4.8 Article

Ordered Coimmobilization of a Multienzyme Cascade System with a Metal Organic Framework in a Membrane: Reduction of CO2 to Methanol

Journal

ACS APPLIED MATERIALS & INTERFACES
Volume 11, Issue 37, Pages 33581-33588

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acsami.9b09811

Keywords

multienzyme cascade system (MECS); enzyme immobilization; metal organic framework (MOF); enzyme membrane reactor; reduction CO2 to methanol

Funding

  1. National Natural Science Foundation of China [51473148]
  2. Public Technology Research Program of Zhejiang Province [LGG19E030009, NGF18B070005]
  3. Science Foundation of Zhejiang Sci-Tech University [15062095-Y]

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Enzymatic reduction of CO2 is of great significant, which involves an efficient multienzyme cascade system (MECS). In this work, formate dehydrogenase (FDH), glutamate dehydrogenase (GDH), and reduced pyridine nucleotide (NADH) (FDH&GDH&NADH), formaldehyde dehydrogenase (FalDH), GDH, and NADH (FalDH&GDH&NADH), and alcohol dehydrogenase (ADH), GDH, and NADH (ADH&GDH&NADH) were embedded in ZIF-8 (one kind of metal organic framework) to prepare three kinds of enzymes and coenzymes/ZIF-8 nanocomposites. Then by dead-end filtration these nanocomposites were sequentially located in a microporous membrane, which was combined with a pervaporation membrane to timely achieve the separation of product methanol. Incorporation of the pervaporation membrane was helpful to control reaction direction, and the methanol amount increased from 5.8 +/- 0.5 to 6.7 +/- 0.8 mu mol. The reaction efficiency of an immobilized enzymes-ordered distribution in a membrane was higher than that disordered distribution in the membrane, and the methanol amount increased from 6.7 +/- 0.8 to 12.6 +/- 0.6 mu mol. Moreover, it appeared that introduction of NADH into ZIF-8 enhanced the transformation of CO2 to methanol from 12.6 +/- 0.6 to 13.4 +/- 0.9 mu mol. Over 50% of their original productivity was retained after 12 h of use. This method has wide applicability and can be used in other kinds of multienzyme systems.

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