Identification and characterization of a novel esterase from <i>Thauera</i> sp.

Yu, Ning; Yang, J; Guo, Yin; Li, Rongsheng; Zou, Weixin; He, Chang

doi:10.1002/bab.1659

Cited by 10 publications

(6 citation statements)

References 39 publications

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“…Among them, the relative abundance of Thauera was 8.91% in the SBR, which was much higher than that of the source sludge (1.25%). Thauera plays an important role in the removal of pollutants including ammonium-nitrogen, organic matter, and aromatic compounds [45]. This genus was also shown to be a quinoline-degrading taxon in CWW [46].…”

Section: Microbial Composition Of the Source And Acclimated Sludgementioning

confidence: 98%

Glucose Addition Enhanced the Advanced Treatment of Coking Wastewater

Xia

et al. 2021

Water

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Biological processes have high removal efficiencies and low operational costs, but the secondary effluent of coking wastewater (CWW), even at a low concentration, is difficult for microorganisms to degrade directly. In this study, glucose was used as a carbon source and co-metabolic substrate for microbial acclimation in order to enhance the advanced treatment of coking wastewater (CWW). The removal performance of the pollutants, especially recalcitrant compounds, was studied and the changes in the microbial community structure after activated sludge acclimation were analyzed. The effect of glucose addition on the secondary biochemical effluent of coking wastewater (SBECW) treatment by the acclimated sludge was further studied by a comparison between the performance of two parallel reactors seeded with the acclimated sludge. Our results showed that the concentrations of chemical oxygen demand (COD), total organic carbon (TOC), and UV absorption at 254 nm (UV254) of the wastewater decreased in the acclimation process. Refractory organic matter, such as polycyclic aromatic hydrocarbons and nitrogen-containing heterocyclics, in the SBECW was effectively degraded by the acclimated sludge. High-throughput sequencing revealed that microbes with a strong ability to degrade recalcitrant compounds were enriched after acclimation, such as Thauera (8.91%), Pseudomonas (3.35%), and Blastocatella (10.76%). Seeded with the acclimated sludge, the reactor with the glucose addition showed higher COD removal efficiencies than the control system without glucose addition (p < 0.05). Collectively, glucose addition enhanced the advanced treatment of coking wastewater (CWW).

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Section: Microbial Composition Of the Source And Acclimated Sludgementioning

confidence: 98%

Glucose Addition Enhanced the Advanced Treatment of Coking Wastewater

Xia

et al. 2021

Water

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“…This optimum pH is similar to other SGNH family esterases, such as an esterase gene (Tlip) from Thauera sp. [14] or an SGNH hydrolase (LI22) from Listeria innocua [19]. Furthermore, other esterases from L. acidophilus showed the optimum pH of 7.0-8.0 such as a cinnamoyl esterase [30] or LaAcE [31].…”

Section: Characterizations Of Lasgnh1mentioning

confidence: 99%

“…The Asp-x-x-His tetrapeptide in motif V constitutes the catalytic machinery of these enzymes. To date, a number of SGNH family esterases have been identified and characterized from several microorganisms [11][12][13][14][15][16][17][18][19], but there are very few reports in lactic acid bacteria.…”

Section: Introductionmentioning

confidence: 99%

Characterization and Immobilization of a Novel SGNH Family Esterase (LaSGNH1) from Lactobacillus acidophilus NCFM

Yoo

Jeon

et al. 2019

IJMS

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The SGNH family esterases are highly effective biocatalysts due to their strong catalytic efficiencies, great stabilities, relatively small sizes, and ease of immobilization. Here, a novel SGNH family esterase (LaSGNH1) from Lactobacillus acidophilus NCFM, which has homologues in many Lactobacillus species, was identified, characterized, and immobilized. LaSGNH1 is highly active towards acetate-or butyrate-containing compounds, such as p-nitrophenyl acetate or 1-naphthyl acetate. Enzymatic properties of LaSGNH1, including thermal stability, optimum pH, chemical stability, and urea stability, were investigated. Interestingly, LaSGNH1 displayed a wide range of substrate specificity that included glyceryl tributyrate, tert-butyl acetate, and glucose pentaacetate. Furthermore, immobilization of LaSGNH1 by crosslinked enzyme aggregates (CLEAs) showed enhanced thermal stability and efficient recycling property. In summary, this work paves the way for molecular understandings and industrial applications of a novel SGNH family esterase (LaSGNH1) from Lactobacillus acidophilus.

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“…Lipolytic enzymes are widely distributed in nature (i.e., animals, plants, and microorganisms), and a relatively large number has been isolated from metagenomes and bacteria [ 1 , 2 , 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 ]. The latter includes enzymes with different biological activities isolated from genera such as Pseudomonas [ 1 ], Psychrobacter [ 5 ], Salinisphaera [ 9 ], Serratia [ 11 ], Burkholderia [ 12 ], and Staphylococcus [ 13 ].…”

Section: Introductionmentioning

confidence: 99%

Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15

et al. 2021

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Esterases represent an important class of enzymes with a wide variety of industrial applications. A novel hormone-sensitive lipase (HSL) family esterase, Est19, from the Antarctic bacterium Pseudomonas sp. E2-15 is identified, cloned, and expressed. The enzyme possesses a GESAG motif containing an active serine (S) located within a highly conserved catalytic triad of Ser155, Asp253, and His282 residues. The catalytic efficiency (kcat/Km) of Est19 for the pNPC6 substrate is 148.68 s−1mM−1 at 40 °C. Replacing Glu154 juxtaposed to the critical catalytic serine with Asp (E154→D substitution) reduced the activity and catalytic efficiency of the enzyme two-fold, with little change in the substrate affinity. The wild-type enzyme retained near complete activity over a temperature range of 10–60 °C, while ~50% of its activity was retained at 0 °C. A phylogenetic analysis suggested that Est19 and its homologs may represent a new subfamily of HSL. The thermal stability and stereo-specificity suggest that the Est19 esterase may be useful for cold and chiral catalyses.

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Identification and characterization of a novel esterase from Thauera sp.

Cited by 10 publications

References 39 publications

Glucose Addition Enhanced the Advanced Treatment of Coking Wastewater

Glucose Addition Enhanced the Advanced Treatment of Coking Wastewater

Characterization and Immobilization of a Novel SGNH Family Esterase (LaSGNH1) from Lactobacillus acidophilus NCFM

Identification and Biochemical Characterization of a Novel Hormone-Sensitive Lipase Family Esterase Est19 from the Antarctic Bacterium Pseudomonas sp. E2-15

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