Improvement of glutathione production by a metabolically engineered Yarrowia lipolytica strain using a small-scale optimization approach

Diem, Tran Hong; Fickers, Patrick; Tahar, Imen Ben

doi:10.1007/s10529-020-03039-0

Cited by 2 publications

(1 citation statement)

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“…[24] While the reaction achieved a conversion yield of 0.8, it requires a pure GSH solution, as well as the production, purification, and immobilization of recombinant NsPCS, which can be cumbersome and time-consuming. We previously reported on the engineering of the yeast Yarrowia lipolytica for efficient GSH production, [27,28] achieving GSH titers and productivity rates among the highest reported in the literature. Therefore, we employed this yeast as a chassis strain for γ-GC production.…”

Section: Introductionmentioning

confidence: 99%

Biosynthesis of the antioxidant γ‐glutamyl‐cysteine with engineered Yarrowia lipolytica

Do,

Guruk,

Kus‐Liśkiewicz

et al. 2024

Biotechnology Journal

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The dipeptide γ‐glutamylcysteine (γ‐GC), the first intermediate of glutathione (GSH) synthesis, is considered as a promising drug to reduce or prevent plethora of age‐related disorders such as Alzheimer and Parkinson diseases. The unusual γ‐linkage between the two constitutive amino acids, namely cysteine and glutamate, renders its chemical synthesis particularly challenging. Herein, we report on the metabolic engineering of the non‐conventional yeast Yarrowia lipolytica for efficient γ‐GC synthesis. The yeast was first converted into a γ‐GC producer by disruption of gene GSH2 encoding GSH synthase and by constitutive expression of GSH1 encoding glutamylcysteine ligase. Subsequently genes involved in cysteine and glutamate anabolism, namely MET4, CYSE, CYSF, and GDH1 were overexpressed with the aim to increase their intracellular availability. With such a strategy, a γ‐GC titer of 464 nmol mg−1 protein (93 mg gDCW−1) was obtained within 24 h of cell growth.

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Section: Introductionmentioning

confidence: 99%