Higher tolerance of a novel lipase from Aspergillus flavus to the presence of free fatty acids at lipid/water interface

Laachari, Faouzi; Bergad, Fatimazahra El; Sadiki, Moulay; Sayari, Adel; Bahafid, Wifak; Abed, Soumya El; Iraqui, Mohammed; Koraichi, Saâd Ibnsouda

doi:10.5897/ajbr2014.0804

Cited by 8 publications

(2 citation statements)

References 18 publications

(22 reference statements)

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“…Although the molecular weights of microbial lipases can vary from 20 to 60 kDa, they are all members of the α/β-hydrolase fold protein family ( Nardini and Dijkstra, 1999 ; Singh and Mukhopadhyay, 2012 ). Hydrolases are a class of enzymes whose activity depends on the catalytic triad that includes Ser, His and Asp ( Farrokh et al, 2014 ; Faouzi et al, 2015 ). In the α/β hydrolases, these three amino acid residues are detected in order as Ser-Asp-His; the Ser residues are all located in a conserved catalytic Gly-X-Ser-X-Gly sequence.…”

Section: The Structure and Catalytic Mechanism Of Microbial Lipasesmentioning

confidence: 99%

A Valuable Product of Microbial Cell Factories: Microbial Lipase

Yao

Liu

et al. 2021

Front. Microbiol.

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As a powerful factory, microbial cells produce a variety of enzymes, such as lipase. Lipase has a wide range of actions and participates in multiple reactions, and they can catalyze the hydrolysis of triacylglycerol into its component free fatty acids and glycerol backbone. Lipase exists widely in nature, most prominently in plants, animals and microorganisms, among which microorganisms are the most important source of lipase. Microbial lipases have been adapted for numerous industrial applications due to their substrate specificity, heterogeneous patterns of expression and versatility (i.e., capacity to catalyze reactions at the extremes of pH and temperature as well as in the presence of metal ions and organic solvents). Now they have been introduced into applications involving the production and processing of food, pharmaceutics, paper making, detergents, biodiesel fuels, and so on. In this mini-review, we will focus on the most up-to-date research on microbial lipases and their commercial and industrial applications. We will also discuss and predict future applications of these important technologies.

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Section: The Structure and Catalytic Mechanism Of Microbial Lipasesmentioning

confidence: 99%

A Valuable Product of Microbial Cell Factories: Microbial Lipase

Yao

Liu

et al. 2021

Front. Microbiol.

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“…It was reported that bacterial esterases could adopt monomers or oligomers with molecular weights in the range of 25–85 kDa [ 19 ]. As they belong to the class of α/β-hydrolases, their active sites generally consist of highly conserved catalytic triad such as a nucleophilic residue (Ser, Cys, or Asp), a catalytic acidic residue (Glu or Asp), and a proton carrier His [ 20 , 21 ] in close spatial proximity. Thus, a short consensus sequence, GXSXG pentapeptide, in which X stands for various amino acids, commonly exists in esterases [ 11 , 22 , 23 ].…”

Section: Introductionmentioning

confidence: 99%

Enzymatic Characterization of a Novel HSL Family IV Esterase EstD04 from Pseudomonas sp. D01 in Mealworm Gut Microbiota

et al. 2023

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Pseudomonas sp. D01, capable of growing in tributyrin medium, was isolated from the gut microbiota of yellow mealworm. By using in silico analyses, we discovered a hypothesized esterase encoding gene in the D01 bacterium, and its encoded protein, EstD04, was classified as a bacterial hormone-sensitive lipase (bHSL) of the type IV lipase family. The study revealed that the recombinant EstD04-His(6x) protein exhibited esterase activity and broad substrate specificity, as it was capable of hydrolyzing p-nitrophenyl derivatives with different acyl chain lengths. By using the most favorable substrate p-nitrophenyl butyrate (C4), we defined the optimal temperature and pH value for EstD04 esterase activity as 40 °C and pH 8, respectively, with a catalytic efficiency (kcat/Km) of 6.17 × 103 mM−1 s−1 at 40 °C. EstD04 demonstrated high stability between pH 8 and 10, and thus, it might be capably used as an alkaline esterase in industrial applications. The addition of Mg2+ and NH4+, as well as DMSO, could stimulate EstD04 enzyme activity. Based on bioinformatic motif analyses and tertiary structural simulation, we determined EstD04 to be a typical bHSL protein with highly conserved motifs, including a triad catalytic center (Ser160, Glu253, and His283), two cap regions, hinge sites, and an oxyanion hole, which are important for the type IV enzyme activity. Moreover, the sequence analysis suggested that the two unique discrete cap regions of EstD04 may contribute to its alkali mesophilic nature, allowing EstD04 to exhibit extremely distinct physiological properties from its evolutionarily closest esterase.

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Immobilization of an endophytic Bacillus sp. on Phragmites karka stem for lipase production in the presence of Cassia fistula seeds

Ashraf,

Sohail,

Abideen

et al. 2024

Biofuels Bioprod Bioref

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Endophytic bacteria have not been reported widely for their lipolytic abilities, so they are not used for large‐scale lipase production. The purpose of this study was to explore an endophytic bacterium for the production of lipase implementing cost‐effective techniques, including the use of Cassia fistula seeds, as a substrate in the production medium and stem pieces of Phragmites karka as the immobilization matrix. The endophytic strain Bacillus sp. E4 was originally isolated from the halophytic plant Arthrocnemum macrostachyum. Bacillus sp. E4 produced 6.05 IU mL−1 lipase in the presence of powdered seeds of Cassia fistula (golden shower tree). Initial trial experiments using a one‐factor‐at‐a‐time approach led to an improvement in lipase titers to 10.05 IU mL−1. Consequently, investigations using the Plackett–Burman design suggested the influence of three significant factors – incubation period, inoculum size, and substrate concentration – on lipase production. They were optimized using the Box–Behnken design (BBD). In the response optimization experiment, strain E4 yielded 52.35 IU mL−1 lipase, which was in accordance with the predicted yield and indicated an overall 8.65 fold improvement in lipase production. To investigate the use of free cells, strain E4 was immobilized on the stem pieces of a halophytic plant, Phragmites karka, which was used for the first time as an immobilization matrix. The immobilized cells retained lipase production ability for up to six cycles with the highest yield of 110 IU mL−1, which corresponded to an improvement of more than eighteenfold. Scanning electron micrographs confirmed the colonization of E4 cells in the matrix and demonstrated the utilization of C. fistula seeds. Fourier transform infrared spectroscopy affirmed the utilization of components including fatty acids by the immobilized E4 cells. The study suggests that endophytic bacterial strains could be applied for the production of lipase with the utilization of nontraditional oil sources.

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Higher tolerance of a novel lipase from Aspergillus flavus to the presence of free fatty acids at lipid/water interface

Cited by 8 publications

References 18 publications

A Valuable Product of Microbial Cell Factories: Microbial Lipase

A Valuable Product of Microbial Cell Factories: Microbial Lipase

Enzymatic Characterization of a Novel HSL Family IV Esterase EstD04 from Pseudomonas sp. D01 in Mealworm Gut Microbiota

Immobilization of an endophytic Bacillus sp. on Phragmites karka stem for lipase production in the presence of Cassia fistula seeds

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