Substrate specificity and effects of water-miscible solvents on the activity and stability of extracellular lipase from Streptomyces rimosus

Leščić, Ivana; Vukelić, Bojana; Majerić-Elenkov, Maja; Saenger, Wolfram; Abramić, Marija

doi:10.1016/s0141-0229(01)00433-1

Cited by 37 publications

(16 citation statements)

References 21 publications

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“…LP28, in this regard, is related to non-specific lipase group. Similar results were observed in Streptomyces rimosus lipase [25] and psychrotrophic lipase from Pseudomonas sp. Strain KB700A [22].…”

Section: Effect Of Methanol and Various Effectorssupporting

confidence: 86%

A novel cold-adapted lipase, LP28, from a mesophilic Streptomyces strain

Simkhada

Yoo²,

Cho

et al. 2011

Bioprocess Biosyst Eng

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Fossil fuel is limited but its usage has been growing rapidly, thus the fuel is predicted to be completely running out and causing an unbearable global energy crisis in the near future. To solve this potential crisis, incorporating with increasing environmental concerns, significant attentions have been given to biofuel production in the recent years. With the aim of isolating a microbial biocatalyst with potential application in the field of biofuel, a lipase from Streptomyces sp. CS628, LP28, was purified using hydroxyapatite column chromatography followed by a gel filtration. Molecular weight of LP28 was estimated to be 32,400 Da by SDS-PAGE. The activity was the highest at 30 °C and pH 8.0 and was stable at pH 6.0-8.0 and below 25 °C. The enzyme preferentially hydrolyzed p-nitrophenyl decanoate (C10), a medium chain substrate. Furthermore, LP28 non-specifically hydrolyzed triolein releasing both 1,2- and 1,3-diolein. More importantly, LP28 manifestly catalyzed biodiesel production using palm oil and methanol; therefore, it can be a potential candidate in the field of biofuel.

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Section: Effect Of Methanol and Various Effectorssupporting

confidence: 86%

A novel cold-adapted lipase, LP28, from a mesophilic Streptomyces strain

Simkhada

Yoo²,

Cho

et al. 2011

Bioprocess Biosyst Eng

View full text Add to dashboard Cite

show abstract

“…Organic solvents such as acetone, EDTA, ethanol, isopropanol, PMSF and SDS [49] are reported to inhibit triacylglycerol lipases [62,63]. Under lab conditions, Triton X-100, Tween-20, Tween-40, Tween-80 [64], 1,4-dioxane, acetone, dimethyl sulfoxide, ethanol and tetrahydrofuran [65] are reported activators to carboxyl esterases. Interestingly, acetone, Brij 52, cholic acid, deoxycholic acid, isopropanol, Dimethyl sulfoxide (DMSO), lithocholic acid, rhamnolipid and sodium deoxycholate are also reported as activators for triacylglycerol lipases [66].…”

Section: Lipasementioning

confidence: 99%

Enzyme Dynamic in Plant Nutrition Uptake and Plant Nutrition

Turan¹,

Nikerel²,

Kaya³

et al. 2017

Enzyme Inhibitors and Activators

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Soil contains enzymes, constantly interacting with soil constituents, e.g. minerals, rhizosphere and numerous nutrients. Enzymes, in turn, catalyse important biochemical reactions for rhizobacteria and plants, stabilize the soil by degrading wastes and mediate nutrient recycling.The available enzymes inside soil could originate from plants, animals or microbes. The enzymes that are produced from these organism could exhibit intracellular activities, at the cell membrane, interacting therefore with soil and its constituents, or extracellularly (so freely available). Therefore, vis-à-vis to plant nutrition, the (extra or sub) cellular localization has a key role. Typical major enzymes available in soil can be listed as dehydrogenases, hydrogenases, oxidases, catalases, peroxidases, phenol o-hydroxylase, dextransucrase, aminotransferase, rhodanese, carboxylesterase, lipase, phosphatase, nuclease, phytase, arylsulphatase, amylase, cellulase, inulase, xylanase, dextranase, levanase, poly-galacturonase, glucosidase, galactosidase, invertase, peptidase, asparaginase, glutaminase, amidase, urease, aspartate decarboxylase, glutamate decarboxylase and aromatic amino acid decarboxylase. An interesting strategy for improving the nutritional quality of the soil would be to inoculate microorganism to soil while giving attention to mineral or other compounds that affect enzyme activity in soil. Since, some elements or compounds could show both activation and inhibitory effect, such as Fe, Na, etc. metals, the regulation of their bioavailability is crucial.

