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Rewiring Lactococcus lactis for Ethanol Production

机译:重新连接乳酸乳球菌以生产乙醇

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Lactic acid bacteria (LAB) are known for their high tolerance toward organic acids and alcohols (R. S. Gold, M. M. Meagher, R. Hutkins, and T. Conway, J. Ind. Microbiol. 10:45–54, 1992) and could potentially serve as platform organisms for production of these compounds. In this study, we attempted to redirect the metabolism of LAB model organism Lactococcus lactis toward ethanol production. Codon-optimized Zymomonas mobilis pyruvate decarboxylase (PDC) was introduced and expressed from synthetic promoters in different strain backgrounds. In the wild-type L. lactis strain MG1363 growing on glucose, only small amounts of ethanol were obtained after introducing PDC, probably due to a low native alcohol dehydrogenase activity. When the same strains were grown on maltose, ethanol was the major product and lesser amounts of lactate, formate, and acetate were formed. Inactivating the lactate dehydrogenase genes ldhX , ldhB , and ldh and introducing codon-optimized Z. mobilis alcohol dehydrogenase (ADHB) in addition to PDC resulted in high-yield ethanol formation when strains were grown on glucose, with only minor amounts of by-products formed. Finally, a strain with ethanol as the sole observed fermentation product was obtained by further inactivating the phosphotransacetylase (PTA) and the native alcohol dehydrogenase (ADHE).
机译:乳酸菌(LAB)以其对有机酸和醇类的高度耐受性而著称(RS Gold,MM Meagher,R。Hutkins和T. Conway,J。Ind。Microbiol。10:45-54,1992),并且可能用作生产这些化合物的平台生物。在这项研究中,我们试图将LAB模型生物乳酸乳球菌的代谢重新定向为乙醇生产。引入密码子优化的运动发酵单胞菌丙酮酸脱羧酶(PDC),并由合成启动子在不同菌株背景中表达。在生长于葡萄糖上的野生型乳酸乳球菌MG1363中,引入PDC后仅获得少量乙醇,这可能是由于天然乙醇脱氢酶活性低所致。当相同菌株在麦芽糖上生长时,乙醇是主要产物,形成的乳酸,甲酸和乙酸的量较少。当菌株在葡萄糖上生长时,灭活乳酸脱氢酶ldhX,ldhB和ldh并引入密码子优化的运动发酵单胞菌乙醇脱氢酶(ADHB)导致高产乙醇的形成,副产物很少形成。最后,通过进一步灭活磷酸转乙酰酶(PTA)和天然醇脱氢酶(ADHE),获得了以乙醇为唯一观察到的发酵产物的菌株。

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