Purification and Some Characteristics of Extracellular Lipase from<i>Fusarium oxysporum</i>f. sp.<i>lini</i>

Hashizume, Tamotsu; Sasaki, Takuji; Watanabe, Yuichi; Nagasawa, Tôru; Yamané, Tsuneo

doi:10.1271/bbb.56.660

Cited by 35 publications

(25 citation statements)

References 3 publications

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“…These results show that this enzyme is more stable than lipase from F. oxysporum f. sp. lini which activity was reduced by about 50% at 60ºC when the enzyme solution was incubated for 1h (6). Fig.…”

Section: Resultsmentioning

confidence: 90%

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Characterization of alkaline lipase from Fusarium oxysporum and the effect of different surfactants and detergents on the enzyme activity

Prazeres¹,

Cruz²,

Pastore³

2006

Braz. J. Microbiol.

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Nowadays, there is a tendency of use of low temperature in laundry cleaning for both environmental and economical reasons, which makes the use of enzymes in detergent products indispensable. Since lipases are efficient catalyst both in solution and at the water-liquid interface, they are potentially suitable for lipid stain removal applications in industrial laundry and household detergents. The effect of different commercial detergents and surfactants on enzymatic activity of lipase from Fusarium oxysporum was observed through p-nitrophenylpalmitate (pNPP) assay. The enzyme was compatible with various ionic and non-ionic surfactants as well as commercial detergents. Lipase activity was strongly inhibited by Sodium Dodecyl Sulphate (SDS), but not by Triton X-100 and Triton X-114. The best assay conditions observed for this lipase were pH 8.0 and 50ºC. The enzyme was stable at alkaline pH and remained 93% of residual activity during 1 h incubation at 60ºC. The highest lipase activity was measured with triglycerides of middle and long chain fatty acids (C8-C18). This enzyme showed a variable specifity/hydrolytic activity towards various fats and oils. All these properties and its resistance towards various surfactants and tolerance to commercial detergents make this lipase a potential additive for detergent formulation.

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Section: Resultsmentioning

confidence: 90%

“…These results were similar to those presented by lipase from Fusarium oxysporum f. sp. lini (6). On another hand, Rapp (15) found different properties for lipase from Fusarium oxysporum f. sp.…”

Section: Resultsmentioning

confidence: 99%

Characterization of alkaline lipase from Fusarium oxysporum and the effect of different surfactants and detergents on the enzyme activity

Prazeres¹,

Cruz²,

Pastore³

2006

Braz. J. Microbiol.

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“…3). The optimum activity for pNPP hydrolysis of 10,620 U.L (8,14). Lipase mantained around 80% its initial activity when incubated for one hour at pH values between 7.2 and 8.6, with an decrease in lipase activity at pH beyond this range.…”

Section: Resultsmentioning

confidence: 96%

“…The selectivity of lipases has been exploited in industry in the synthesis of chiral compounds as well as in the resolution of racemic mixtures (19). The production of lipase by several Fusarium oxysporum strains has been studied in terms of enzyme production, protein properties and purification (7,8,11). The aim of this work was to describe the production of an extracellular lipase by a Fusarium solani FS1 isolated from Carica papaya fruit.…”

Section: Introductionmentioning

confidence: 99%

Production of extracellular lipase by the phytopathogenic fungus Fusarium solani FS1

Maia

Morais

et al. 1999

Rev. Microbiol.

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A Brazilian strain of Fusarium solani was tested for extracellular lipase production in peptone-olive oil medium. The fungus produced 10,500 U.L -1 of lipase after 72 hours of cultivation at 25ºC in shake-flask at 120 rpm in a medium containing 3% (w/ v) peptone plus 0.5% (v/v) olive oil. Glucose (1% w/v) was found to inhibit the inductive effect of olive oil. Peptone concentrations below 3% (w/v) resulted in a reduced lipase production while increased olive oil concentration (above 0.5%) did not further stimulate lipase production. The optimum lipase activity was achieved at pH 8.6 and 30ºC and a good enzyme stability (80% activity retention) was observed at pH ranging from 7.6 to 8.6, and the activity rapidly dropped at temperatures above 50ºC. Lipase activity was stimulated by the addition of n-hexane to the culture medium supernatants, in contrast to incubation with water-soluble solvents.

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“…The preliminary investigation showed that the strain SUF 1377 had the highest lipase productivity and this strain was used throughout this study. Lipase production medium contained Tween 80 instead of Tween 20 and was based on the Fusnriumminimal medium (Hoshino et al, 1992).…”

Section: Fungal Strains and Mediamentioning

confidence: 99%

Production of low temperature active lipase from the pink snow mold, Microdochium nivale (syn. Fusarium nivale)

et al. 1996

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Purification and Some Characteristics of Extracellular Lipase fromFusarium oxysporumf. sp.lini

Cited by 35 publications

References 3 publications

Characterization of alkaline lipase from Fusarium oxysporum and the effect of different surfactants and detergents on the enzyme activity

Characterization of alkaline lipase from Fusarium oxysporum and the effect of different surfactants and detergents on the enzyme activity

Production of extracellular lipase by the phytopathogenic fungus Fusarium solani FS1

Production of low temperature active lipase from the pink snow mold, Microdochium nivale (syn. Fusarium nivale)

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