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“…14 -23 The extracellular lipase from Streptomyces rimosus R6-554W investigated in this study was first isolated and biochemically characterized by Abramić et al 19 The substrate specificity, regioselectivity and transesterification activity of this lipase and also its stability were further investigated. 20 In order to explore biotechnological applications and to characterize the structure on the protein level, large quantities of enzyme are required. Therefore, cloning, sequencing and high-level expression of S. rimosus lipase gene was carried out, 21 and the derived nucleotide sequence was analyzed by bioinformatic approaches.…”

Section: Introductionmentioning

confidence: 99%

“…19,20 The enzyme hydrolyzes primary and secondary ester bonds in triacylglycerols, with a preference for medium chain length fatty acids (C 8 -C 12 ), and also it catalyzes the hydrolysis of poly(oxyethylene)sorbitan monoesters (Tween 20-80) with a rate comparable to that for triacylglycerols. Its highest activity was detected in alkaline solution (pH 9-10) at 50-60°C.…”

Section: Introductionmentioning

confidence: 99%

“…The observed pronounced thermal stability, which is comparable to that of lipases from thermophilic microorganisms, the preservation of its activity in a broad pH range and the ruggedness towards various agents and water-miscible organic solvents recommend the newly isolated extracellular lipase from S. rimosus as a biocatalyst for industrial applications. 19,20 Costeffective biotechnological production of this enzyme should be facilitated by its secretion to the extracellular medium, its high stability and its homogeneity, i.e. the absence of isoenzymes and post-translational modifications.…”

Section: Introductionmentioning

confidence: 99%

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Characterization of covalently inhibited extracellular lipase from Streptomyces rimosus by matrix‐assisted laser desorption/ionization time‐of‐flight and matrix‐assisted laser desorption/ionization quadrupole ion trap reflectron time‐of‐flight mass spectrometry: localization of the active site serine

et al. 2004

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A chemical modification approach combined with matrix-assisted laser desorption/ionization (MALDI) mass spectrometry was used to identify the active site serine residue of an extracellular lipase from Streptomyces rimosus R6-554W. The lipase, purified from a high-level overexpressing strain, was covalently modified by incubation with 3,4-dichloroisocoumarin, a general mechanism-based serine protease inhibitor. MALDI time-of-flight (TOF) mass spectrometry was used to probe the nature of the intact inhibitor-modified lipase and to clarify the mechanism of lipase inhibition by 3,4-dichloroisocoumarin. The stoichiometry of the inhibition reaction revealed that specifically one molecule of inhibitor was bound to the lipase. The MALDI matrix 2,6-dihydroxyacetophenone facilitated the formation of highly abundant [M + 2H](2+) ions with good resolution compared to other matrices in a linear TOF instrument. This allowed the detection of two different inhibitor-modified lipase species. Exact localization of the modified amino acid residue was accomplished by tryptic digestion followed by low-energy collision-induced dissociation peptide sequencing of the detected 2-(carboxychloromethyl)benzoylated peptide by means of a MALDI quadrupole ion trap reflectron TOF instrument. The high sequence coverage obtained by this approach allowed the confirmation of the site specificity of the inhibition reaction and the unambiguous identification of the serine at position 10 as the nucleophilic amino acid residue in the active site of the enzyme. This result is in agreement with the previously obtained data from multiple sequence alignment of S. rimosus lipase with different esterases, which indicated that this enzyme exhibits a characteristic Gly-Asp-Ser-(Leu) motif located close to the N-terminus and is harboring the catalytically active serine residue. Therefore, this study experimentally proves the classification of the S. rimosus lipase as GDS(L) lipolytic enzyme.

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Substrate specificity and effects of water-miscible solvents on the activity and stability of extracellular lipase from Streptomyces rimosus

Cited by 37 publications

References 21 publications

A novel cold-adapted lipase, LP28, from a mesophilic Streptomyces strain

A novel cold-adapted lipase, LP28, from a mesophilic Streptomyces strain

Enzyme Dynamic in Plant Nutrition Uptake and Plant Nutrition

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