Zhu Wen-Yuan, Niu Kun, Liu Peng, Fan Yu-Hang, Liu Zhi-Qiang, Zheng Yu-Guo
The National and Local Joint Engineering Research Center for Biomanufacturing of Chiral Chemicals, Zhejiang University of Technology, Hangzhou, China.
Key Laboratory of Bioorganic Synthesis of Zhejiang, College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, China.
Front Chem. 2021 Apr 14;9:672414. doi: 10.3389/fchem.2021.672414. eCollection 2021.
L-methionine is an important natural amino acid with broad application prospects. A novel gene encoding the enzyme with the ability to catalyze O-succinyl-L-homoserine (OSH) to L-methionine was screened and characterized. The recombinant O-succinyl-L-homoserine sulfhydrylase from (OSHS) exhibited maximum activity at 35°C and pH 6.5. OSHS displayed an excellent thermostability with a half-life of 21.72 h at 30°C. Furthermore, the activity of OSHS increased 115% after Fe added. L-methionine was obtained with a total yield reaching 42.63 g/L under the concentration of O-succinyl-L-homoserine 400 mM (87.6 g/L). These results indicated that OSHS is a potential candidate for applying in the large-scale bioproduction of L-methionine.
L-甲硫氨酸是一种具有广阔应用前景的重要天然氨基酸。筛选并鉴定了一个编码能够催化O-琥珀酰-L-高丝氨酸（OSH）生成L-甲硫氨酸的酶的新基因。来自[具体来源未给出]的重组O-琥珀酰-L-高丝氨酸硫氢解酶（OSHS）在35°C和pH 6.5时表现出最大活性。OSHS具有出色的热稳定性，在30°C下半衰期为21.72小时。此外，添加铁后OSHS的活性提高了115%。在O-琥珀酰-L-高丝氨酸浓度为400 mM（87.6 g/L）的情况下，L-甲硫氨酸的总产量达到42.63 g/L。这些结果表明OSHS是大规模生物生产L-甲硫氨酸的潜在候选者。
