Proteomic Analysis of Erythritol-Producing Yarrowia lipolytica from Glycerol in Response to Osmotic Pressure

雅罗维亚 渗透性休克 生物化学 赤藓糖醇 生物 渗透压 酵母 蛋白质组 基因
作者
Libo Yang,Xiao-Meng Dai,Zhiyong Zheng,Li Zhu,Xiaobei Zhan,Chi‐Chung Lin
出处
期刊:Journal of Microbiology and Biotechnology [Journal of Microbiology and Biotechnology]
卷期号:25 (7): 1056-1069 被引量:64
标识
DOI:10.4014/jmb.1412.12026
摘要

Osmotic pressure is a critical factor for erythritol production with osmophilic yeast.Protein expression patterns of an erythritol-producing yeast, Yarrowia lipolytica, were analyzed to identify differentially-expressed proteins in response to osmotic pressure.In order to analyze intracellular protein levels quantitatively, two-dimensional gel electrophoresis was performed to separate and visualize the differential expression of the intracellular proteins extracted from Y. lipolytica cultured under low (3.17 osmol/kg) and high (4.21osmol/kg) osmotic pressures.Proteomic analyses allowed identification of 54 differentially-expressed proteins among the proteins distributed in the range of pI 3-10 and 14.4-97.4kDa molecular mass between the osmotic stress conditions.Remarkably, the main proteins were involved in the pathway of energy, metabolism, cell rescue, and stress response.The expression of such enzymes related to protein and nucleotide biosynthesis was inhibited drastically, reflecting the growth arrest of Y. lipolytica under hyperosmotic stress.The improvement of erythritol production under high osmotic stress was due to the significant induction of a range of crucial enzymes related to polyols biosynthesis, such as transketolase and triosephosphate isomerase, and the osmotic stress responsive proteins like pyridoxine-4-dehydrogenase and the AKRs family.The polyols biosynthesis was really related to an osmotic response and a protection mechanism against hyperosmotic stress in Y. lipolytica.Additionally, the high osmotic stress could also induce other cell stress responses as with heat shock and oxidation stress responses, and these responsive proteins, such as the HSPs family, catalase T, and superoxide dismutase, also had drastically increased expression levels under hyperosmotic pressure.

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