Identification of the Gene Encoding Esterase, a Homolog of Hormone-Sensitive Lipase, from an Oil-Degrading Bacterium, Strain HD-1

Mizuguchi, Satoru; Amada, Kei; Haruki, Mitsuru; Imanaka, Tadayuki; Morikawa, Masaaki; Kanaya, Shigenori

doi:10.1093/oxfordjournals.jbchem.a022510

Cited by 7 publications

(5 citation statements)

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“…Since the discovery of the bHSL family, many bHSLs have been identified in a wide range of bacteria, such as Pseudomonas sp. B11-1 [27], Bacillus acidocaldarius [28], oildegrading bacterium strain HD-1 [29], Escherichia coli [30], Archaeoglobus fulgidus [31], Psychrobacter sp. Ant300 [32], Mycobacterium tuberculosis [33][34][35][42][43][44], Streptomyces coelicolor [36], Oenococcus oeni [37], Rhodococcus sp.…”

Section: Bacterial Hormone-sensitive Lipasesmentioning

confidence: 99%

Bacterial Hormone-Sensitive Lipases (bHSLs): Emerging Enzymes for Biotechnological Applications

Kim

2017

Journal of Microbiology and Biotechnology

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Lipases are important enzymes with biotechnological applications in dairy, detergent, food, fine chemicals, and pharmaceutical industries. Specifically, hormone-sensitive lipase (HSL) is an intracellular lipase that can be stimulated by several hormones, such as catecholamine, glucagon, and adrenocorticotropic hormone. Bacterial hormone-sensitive lipases (bHSLs), which are homologous to the C-terminal domain of HSL, have α/β-hydrolase fold with a catalytic triad composed of His, Asp, and Ser. These bHSLs could be used for a wide variety of industrial applications because of their high activity, broad substrate specificity, and remarkable stability. In this review, the relationships among HSLs, the microbiological origins, the crystal structures, and the biotechnological properties of bHSLs are summarized.

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Section: Bacterial Hormone-sensitive Lipasesmentioning

confidence: 99%

Bacterial Hormone-Sensitive Lipases (bHSLs): Emerging Enzymes for Biotechnological Applications

Kim

2017

Journal of Microbiology and Biotechnology

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“…The levels of amino acid sequence identity between EstZ and the other esterases/ lipases listed in Fig. 2 varied between 30 and 41% (7,8,33,42). The consensus motif for esterases, LAVVGDSVGG (10,17), is located between positions 159 and 168 of the translated EstZ sequence.…”

Section: Resultsmentioning

confidence: 99%

Decreasing the Level of Ethyl Acetate in Ethanolic Fermentation Broths ofEscherichia coliKO11 by Expression ofPseudomonas putida estZEsterase

Hasona

York

Yomano

et al. 2002

Appl Environ Microbiol

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During the fermentation of sugars to ethanol relatively high levels of an undesirable coproduct, ethyl acetate, are also produced. With ethanologenic Escherichia coli strain KO11 as the biocatalyst, the level of ethyl acetate in beer containing 4.8% ethanol was 192 mg liter ؊1 . Although the E. coli genome encodes several proteins with esterase activity, neither wild-type strains nor KO11 contained significant ethyl acetate esterase activity. A simple method was developed to rapidly screen bacterial colonies for the presence of esterases which hydrolyze ethyl acetate based on pH change. This method allowed identification of Pseudomonas putida NRRL B-18435 as a source of this activity and the cloning of a new esterase gene, estZ. Recombinant EstZ esterase was purified to near homogeneity and characterized. It belongs to family IV of lipolytic enzymes and contains the conserved catalytic triad of serine, aspartic acid, and histidine. As expected, this serine esterase was inhibited by phenylmethylsulfonyl fluoride and the histidine reagent diethylpyrocarbonate. The native and subunit molecular weights of the recombinant protein were 36,000, indicating that the enzyme exists as a monomer. By using ␣-naphthyl acetate as a model substrate, optimal activity was observed at pH 7.5 and 40°C. The K m and V max for ␣-naphthyl acetate were 18 M and 48.1 mol · min ؊1 · mg of protein ؊1 , respectively. Among the aliphatic esters tested, the highest activity was obtained with propyl acetate (96 mol · min ؊1 · mg of protein ؊1 ), followed by ethyl acetate (66 mol · min ؊1 · mg of protein ؊1 ). Expression of estZ in E. coli KO11 reduced the concentration of ethyl acetate in fermentation broth (4.8% ethanol) to less than 20 mg liter ؊1 .

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“…Compared with other HSL esterases, Ba EstB retains its activity in a wider alkaline pH range. Ba EstB optimal pH of 7.0 is lower than other esterases like that of an oil‐degrading bacterium (pH 8.5) (Mizuguchi et al., ), Pseudoalteromonas sp (pH 8) (Cieśliński et al., ) or Thermoanaerobacter tengcongensi (pH 9.5) (Rao et al., ), but higher than an esterase from the basidiomycete Pleurotus sapidus (pH 6) (Linke et al., ).…”

Section: Resultsmentioning

confidence: 99%

The first description of a hormone‐sensitive lipase from a basidiomycete: Structural insights and biochemical characterization revealed Bjerkandera adusta BaEstB as a novel esterase

et al. 2017

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The heterologous expression and characterization of a Hormone‐Sensitive Lipases (HSL) esterase (BaEstB) from the Basidiomycete fungus Bjerkandera adusta is reported for the first time. According to structural analysis, amino acid similarities and conservation of particular motifs, it was established that this enzyme belongs to the (HSL) family. The cDNA sequence consisted of 969 nucleotides, while the gene comprised 1133, including three introns of 57, 50, and 57 nucleotides. Through three‐dimensional modeling and phylogenetic analysis, we conclude that BaEstB is an ortholog of the previously described RmEstB‐HSL from the phylogenetically distant fungus Rhizomucor miehei. The purified BaEstB was characterized in terms of its specificity for the hydrolysis of different acyl substrates confirming its low lipolytic activity and a noticeable esterase activity. The biochemical characterization of BaEstB, the DLS analysis and the kinetic parameters determination revealed this enzyme as a true esterase, preferentially found in a dimeric state, displaying activity under alkaline conditions and relative low temperature (pH = 10, 20°C). Our data suggest that BaEstB is more active on substrates with short acyl chains and bulky aromatic moieties. Phylogenetic data allow us to suggest that a number of fungal hypothetical proteins could belong to the HSL family.

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Identification of the Gene Encoding Esterase, a Homolog of Hormone-Sensitive Lipase, from an Oil-Degrading Bacterium, Strain HD-1

Cited by 7 publications

References 0 publications

Bacterial Hormone-Sensitive Lipases (bHSLs): Emerging Enzymes for Biotechnological Applications

Bacterial Hormone-Sensitive Lipases (bHSLs): Emerging Enzymes for Biotechnological Applications

Decreasing the Level of Ethyl Acetate in Ethanolic Fermentation Broths ofEscherichia coliKO11 by Expression ofPseudomonas putida estZEsterase

The first description of a hormone‐sensitive lipase from a basidiomycete: Structural insights and biochemical characterization revealed Bjerkandera adusta BaEstB as a novel esterase

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