Saccharomyces cerevisiae KNU5377 stress response during high-temperature ethanol fermentation
Saccharomyces cerevisiae KNU5377 stress response during high-temperature ethanol fermentation
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DOI：
10.1007/s10059-013-2258-0
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发表时间：
2013-03-01
影响因子：
3.8
通讯作者：
Yoon, Ho-Sung
中科院分区：
文献类型：
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作者：
Kim, Il-Sup;Kim, Young-Saeng;Yoon, Ho-Sung
生产燃料乙醇的成本比生产化石燃料高得多。有许多方法可以从生物质中生产具有成本效益的燃料乙醇。研究了耐高温酿酒酵母KNU5377在高温(40A℃)葡萄糖分批发酵过程中的应激反应。与酿酒酵母S288C(S288C)相比，酿酒酵母KNU5377(KNU5377)转录因子(HSF1、MSN2/4和YAP1)、代谢酶(己糖激酶、甘油醛-3-磷酸脱氢酶、葡萄糖-6-磷酸脱氢酶、异柠檬酸脱氢酶和酒精脱氢酶)、抗氧化酶(硫氧还蛋白3、硫氧还蛋白还原酶和孔蛋白)以及分子伴侣及其辅因子(Hsp104、Hsp82、Hsp60、Hsp42、Hsp30、Hsp26、Cpr1、Sti1和Zpr1)表达上调。3-磷酸甘油醛脱氢酶在KNU5377细胞中的表达显著增加。此外，细胞过氧化氢和蛋白质氧化，尤其是磷酸丙糖异构酶的脂质过氧化作用，KNU5377比S288C低。因此，KNU5377通过转录激活子激活各种细胞拯救蛋白，通过氧化还原稳态和蛋白质平衡来快速响应发酵压力，从而提高耐受性和增加酒精产量。
Fuel ethanol production is far more costly to produce than fossil fuels. There are a number of approaches to costeffective fuel ethanol production from biomass. We characterized stress response of thermotolerant Saccharomyces cerevisiae KNU5377 during glucose-based batch fermentation at high temperature (40A degrees C). S. cerevisiae KNU5377 (KNU5377) transcription factors (Hsf1, Msn2/4, and Yap1), metabolic enzymes (hexokinase, glyceraldehyde-3-phosphate dehydrogenase, glucose-6-phosphate dehydrogenase, isocitrate dehydrogenase, and alcohol dehydrogenase), antioxidant enzymes (thioredoxin 3, thioredoxin reductase, and porin), and molecular chaperones and its cofactors (Hsp104, Hsp82, Hsp60, Hsp42, Hsp30, Hsp26, Cpr1, Sti1, and Zpr1) are upregulated during fermentation, in comparison to S. cerevisiae S288C (S288C). Expression of glyceraldehyde-3-phosphate dehydrogenase increased significantly in KNU5377 cells. In addition, cellular hydroperoxide and protein oxidation, particularly lipid peroxidation of triosephosphate isomerase, was lower in KNU5377 than in S288C. Thus, KNU5377 activates various cell rescue proteins through transcription activators, improving tolerance and increasing alcohol yield by rapidly responding to fermentation stress through redox homeostasis and proteostasis.