Enzymatic activity of catechol 1,2-dioxygenase and catechol 2,3-dioxygenase produced by Gordonia polyisoprenivorans

Silva, Andréa Scaramal da; Camargo, Flávio Anastácio de Oliveira; Andreazza, Robson; Jacques, Rodrigo Josemar Seminoti; Baldoni, Daiane Bortoluzzi; Bento, Fátima Menezes

doi:10.1590/s0100-40422012000800018

Cited by 48 publications

(26 citation statements)

References 29 publications

(38 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Another similarity that these enzymes share is the ferrous ion at the catalytic center [23]. But unlike most C23Os from other microorganisms [24][25][26], the C23O activity in this study was not enhanced with in the presence of Fe 3+ . This may indicate that the C23O from Thauera sp.…”

Section: Discussioncontrasting

confidence: 60%

Catechol 2,3‐dioxygenase from a new phenolic compound degrader Thauera sp. K11: purification and biochemical characterization

Liu

Wang

et al. 2018

J Basic Microbiol

View full text Add to dashboard Cite

Catechol 2,3-dioxygenase (C23O) from a new phenolic compound degrader Thauera sp. K11 was purified and characterized. The native form of the enzyme was determined as a homotetramer with a molecular weight of 140 kDa, and its isoelectric point was close to 6.4. One iron per enzyme subunit was detected using atom absorption spectroscopy, and the effective size of C23O in its dilute solution (0.2 g L , pH 8.0) was 14.5 nm. The optimal pH and temperature were 8.4 and 45 °C, respectively. The addition of Mg , Cu , Fe , and Mn could improve the enzyme activity, while Ag was found to be a strong inhibitor. C23O was stable in alkali conditions (pH 7.6-11.0) and thermostable below 50 °C. The final purified C23O had a sheet content of 53%, consistent with the theoretical value. This showed that the purified catechol 2,3-dioxygenase folded with a reasonable secondary structure.

show abstract

Section: Discussioncontrasting

confidence: 60%

Catechol 2,3‐dioxygenase from a new phenolic compound degrader Thauera sp. K11: purification and biochemical characterization

Liu

Wang

et al. 2018

J Basic Microbiol

View full text Add to dashboard Cite

show abstract

“…This enzyme catalyzes the initial degradation of PAHs to epoxide and to dihydrodiols by epoxide hydrolase. The dihydrodiols are further degraded to PAH catechols by dihydrodiols dehydrogenase . It has been advocated that the metabolism of the HMW PAHs often is initiated by fungal exoenzymes, thereby creating a diffusion gradient that facilitates further PAH biodegradation by other types of microorganisms, especially bacteria .…”

Section: Introductionmentioning

confidence: 99%

“…The dihydrodiols are further degraded to PAH catechols by dihydrodiols dehydrogenase. 19 It has been advocated that the metabolism of the HMW PAHs often is initiated by fungal exoenzymes, thereby creating a diffusion gradient that facilitates further PAH biodegradation by other types of microorganisms, especially bacteria. 9 Bacteria usually degrade LMW PAHs and a crucial phase in the aerobic bacterial metabolism of PAHs is the oxidation of the fused-benzene ring of the PAHs through the integration of molecular oxygen by the dioxygenase enzyme to form cis-dihydrodiols.…”

Section: Introductionmentioning

confidence: 99%

Potential microbial drivers of biodegradation of polycyclic aromatic hydrocarbons in crude oil sludge using a composting technique

Obi

Atagana

Adeleke

et al. 2020

J of Chemical Tech & Biotech

View full text Add to dashboard Cite

BACKGROUND Improper disposal of crude oil sludge poses a public health risk due to the toxic nature of components of the waste, especially polycyclic aromatic hydrocarbons (PAHs). Such toxic wastes can be treated by bioremediation of the polluted sites with composting, an eco‐friendly technique that is gaining acceptance. Crude oil sludge was composted for four months during which surfactants were introduced. Fungi and bacteria were isolated from the compost using basic culture techniques. Residual concentrations of PAH components of the sludge during the composting period was monitored with gas chromatography – mass spectrometry (GC‐MS). RESULTS Molecular characterization of the internal transcribed spacer (ITS) genes of fungal isolates classified fungi in the compost into different genera including Aspergillus, Bionectria, Doratomyces, Exophiala, Fusarium, Galactomyces, Geotrichum, Mucor, Penicillium, Trichoderma and Trichurus. The bacterial isolates were classified into Stenotrophomonas, Pseudomonas, Bordetella, Brucella, Bacillus, Achromobacter, Advenella, Klebsiella, Mesorhizobium, Mycobacterium, Ochrobactrum, Pusillimonas and Raoultella. Results from analysis of residual PAH concentrations of composted samples showed higher degradation efficiency of the higher molecular weight (HMW) PAHs resulting in their complete degradation, whereas the lower molecular weight PAHs were not degraded completely. CONCLUSIONS Compost bioremediation is a sustainable waste management technique for hazardous wastes such as crude oil sludge. Inclusion of surfactants at different concentrations did not constantly improve the bioavailability of PAH compounds in the crude oil sludge but it promoted fungal growth in the treatments. © 2020 Society of Chemical Industry

show abstract

“…This unique C12O exhibited remarkable thermostability, up to 65°C. Whilst C12O and C23O play a major role in (1) the breakdown of environmental contaminants, including aniline and its derivatives in agricultural soils [55] and (2) the degradation of biodiesel, diesel, chlorinated benzenes and some PAHs such as dibenzothiopene [56][57], the use of free enzymes are currently not a viable option since the enzymes are typically unstable under certain environmental conditions. Silva et al [57] isolated C12O and C23O from Gordonia polyisoprenivorans and tested both the cell-free extracts and immobilised extracts.…”

Section: Peroxidases (Ec 1111x)mentioning

confidence: 99%

Biotechnological Potential of Oxidative Enzymes from Actinobacteria

Roes‐Hill¹,

Prins²

2016

Actinobacteria - Basics and Biotechnological Applications

View full text Add to dashboard Cite

Oxidative enzymes are often considered for use in industrial processes because of the variety of reactions they are able to catalyse. In the past, most of these oxidative enzymes were obtained from fungi. However, in recent years, it has become evident that these enzymes are also produced by bacteria, including actinobacterial strains, which can therefore be considered as an underexploited resource of oxidative enzymes with potential for application in various industries. This chapter will focus on selected oxidative enzymes found in actinobacteria, their potential for application in industrial processes and how we can access and improve these enzymes to suit the required bioprocess conditions.

show abstract

Enzymatic activity of catechol 1,2-dioxygenase and catechol 2,3-dioxygenase produced by Gordonia polyisoprenivorans

Cited by 48 publications

References 29 publications

Catechol 2,3‐dioxygenase from a new phenolic compound degrader Thauera sp. K11: purification and biochemical characterization

Catechol 2,3‐dioxygenase from a new phenolic compound degrader Thauera sp. K11: purification and biochemical characterization

Potential microbial drivers of biodegradation of polycyclic aromatic hydrocarbons in crude oil sludge using a composting technique

Biotechnological Potential of Oxidative Enzymes from Actinobacteria

Contact Info

Product

Resources

About