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构建用于生产D-甘露醇的高效大肠杆菌全细胞生物催化剂。

Construction of an efficient Escherichia coli whole-cell biocatalyst for D-mannitol production.

作者信息

Reshamwala Shamlan M S, Pagar Sandip K, Velhal Vishal S, Maranholakar Vijay M, Talangkar Vishal G, Lali Arvind M

机构信息

DBT-ICT-Centre for Energy Biosciences, Institute of Chemical Technology, Nathalal Parekh Marg, Matunga (East), Mumbai 400019, Maharashtra, India.

DBT-ICT-Centre for Energy Biosciences, Institute of Chemical Technology, Nathalal Parekh Marg, Matunga (East), Mumbai 400019, Maharashtra, India.

出版信息

J Biosci Bioeng. 2014 Dec;118(6):628-31. doi: 10.1016/j.jbiosc.2014.05.004. Epub 2014 Jun 5.

Abstract

Mannitol is a six carbon sugar alcohol that finds applications in the pharmaceutical and food industries. A novel Escherichia coli strain capable of converting D-glucose to D-mannitol has been constructed, wherein native mannitol-1-phosphate dehydrogenase (MtlD) and codon-optimized Eimeria tenella mannitol-1-phosphatase (M1Pase) have been overexpressed. Codon-optimized Pseudomonas stutzeri phosphite dehydrogenase (PtxD) was overexpressed for cofactor (NADH) regeneration with the concomitant oxidation of phosphite to phosphate. Whole-cell biotransformation using resting cells in a medium containing D-glucose and equimolar sodium phosphite resulted in d-mannitol yield of 87 mol%. Thus, production of an industrially relevant biochemical without using complex media components and elaborate process control mechanisms has been demonstrated.

摘要

甘露醇是一种六碳糖醇,在制药和食品工业中有应用。构建了一种能够将D-葡萄糖转化为D-甘露醇的新型大肠杆菌菌株,其中天然的甘露醇-1-磷酸脱氢酶(MtlD)和密码子优化的艾美耳球虫甘露醇-1-磷酸酶(M1Pase)已过表达。密码子优化的斯氏假单胞菌亚磷酸脱氢酶(PtxD)过表达用于辅因子(NADH)再生,同时亚磷酸氧化为磷酸盐。在含有D-葡萄糖和等摩尔亚磷酸钠的培养基中使用静息细胞进行全细胞生物转化,D-甘露醇产率为87摩尔%。因此,已证明在不使用复杂培养基成分和精细过程控制机制的情况下生产工业相关生化物质。

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