Transformation of low molecular compounds and soil humic acid by two domain laccase of Streptomyces puniceus in the presence of ferulic and caffeic acidsстатья

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Дата последнего поиска статьи во внешних источниках: 14 октября 2020 г.

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1. Trubitsina_et_al_Plos_One_2020.pdf Trubitsina_et_al_Plos_One_2020.pdf 1,6 МБ 1 октября 2020 [AZavarzina]
2. Notification_of_Formal_Acceptance_for_PONE.docx Notification_of_Formal_Acceptance_for_PONE.docx 13,8 КБ 7 сентября 2020 [AZavarzina]

[1] Transformation of low molecular compounds and soil humic acid by two domain laccase of streptomyces puniceus in the presence of ferulic and caffeic acids / L. I. Trubitsina, A. V. Lisov, O. V. Belova et al. // PLoS ONE. — 2020. — Vol. 15, no. 9. — P. e0239005. The two-domain bacterial laccases oxidize substrates at alkaline pH. The role of naturalphenolic compounds in the oxidation of substrates by the enzyme is poorly understood. Wehave studied the role of ferulic and caffeic acids in the transformation of low molecularweight substrates and of soil humic acid (HA) by two-domain laccase of Streptomyces puniceus(SpSL, previously undescribed). A gene encoding a two-domain laccase was clonedfrom S. puniceus and over-expressed in Escherichia coli. The recombinant protein was purifiedby affinity chromatography to an electrophoretically homogeneous state. The enzymeshowed high thermal stability, alkaline pH optimum for the oxidation of phenolic substratesand an acidic pH optimum for the oxidation of K4[Fe(CN)6] (potassium ferrocyanide) andABTS (2,20-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt). Phenoliccompounds were oxidized with lower efficiency than K4[Fe(CN)6] and ABTS. The SpSL didnot oxidize 3.4-dimethoxybenzoic alcohol and p-hydroxybenzoic acid neither in the absenceof phenolic acids nor in their presence. The enzyme polymerized HA—the amount of its highmolecular weight fraction (>80 kDa) increased at the expense of lowMWfraction (10 kDa).The addition of phenolic acids as potential mediators did not cause the destruction of HA bySpSL. In the absence of the HA, the enzyme polymerized caffeic and ferulic acids to macromolecularfractions (>80 kDa and 10–12 kDa). The interaction of SpSL with HA in the presenceof phenolic acids caused an increase in the amount of HA highMWfraction and a twofoldincrease in the molecular weight of its lowMW fraction (from 10 to 20 kDa), suggestinga cross-coupling reaction. Infrared and solution-state 1H-NMR spectroscopy revealed anincrease in the aromaticity of HA after its interaction with phenolic acids. The results of thestudy expand our knowledge on the transformation of natural substrates by two-domain bacteriallaccases and indicate a potentially important role of the enzyme in the formation of soilorganic matter (SOM) at alkaline pH values. [ DOI ]

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