induce the correct folding and recover the enzyme activity of the IBs, peptides, such as ELK16, DKL6, L6KD, ELP10, ELP20, L6K2, EAK16, 18A, and GFIL16, were fused to the carboxyl terminus of TPL. The results showed that aggregate particles of TPL-DKL6, TPL-ELP10, TPL-EAK16, TPL-18A, and TPL-GFIL16 improved the enzyme activity by 40.9%, 50.7%, 48.9%, 86.6%, and 97.9%, respectively. The peptides TPL-DKL6, TPL-EAK16, TPL-18A, and TPL-GFIL16 displayed significantly improved thermostability compared with TPL. L-DOPA titer of TPL-ELP10, TPL-EAK16, TPL-18A, and TPL-GFIL16, with cells reaching 37.8 g/L, 53.8 g/L, 37.5 g/L, and 29.1 g/L, had an improvement of 111%, 201%, 109%, and 63%, respectively. A higher activity and L-DOPA titer of the TPL-EAK16 could be valuable for its industrial application to biosynthesize L-DOPA.

在细菌研究中，没有酶活性的包涵体 (IB) 的形成通常是不受欢迎的。研究人员试图恢复IBs的酶活性，这些IBs通常被称为活性IBs。酪氨酸酚裂解酶（TPL）是一种重要的酶，可将丙酮酸和苯酚转化为3,4-二羟基苯基-l-丙氨酸（L-DOPA），TPL的IBs常发生。为了诱导 IB 的正确折叠并恢复酶活性，将 ELK16、DKL6、L6KD、ELP10、ELP20、L6K2、EAK16、18A 和 GFIL16 等肽融合到 TPL 的羧基末端。结果表明，TPL-DKL6、TPL-ELP10、TPL-EAK16、TPL-18A和TPL-GFIL16的聚集颗粒分别提高了酶活性40.9%、50.7%、48.9%、86.6%和97.9%。与TPL相比，肽TPL-DKL6、TPL-EAK16、TPL-18A和TPL-GFIL16显示出显着改善的热稳定性。 TPL-ELP10、TPL-EAK16、TPL-18A和TPL-GFIL16的L-DOPA滴度提高，细胞分别达到37.8 g/L、53.8 g/L、37.5 g/L和29.1 g/L。分别为 111%、201%、109% 和 63%。 TPL-EAK16 的较高活性和 L-DOPA 效价对其生物合成 L-DOPA 的工业应用具有重要价值。