Realm of Thermoalkaline Lipases in Bioprocess Commodities

Lajis, Ahmad Firdaus B.

doi:10.1155/2018/5659683

Cited by 14 publications

(12 citation statements)

References 104 publications

(288 reference statements)

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Section: Introductionmentioning

confidence: 99%

“…The use of lipases from thermophiles has been frequently reported [23,35,36]. Among them, the term "thermoalkaline (TA) lipases" describes some enzymes resistant not only to temperature (70-80 • C) but also to the presence of alkaline media (pH values between 8 and 10) [36]. These enzymes possess a peculiar feature in their 3D structure due to the presence of a relatively large lid domain (around 70 residues) formed by two alpha-helices (α6 and α7) [37], so that the opening of this lid domain upon exposing the active site requires a significant conformational change [38].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Biocatalysis at Extreme Temperatures: Enantioselective Synthesis of both Enantiomers of Mandelic Acid by Transesterification Catalyzed by a Thermophilic Lipase in Ionic Liquids at 120 °C

Ramos-Martín¹,

Khiari²,

Alcántara³

et al. 2020

Catalysts

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The use of biocatalysts in organic chemistry for catalyzing chemo-, regio- and stereoselective transformations has become an usual tool in the last years, both at lab and industrial scale. This is not only because of their exquisite precision, but also due to the inherent increase in the process sustainability. Nevertheless, most of the interesting industrial reactions involve water-insoluble substrates, so the use of (generally not green) organic solvents is generally required. Although lipases are capable of maintaining their catalytic precision working in those solvents, reactions are usually very slow and consequently not very appropriate for industrial purposes. Increasing reaction temperature would accelerate the reaction rate, but this should require the use of lipases from thermophiles, which tend to be more enantioselective at lower temperatures, as they are more rigid than those from mesophiles. Therefore, the ideal scenario would require a thermophilic lipase capable of retaining high enantioselectivity at high temperatures. In this paper, we describe the use of lipase from Geobacillus thermocatenolatus as catalyst in the ethanolysis of racemic 2-(butyryloxy)-2-phenylacetic to furnish both enantiomers of mandelic acid, an useful intermediate in the synthesis of many drugs and active products. The catalytic performance at high temperature in a conventional organic solvent (isooctane) and four imidazolium-based ionic liquids was assessed. The best results were obtained using 1-ethyl-3-methyl imidazolium tetrafluoroborate (EMIMBF4) and 1-ethyl-3-methyl imidazolium hexafluorophosphate (EMIMPF6) at temperatures as high as 120 °C, observing in both cases very fast and enantioselective kinetic resolutions, respectively leading exclusively to the (S) or to the (R)-enantiomer of mandelic acid, depending on the anion component of the ionic liquid.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Biocatalysis at Extreme Temperatures: Enantioselective Synthesis of both Enantiomers of Mandelic Acid by Transesterification Catalyzed by a Thermophilic Lipase in Ionic Liquids at 120 °C

Ramos-Martín¹,

Khiari²,

Alcántara³

et al. 2020

Catalysts

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“…Lipase is an enzyme with considerable commercial and industrial importance. Lipase (triacylglycerol acyl hydrolases (E.C.3.1.1.3) belongs to the class of hydrolases which catalyze the hydrolysis of triglycerides to glycerol and free fatty acids over an oil-water interface 3 . Lipases catalyze the reverse reactions in the synthesis of esters (triacylglycerols) consist of glycerol and fatty acids of long-chain in non-aqueous circumstances 4 .…”

Section: Introductionmentioning

confidence: 99%

Determination the Lipase Activity of Staphylococcus sp. Strain Isolated from Clinical Specimens

Alkabee¹,

Al-Salami²,

Ansari³

2020

J. Pure Appl. Microbiol.

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Bacterial lipases are the most important collection of biocatalysts used for a variety of biotechnological applications. In the current study the morphological, biochemical and Molecular characteristics to the extracellular lipase producing bacteria were identified. The bacterial isolates were selected as lipase producing bacteria using Rhodamine-B agar plate. the production of Lipase from the organism were determined with varying incubation temperature (20 to 50°C) and range of incubation time (16-120) hrs. 16 bacterial isolates were identified as Staphylococcus hemolyticus strain SHKS1 with Genbank acc. MK977614.1. By comparing the observed DNA sequences of these local samples with the retrieved DNA sequences (GenBank acc. MG595372.1) as showed high lipase activity according to experimental conditions about 140 U/ml. The current study showed that enzymatic activity of crude lipase extract was maximum in 72 hrs incubation period and 37°C.

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“…Lipases (EC 3.1.1.3) are lipolytic enzymes that are able to perform as a biocatalyst for hydrolysis reaction of triacylglycerol to glycerol and free fatty acid [1]. Not only hydrolysis reaction, but a wide range of chemical reactions could also be assisted by lipase, namely acidolysis, transesterification, esterification, and aminolysis, which make lipase vastly used in various fields of industry.…”

Section: ■ Introductionmentioning

confidence: 99%

Overexpression of Lipase Gene from <i>Alcaligenes</i> sp. JG3 and its Activity toward Hydrolysis Reaction

2019

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Bacterial lipase holds an important role as a new source for many industrial catalysts. The investigation and understanding of the lipase-encoding gene become apparent as the key step for generating high-quality lipase as biocatalyst for many chemical reactions. In this study, bacterial lipase from Alcaligenes sp. JG3 was produced via overexpression gene method. This specific lipase was successfully overexpressed using pQE-30 vector and E. coli M15[pREP4] as host, producing His-tagged protein sized 46 kDa and was able to hydrolyze triacylglycerol from olive oil with the calculated unit activity and specific activity of 0.012 U and 1.175 U/mg respectively. The in silico investigation towards lipase JG3 revealed that it was categorized as ABC transporter protein as opposed to the conventional hydrolase family. Lastly, amino acid sequences SGSGKTT from lipase JG3 was highly conserved sequences and was predicted as the ATP-binding site but the catalytic triad of serine, histidine, and aspartate has not been solved yet.

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Realm of Thermoalkaline Lipases in Bioprocess Commodities

Cited by 14 publications

References 104 publications

Biocatalysis at Extreme Temperatures: Enantioselective Synthesis of both Enantiomers of Mandelic Acid by Transesterification Catalyzed by a Thermophilic Lipase in Ionic Liquids at 120 °C

Biocatalysis at Extreme Temperatures: Enantioselective Synthesis of both Enantiomers of Mandelic Acid by Transesterification Catalyzed by a Thermophilic Lipase in Ionic Liquids at 120 °C

Determination the Lipase Activity of Staphylococcus sp. Strain Isolated from Clinical Specimens

Overexpression of Lipase Gene from <i>Alcaligenes</i> sp. JG3 and its Activity toward Hydrolysis Reaction

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