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描述辅因子添加剂对“粗提物”生物电催化活性影响的数据。

Data describing the cofactor additives effect on bioelectrocatalytic activity of «crude» extracts.

作者信息

Dmitrieva M V, Zolotukhina E V

机构信息

Institute of Problems of Chemical Physics, Chernogolovka, Russia.

Moscow Institute of Physics and Technology, Dolgoprudny, Russia.

出版信息

Data Brief. 2020 Apr 22;30:105513. doi: 10.1016/j.dib.2020.105513. eCollection 2020 Jun.

DOI:10.1016/j.dib.2020.105513
PMID:32368583
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7186515/
Abstract

«Crude» extracts obtained via simple ultrasonic disintegration of microbial cell membrane are perspective bioelectrocatalysts. This extract contains all the necessary enzymes and cofactors required for oxidative or reductive conversion. The technology of synthesis of «crude extract» is simpler and less costly in comparison with technology of obtaining pure enzymes. Dialysis of the obtained extracts was performed with different molecular weight cut-off (3.5 kDa, 12-14 kDa, 25 kDa, 50 kDa). The obtained data show that after dialysis extracts lose their dehydrogenase and bioelectrocatalytic activity due to the loss of cofactors. However, the addition of NAD and NADP cofactors leads to a recovery of activity. The obtained data demonstrate that the concentration of the cofactor directly affects the rate of the bioelectrocatalytic reaction. Also, the obtained data indicate that the composition of the enzyme systems of the extract includes succinate dehydrogenase. Analyzing this data set can provide insight on increase of the electrocatalytic activity of a new type of bioelectrocatalyst.

摘要

通过简单的微生物细胞膜超声破碎获得的“粗”提取物是有前景的生物电催化剂。这种提取物包含氧化或还原转化所需的所有必需酶和辅因子。与获得纯酶的技术相比,“粗提取物”的合成技术更简单且成本更低。用不同截留分子量(3.5 kDa、12 - 14 kDa、25 kDa、50 kDa)对所得提取物进行透析。所得数据表明,透析后提取物由于辅因子的损失而失去其脱氢酶和生物电催化活性。然而,添加NAD和NADP辅因子会导致活性恢复。所得数据表明,辅因子的浓度直接影响生物电催化反应的速率。此外,所得数据表明提取物的酶系统组成包括琥珀酸脱氢酶。分析该数据集可为提高新型生物电催化剂的电催化活性提供见解。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a03d/7186515/a19d4e6dd167/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a03d/7186515/4a36e732d523/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a03d/7186515/5a9f88cb16fd/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a03d/7186515/4213a9060c73/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a03d/7186515/3a0cd32e92dc/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a03d/7186515/a19d4e6dd167/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a03d/7186515/4a36e732d523/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a03d/7186515/5a9f88cb16fd/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a03d/7186515/4213a9060c73/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a03d/7186515/3a0cd32e92dc/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a03d/7186515/a19d4e6dd167/gr5.jpg

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Chem Commun (Camb). 2016 Jan 21;52(6):1147-50. doi: 10.1039/c5cc09161f.
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Characterization of different FAD-dependent glucose dehydrogenases for possible use in glucose-based biosensors and biofuel cells.
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