Lipolytic Potential of<i>Aspergillus japonicus</i>LAB01: Production, Partial Purification, and Characterisation of an Extracellular Lipase

Souza, Leandro Torres de; Oliveira, Jamil S.; Santos, Vera Lúcia dos; Régis, Wiliam César Bento; Santoro, Marcelo M.; Resende, Rodrigo R.

doi:10.1155/2014/108913

Cited by 16 publications

(16 citation statements)

References 63 publications

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“…A significant ( p < 0.00015) enhancement in lipase activity, as shown by the combinatorial influence of nitrogen supplements, could be attributed to improved metabolism of the fungus in the presence of accessory growth factors, vitamins and amino acids supplied by tryptone. Souza et al reported that a combination of casein and sodium nitrate led to increased lipase production from Aspergillus japonicus LAB01 in medium supplemented with sunflower oil (1%, v/v).…”

Section: Discussionmentioning

confidence: 99%

Coconut oil induced production of a surfactant-compatible lipase fromAspergillus tamariiunder submerged fermentation

Das

Bhattacharya

Shivakumar

et al. 2016

J. Basic Microbiol.

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Filamentous fungi are efficient producers of lipases. The present study focuses on identification of a potent lipolytic fungus and enhancement of lipase production through optimization of nutritional and cultural conditions under submerged fermentation. Molecular characterization of the fungus by 18S rDNA sequencing revealed its identity as Aspergillus tamarii with 98% homology. Maximum lipase production was noted in mineral salts medium supplemented with coconut oil (2.5%, v/v). A combination of ammonium chloride (2%, w/v) and tryptone (2%, w/v) facilitated maximum lipase production at pH 5 of the production medium. A carbon: nitrogen ratio of 1:4 led to significant (p < 0.00008) increase in the enzyme production in the presence of surfactant cetyltrimethylammonium bromide (0.5%, w/v). Maximum lipase activity (2,32,500 ± 192 U/ml/min) was recorded after 7 days of incubation at 25 °C on a rotary shaker at 120 rpm. A 9.8-fold increase in lipase activity was recorded after optimization of the process parameters. Addition of crude lipase enhanced the oil stain removal activity of a commercially available detergent by 2.2-fold. The current findings suggest the potentiality of this fungal lipase to be used in detergent formulation.

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Section: Discussionmentioning

confidence: 99%

Coconut oil induced production of a surfactant-compatible lipase fromAspergillus tamariiunder submerged fermentation

Das

Bhattacharya

Shivakumar

et al. 2016

J. Basic Microbiol.

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“…The purification result of the lipase using Sepharose CL-6B in this study is comparable with those using other gel filtration matrices. For example, purification of lipase from Geobacillus thermodenitrificans using Sephadex G-100 is 34-fold higher than the crude extract ( Balan et al., 2012 ), while purification of lipase from Aspergillus japonicus using Superose 12 H is 4-fold higher than the crude extract ( Souza et al., 2014 ).…”

Section: Resultsmentioning

confidence: 99%

Novel thermostable lipase produced by a thermo-halophilic bacterium that catalyses hydrolytic and transesterification reactions

Febriani

Aura

Kemala

et al. 2020

Heliyon

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Lipase belongs to the class of hydrolytic enzymes that are widely used in the biotechnology industries. The goal of this research was to purify and characterize lipase produced from a thermo-halophilic bacterium, namely Pria Laot Sabang 80 (PLS 80). Purification was performed using ammonium sulphate fractionation, followed by gel filtration chromatography using Sepharose Cl-6B. After purification, the enzyme had a specific activity of 326.6 U/mg with a purity of 6.02 higher than the crude extract; with a molecular weight of around 50 kDa. The optimum activity was observed at 70 °C and pH 9. The activity increased in the presence of 10 mM Mn 2+ , K + and Ca 2+ ions, while Hg 2+ only slightly increased the enzyme activity. In contrast, the activity decreased in 10 mM Mg 2+ , Zn 2+ , Co 2+ , EDTA, and PMSF. The enzyme showed good hydrolytic activity on long fatty acids substrates ( p -nitrophenyl palmitate) with a value of 35.5 U/mL. It was also able to catalyze a transesterification reaction. GC-MS result showed that the biodiesel consisted of methyl octanoate (5.3%), methyl caprate (12.4%), methyl laurate (34.1%), methyl myristate (10.7%), methyl palmitate (3.9%), and methyl stearate (1.2%) when using coconut oil as the substrate. The results suggested that the lipase from PLS 80 had unique attributes that could be useful in various industrial applications.

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“…Enzyme activity was measured by monitoring spectrophotometrically the increase in absorbance at 410 nm, produced by the release of p -nitrophenol (pNP) in the hydrolysis of p -nitrophenylpalmitate (pNPP). For the hydrolytic assay, the substrate solution was prepared by mixing 1 mL of solution A (90 mg of pNPP dissolved in 30 mL 2-propanol) and 9 mL of solution B (90 mM Tris-HCl buffer (pH 8.0); 2.0% Triton X-100; and 0.2% gum arabic) [ 37 ]. All analyses were performed in triplicate.…”

Section: Methodsmentioning

confidence: 99%

Immobilization of Moniliella spathulata R25L270 Lipase on Ionic, Hydrophobic and Covalent Supports: Functional Properties and Hydrolysis of Sardine Oil

et al. 2017

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The oleaginous yeast Moniliella spathulata R25L270 was the first yeast able to grow and produce extracellular lipase using Macaúba (Acrocomia aculeate) cake as substrate. The novel lipase was recently identified, and presented promising features for biotechnological applications. The M. spathulata R25L270 lipase efficiently hydrolyzed vegetable and animal oils, and showed selectivity for generating cis-5,8,11,15,17-eicosapentaenoic acid from sardine oil. The enzyme can act in a wide range of temperatures (25–48 °C) and pH (6.5–8.4). The present study deals with the immobilization of M. spathulata R25L270 lipase on hydrophobic, covalent and ionic supports to select the most active biocatalyst capable to obtain omega-3 fatty acids (PUFA) from sardine oil. Nine immobilized agarose derivatives were prepared and biochemically characterized for thermostability, pH stability and catalytic properties (KM and Vmax). Ionic supports improved the enzyme–substrate affinity; however, it was not an effective strategy to increase the M. spathulata R25L270 lipase stability against pH and temperature. Covalent support resulted in a biocatalyst with decreased activity, but high thermostability. The enzyme was most stabilized when immobilized on hydrophobic supports, especially Octyl-Sepharose. Compared with the free enzyme, the half-life of the Octyl-Sepharose derivative at 60 °C increased 10-fold, and lipase stability under acidic conditions was achieved. The Octyl-Sepharose derivative was selected to obtain omega-3 fatty acids from sardine oil, and the maximal enzyme selectivity was achieved at pH 5.0.

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Lipolytic Potential ofAspergillus japonicusLAB01: Production, Partial Purification, and Characterisation of an Extracellular Lipase

Cited by 16 publications

References 63 publications

Coconut oil induced production of a surfactant-compatible lipase fromAspergillus tamariiunder submerged fermentation

Coconut oil induced production of a surfactant-compatible lipase fromAspergillus tamariiunder submerged fermentation

Novel thermostable lipase produced by a thermo-halophilic bacterium that catalyses hydrolytic and transesterification reactions

Immobilization of Moniliella spathulata R25L270 Lipase on Ionic, Hydrophobic and Covalent Supports: Functional Properties and Hydrolysis of Sardine Oil

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