Microorganisms Isolated from Moroccan Olive-Mill Wastes: Screening of Their Enzymatic Activities for Biotechnological Use

Misbah, Asmae; Aouine, Mouna; Raouan, Safae Er; Lekbach, Yassir; Ettadili, Hamza; Koraichi, Saâd Ibnsouda; Jouti, Mohamed Ali Tahri

doi:10.19044/esj.2019.v15n30p464

Cited by 2 publications

(2 citation statements)

References 66 publications

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“…Proteus vulgaris OR34 (NCBI accession number: MN 622879) was previously isolated from Moroccan olive mill wastes [22] and routinely maintained on Luria-Bertani agar. The production of Proteus vulgaris OR34 lipase is ensured on a liquid medium previously described [22], which composed of (g• l -1 ): 15 casein peptone, 5 yeast extract, 5 NaCl, 2.5 glucose, 3 K 2 HPO 4 , 1 KH 2 PO 4 , with a final pH of 7.4. After 30 h of incubation at 37℃ and 180 rpm, the supernatant that contains the crude extracellular lipase, was recovered by centrifugation at 13,000 rpm for 20 min at 4℃.…”

Section: Lipase Production and Extractionmentioning

confidence: 99%

Purification, Characterization and Immobilization of Lipase from Proteus vulgaris OR34 for Synthesis of Methyl Oleate

Misbah¹,

Koraichi²,

Jouti³

2020

Microbiology and Biotechnology Letters

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A newly isolated strain, Proteus vulgaris OR34, from olive mill waste was found to secrete an alkaline extracellular lipase at 11 U• ml -1 when cultivated on an optimized liquid medium. This lipase was purified 94.64fold with a total yield of 9.11% and its maximal specific activity was shown to be 3232.58 and 1777.92 U•mg -1 when evaluated using the pH-stat technique at 55℃ and pH 9 and Tributyrin TC4 or olive oil as the substrate. The molecular mass of the pure OR34 lipase was estimated to be around 31 kDa, as revealed by SDS-PAGE and its substrate specificity was investigated using a variety of triglycerides. This assay revealed that OR34 lipase preferred short and medium chain fatty acids. In addition, this lipase was stable in the presence of high concentrations of bile salt (NaDC) and calcium ions appear not to be necessary for its activity. This lipase was inhibited by THL (Orlistat) which confirmed its identity as a serine enzyme. In addition, the immobilization of OR34 lipase by adsorption onto calcium carbonate increased its stability at higher temperatures and within a larger pH range. The immobilized lipase exhibited a high tolerance to organic solvents and retained 60% of its activity after 10 months of storage at 4℃. Finally, the OR34 lipase was applied in biodiesel synthesis via oleic acid mediated esterification of methanol when using hexane as solvent. The best conversion yield (67%) was obtained at 12 h and 40℃ using the immobilized enzyme and this enzyme could be reused for six cycles with the same efficiency.

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Section: Lipase Production and Extractionmentioning

confidence: 99%

Purification, Characterization and Immobilization of Lipase from Proteus vulgaris OR34 for Synthesis of Methyl Oleate

Misbah¹,

Koraichi²,

Jouti³

2020

Microbiology and Biotechnology Letters

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“…However, such production has led to a much larger number of inedible components. In fact, in the OO extraction process, 20% of oil is acquired, while 80% is considered as olive mill wastewater (OMW) [ 2 , 3 , 4 ]. The valorization of OMW is actually a challenging opportunity for the viable and competitive development of the OO industry.…”

Section: Introductionmentioning

confidence: 99%

Purification, Biochemical and Kinetic Characterization of a Novel Alkaline sn-1,3-Regioselective Triacylglycerol Lipase from Penicilliumcrustosum Thom Strain P22 Isolated from Moroccan Olive Mill Wastewater

Hasnaoui

Dab

Mechri

et al. 2022

IJMS

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A novel extracellular lipase from a filamentous fungus Ascomycota strain, P22, was isolated from olive mill wastewater, then purified and characterized. This strain was identified as Penicillium crustosum Thom based on sequencing analyses. Penicillium crustosum Thom strain P22 lipase (PCrL) was purified 63-fold to homogeneity using ammonium sulfate precipitation and chromatography on a Q-Sepharose Fast Flow column, with a total yield of 34%. The purified PCrL had a molecular mass of 28 kDa, estimated by SDS-PAGE. The 20 NH2-terminal amino-acid residues showed a high degree of homology with those of other Penicillium lipases. The specific activity of PCrL at pH 9 and 37 °C were found to be 5000 and 10,000 U/mg on olive oil and trioctanoin emulsions, respectively. PCrL exhibited clear regioselectivity toward the sn-1 position of the surface-coated triglycerides which were esterified with α-eleostearic acid at the sn-1/3 position. PCrL was completely inhibited by 53 µM of Orlistat, 5 mM of phenylmethylsulfonylfluoride, and 2 mM of diiodopropyl fluorophosphate, suggesting that it belonged to the serine lipase family. PCrL showed high activity and stability in the presence of water-immiscible organic solvents, surfactant, and oxidizing agents, and showed considerable compatibility with commercial laundry detergents. Washing performance analysis revealed that it could effectively remove oil stains. Hence, PCrL has several attractive properties that make it a promising potential candidate for detergent formulations.

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Microorganisms Isolated from Moroccan Olive-Mill Wastes: Screening of Their Enzymatic Activities for Biotechnological Use

Cited by 2 publications

References 66 publications

Purification, Characterization and Immobilization of Lipase from Proteus vulgaris OR34 for Synthesis of Methyl Oleate

Purification, Characterization and Immobilization of Lipase from Proteus vulgaris OR34 for Synthesis of Methyl Oleate

Purification, Biochemical and Kinetic Characterization of a Novel Alkaline sn-1,3-Regioselective Triacylglycerol Lipase from Penicilliumcrustosum Thom Strain P22 Isolated from Moroccan Olive Mill Wastewater

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