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Enzymatic Conversion of Carbon Dioxide to Methanol by Dehydrogenases Encapsulated in Sol-Gel Matrix

机译:脱氢酶包封溶胶 - 凝胶基质中二氧化碳的酶促转化二氧化碳

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The effective generation of methanol directly from gaseous carbon dioxide has received considerable attention in recent years since it can recycle the greenhouse gas and produce a clean fuel. Herein, we report an enzymatic approach for carbon dioxide fixation using formate dehydrogenase (F_(ate)DH), formaldehyde dehydrogenase (F_(ald)DH) and alcohol dehydrogenase (ADH) co-encapsulated in a silica gel as the catalysts. The gels were prepared by a modified sol-gel process that uses tetramethoxysilane (TMOS) as the precursor and nicotinamide adenine dinucleotide (NADH) as an electron donor. The enzymatic conversion of CO_2 to methanol was carried out at low temperatures and low pressures. The effects of the reaction temperature, pH value, the amount of enzyme and the amount of NADH on the yields of methanol have been investigated. The highest yield of methanol was 92.1%. The activity of immobilized enzymes was a little lower than that of the free enzymes due to the minor conformation change of the enzyme and the existence of additional diffusion hindrance.
机译:近年来,近年来它可以再循环温室气体并产生清洁燃料,有效地从气态二氧化碳直接从气态二氧化碳产生了相当大的关注。在此,我们报告了一种使用甲酸脱氢酶(F_(ATE)DH),甲醛脱氢酶(F_(ALD)DH)和醇脱氢酶(ADH)作为催化剂包封的甲醛脱氢酶(F_(ALD)DH)和醇脱氢酶(ADH)的酶法方法。通过改性的溶胶 - 凝胶工艺制备凝胶,其使用四甲氧基硅烷(TMO)作为前体和烟酰胺腺嘌呤二核苷酸(NADH)作为电子给体。在低温和低压力下进行CO_2至甲醇的酶促转化。研究了反应温度,pH值,酶的量和NADH对甲醇产率的影响。甲醇的最高产率为92.1%。由于酶的次要构象变化以及额外的扩散阻断,固定化酶的活性比游离酶的活性略低于游离酶的活性。

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