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一种新型木质纤维素分解菌儿茶酚 2,3-双加氧酶表现出独特的底物偏好和金属需求。

A novel Bacillus ligniniphilus catechol 2,3-dioxygenase shows unique substrate preference and metal requirement.

机构信息

Bioprocessing and Biocatalysis Team, Aquatic and Crop Resource Development Research Centre, National Research Council Canada, 100 Sussex Drive, Ottawa, ON, K1A 0R6, Canada.

School of Environment and Safety Engineering, Jiangsu University, Zhenjiang, Jiangsu, China.

出版信息

Sci Rep. 2021 Dec 14;11(1):23982. doi: 10.1038/s41598-021-03144-8.

DOI:10.1038/s41598-021-03144-8
PMID:34907211
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8671467/
Abstract

Identification of novel enzymes from lignin degrading microorganisms will help to develop biotechnologies for biomass valorization and aromatic hydrocarbons degradation. Bacillus ligniniphilus L1 grows with alkaline lignin as the single carbon source and is a great candidate for ligninolytic enzyme identification. The first dioxygenase from strain L1 was heterologously expressed, purified, and characterized with an optimal temperature and pH of 32.5 °C and 7.4, respectively. It showed the highest activity with 3-ethylcatechol and significant activities with other substrates in the decreasing order of 3-ethylcatechol > 3-methylcatechol > 3-isopropyl catechol > 2, 3-dihydroxybiphenyl > 4-methylcatechol > catechol. It did not show activities against other tested substrates with similar structures. Most reported catechol 2,3-dioxygenases (C23Os) are Fe-dependent whereas Bacillus ligniniphilus catechol 2,3-dioxygenase (BLC23O) is more Mn- dependent. At 1 mM, Mn led to 230-fold activity increase and Fe led to 22-fold increase. Sequence comparison and phylogenetic analyses suggested that BL23O is different from other Mn-dependent enzymes and uniquely grouped with an uncharacterized vicinal oxygen chelate (VOC) family protein from Paenibacillus apiaries. Gel filtration analysis showed that BLC23O is a monomer under native condition. This is the first report of a C23O from Bacillus ligniniphilus L1 with unique substrate preference, metal-dependency, and monomeric structure.

摘要

鉴定木质素降解微生物中的新型酶将有助于开发生物转化技术，实现生物质增值和芳烃降解。Bacillus ligniniphilus L1 可以利用碱性木质素作为唯一碳源进行生长，是木质素氧化酶鉴定的理想候选菌株。该研究首次从 L1 菌株中异源表达、纯化并表征了一种具有最适温度和 pH 值分别为 32.5°C 和 7.4 的双加氧酶。该酶对 3-乙基儿茶酚的活性最高，对其他底物的活性依次为 3-乙基儿茶酚>3-甲基儿茶酚>3-异丙基儿茶酚>2,3-二羟基联苯>4-甲基儿茶酚>儿茶酚。该酶对具有相似结构的其他测试底物没有活性。大多数报道的儿茶酚 2,3-双加氧酶（C23Os）是 Fe 依赖性的，而 Bacillus ligniniphilus 儿茶酚 2,3-双加氧酶（BLC23O）则更依赖于 Mn。在 1mM 时，Mn 导致酶活增加了 230 倍，Fe 导致酶活增加了 22 倍。序列比较和系统发育分析表明，BL23O 与其他 Mn 依赖性酶不同，与 Paenibacillus apiaries 的一种未鉴定的邻氧螯合（VOC）家族蛋白独特地聚为一类。凝胶过滤分析表明，BLC23O 在天然状态下为单体。这是首次报道来自 Bacillus ligniniphilus L1 的 C23O 具有独特的底物偏好、金属依赖性和单体结构。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb0/8671467/d93dfcd95e3f/41598_2021_3144_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb0/8671467/d02d1982b3f2/41598_2021_3144_Fig1_HTML.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb0/8671467/0dff010f008f/41598_2021_3144_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb0/8671467/d93dfcd95e3f/41598_2021_3144_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb0/8671467/d02d1982b3f2/41598_2021_3144_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb0/8671467/dff5335503e0/41598_2021_3144_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb0/8671467/cdefac4972ba/41598_2021_3144_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb0/8671467/2a684f253e0d/41598_2021_3144_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb0/8671467/6cfb6b291761/41598_2021_3144_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb0/8671467/0f2b93e9cb20/41598_2021_3144_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb0/8671467/0dff010f008f/41598_2021_3144_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/bbb0/8671467/d93dfcd95e3f/41598_2021_3144_Fig8_HTML.jpg

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