Acid Lipase from<i>Candida viswanathii</i>: Production, Biochemical Properties, and Potential Application

Almeida, Alex Fernando de; Tauk-Tornisielo, Sâmia Maria; Carmona, Eleonora Cano

doi:10.1155/2013/435818

Cited by 36 publications

(29 citation statements)

References 53 publications

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“…The lipase enzymes are classified as hydrolases (triacylglycerol hydrolases) that catalyze the hydrolysis of triglycerides into diglycerides, monoglycerides, free fatty acids and glycerol (Almeida et al 2013). Besides the hydrolysis, they can also catalyze esterification and GREICE H.S.…”

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confidence: 99%

Bioprospecting of lipolytic microorganisms obtained from industrial effluents

Peil

Kuss

Rave

et al. 2016

An. Acad. Bras. Ciênc.

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The lipases have ability to catalyze diverse reactions and are important in different biotechnological applications. The aim of this work was to isolate and characterize microorganisms that produce lipases, from different food industry effluents localized in Pelotas, RS/Brazil. Bacteria were identified using Gram stain and biochemical tests (Vitek 2®). Fungi were identified according to macro and micromorphology characteristics. The extracellular lipase production was evaluated using the Rhodamine B test and the enzymatic activity by titration. Twenty-one bacteria were isolated and identified as Klebsiella pneumoniae ssp. pneumoniae, Serratia marcescens, Enterobacter aerogenes, Raoultella ornithinolytica and Raoultella planticola. Were characterized isolated filamentous fungi by the following genera: Alternaria sp., Fusarium sp., Geotrichum sp., Gliocladium sp., Mucor sp., Paecilomyces sp. and Trichoderma sp. Extracellular lipase production was observed in 71.43% of the bacteria and 57.14% of the fungi. The bacterium that presented better promising enzymatic activity was E. aerogenes (1.54 U/ml) however between fungi there was not significant difference between the four isolates. This study indicated that microorganisms lipase producers are present in the industrial effluents, as well as these enzymes have potential of biodegradation of lipid compounds.

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confidence: 99%

Bioprospecting of lipolytic microorganisms obtained from industrial effluents

Peil

Kuss

Rave

et al. 2016

An. Acad. Bras. Ciênc.

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“…Above pH 6.5 there was a decrease in the activity up to pH 8.0. The crude C. viswanathii lipase shows optimum activity in slightly more acid condition (pH 3.5) compared to the free purified and immobilized lipase; and also, presents higher activity at pH from 2.0 to 3.0 (45-53%, respectively) [20]. Besides, the present lipase differs from those of C. antarctica, C. rugosa, and C. cylindracea which are neutral or alkaline enzymes [13,14].…”

Section: Effect Of Ph On Activity and Stabilitymentioning

confidence: 74%

“…Erlenmeyer flasks (125 mL) containing 25 mL of the medium were inoculated with 1.0 mL of cells suspension (1 × 10 7 cells/mL). Cultivation was carried out at 27.5°C, 210 rpm for 72 h [20].…”

Section: Liquid Culture and Protein Extract Preparationmentioning

confidence: 99%

“…Lipase activity was assayed with p-nitrophenyl palmitate (p-NPP) (Sigma-Aldrich) as substrate [20]. p-NPP was initially dissolved in 0.5 mL of dimethyl sulfoxide (DMSO), then diluted to 0.5 mM with McIlvaine buffer pH 3.5 containing 0.5% (w/v) Triton X-100.…”

Section: Lipase Activitymentioning

confidence: 99%

“…A Candida viswanathii strain grows and efficiently produces lipase when cultivated in liquid medium containing natural triacylglycerols, under agitation and temperature control [19,20]. Partial characterization showed that the crude enzyme is an acid and organic solvent tolerant lipase that could potentially be applied in bioprocesses.…”

Section: Introductionmentioning

confidence: 99%

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Biochemical properties of free and immobilized Candida viswanathii lipase on octyl-agarose support: Hydrolysis of triacylglycerol and soy lecithin

Almeida

Terrasan

Terrone

et al. 2018

Process Biochemistry

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A B S T R A C TMicrobial lipases are important enzymes in food and pharmaceutical industries. In this work, a Candida viswanathii lipase was purified by hydrophobic interaction chromatography on octyl Sepharose. The purification presented 78.4% yield and the enzyme was 8.7-fold purified, with specific activity 700.4 U/mg protein and 69 kDa molecular weight. Immobilization of the enzyme on the same support presented 72.5% yield and a derivative with 101% expressed activity (109.2 U/g support), indicating hyperactivation of the enzyme. Optimal activity for both free and immobilized lipase was observed at pH 4.0 and 45°C. The free and immobilized lipase showed broad-range stability from acid to neutral pH, and apparent activation and stability on organic solvents. The derivative was 60-fold thermostabilized in relation to the free enzyme and fully retained its activity after four cycles of p-nitrophenyl palmitate hydrolysis. Slight activation was observed with dithiothreitol and βmercaptoethanol. The free and immobilized lipase efficiently hydrolyzed monoesters, simple and mixed long chain triacylglycerols, as well as soy lecithin. The activity and stability in acid pH, the organic solvent tolerance and the lecithin hydrolysis indicate high potential application of the enzyme and its derivative in textile, food and pharma industries and for chemical synthesis.

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