Investigation of lipases from various Carica papaya varieties for hydrolysis of olive oil and kinetic resolution of (R,S)-profen 2,2,2-trifluoroethyl thioesters

Ng, I-Son; Tsai, Shau Wei

doi:10.1016/j.procbio.2005.10.011

Cited by 12 publications

(17 citation statements)

References 15 publications

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“…A similar temperature optimum was reported as 65°C for almond lipase using soy bean oil as the substrate [22]. The optimum temperatures for different C. Papaya lipases have been generally reported between 40 and 50°C by using olive oil as the substrate [21].…”

Section: Temperature Optimumsupporting

confidence: 68%

“…In our previous study, this value was found to be 8.0 for almond lipase [22]. Ng and Tsai reported that the optimum pH of Carica papaya occurred at 8.5 [21]. Plant lipases have been reported as having optimal activity at neutral or basic pH values.…”

Section: Effect Of Ph On Lipase Activitymentioning

confidence: 85%

“…There has been a growing interest in plant lipases in recent years since they are cheap, very versatile, and stable in organic media [11][12][13]. Lipases from plant families like Asclepiadaceae [14], Euphorbiaceae [15][16][17], Caricaceae [18][19][20][21], or Rosaceae [22] have been described as useful biocatalysts for several applications. Very little work on 'unusual' or tropical seeds has been reported [21].…”

Section: Introductionmentioning

confidence: 99%

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Biocatalytic Properties of Lipase from Walnut Seed (Juglans regia L.)

Yeşiloğlu¹,

Demirkan²

2010

J Americ Oil Chem Soc

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Lipase (E.C. 3.1.1.3) from walnut seed was purified 28.6-fold with 31% yield using Sephadex G-100 gel chromatography. Olive oil served as good substrate for the enzyme. The optimum pH and temperature were 9.0 and 70°C, respectively. The lipase was stable between 30 and 80°C for 5 min. K m and V max values were determined as 48 mM and 23.06 9 10 -3 U/min mg for triolein as substrate. Lipase activity was slightly reduced by Cu 2? , Ca 2? , Hg 2? , Mn 2? , and Ni 2? ions, while Mg 2? and Zn 2? had no effects. Anionic surfactant sodium dodecyl sulfate stimulated lipase activity while non-ionic surfactants Tween-80 and Triton X-100 had negligible effects on enzymatic activity. The enzyme activity was not affected by 50 mM urea and thioacetamide. Potassium ferricyanide, n-bromosuccinamide and potassium cyanide reduced the enzyme activity. The enzyme showed a good stability in organic solvents, the best result being in n-hexane (113% residual activity). The activity of dialysate was maintained approximately 80% for 1 year at -20°C.

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Section: Temperature Optimumsupporting

confidence: 68%

Section: Effect Of Ph On Lipase Activitymentioning

confidence: 85%

Section: Introductionmentioning

confidence: 99%

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Biocatalytic Properties of Lipase from Walnut Seed (Juglans regia L.)

Yeşiloğlu¹,

Demirkan²

2010

J Americ Oil Chem Soc

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“…These findings are consistent with those reported by Acikel et al, [14] Ma et al [17] and Pogori et al [15] SDS In the water/SDS system, the mole ratio v o is directly proportional to the size of the dispersed water pool. [18] On the contrary, the optimum pH of the walnut lipase, [19] almond lipase [20] and Carica papaya lipase [21] was found to be 9, 8 and 8.5, respectively. As reported by others for the activity of different micellar-encapsulated enzyme [10,11] For the systems under the study, the lipase contacts the water pool interface.…”

Section: Effect Of Various Cations On the Activity Of Lipasementioning

confidence: 99%

“…[21] The relation between the rate of enzymatic reaction and activation energy is given by empirical equation of Arrhenius: [22] E a ¼ 2:3026 R T 2 T 1 logV 2 =V 1 T 2 À T 1 This was due to the enzyme molecules which can be entrapped in the water pools, avoiding direct contact with olive oil that acts as substrate.…”

Section: Effect Of Ph and Temperature On The Activity Of Dormant Lipasementioning

confidence: 99%

Characteristics of lipase in dormant seeds catalysed hydrolysis of olive oil in SDS‐olive oil reversed microemulsions

El‐Hefnawy

Sakran

2014

Can J Chem Eng

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The activity of lipase-catalysed hydrolysis of olive oil in SDS-1-butanol-olive oil-water microemulsions was investigated. The kinetics of lipases in reverse microemulsions and water were also compared. The influences of the characteristic parameters of these systems, such as pH, temperature (T), molar ratio (v o ) of water to SDS, the concentrations of enzyme and substrate, on the activity of an enzyme were examined. According to the optimum conditions the production and activity were measured at pH ¼ 4, T ¼ 40 8C, v o ¼ 12. The activation energy of the reaction was calculated from the Arrhenius plot. It was found that the hydrolysis reaction obeyed Michaelis-Menten kinetics and the apparent Michaelis K m,a and the apparent maximal reaction rate V max were determined. The effect of microemulsion's surfactant (SDS) on enzymatic activity was also discussed.

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Purification and Biochemical Characterization of Lipase from Tunisian Euphorbia peplus Latex

Aref

Mosbah²,

Fekih

et al. 2014

J Americ Oil Chem Soc

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Lipases from vegetable sources have been the focus of intense and growing research. The use of enzymes from plants has the advantage of employing industrial waste products. The lipase activity of Euphorbia peplus L. (Euphorbiaceae) was investigated for the first time. The Euphorbia peplus latex lipase (EpLL) was purified after ammonium sulfate fractionation and anion exchange chromatography on a DEAE-Cellulose column leading to 12.57-fold purification. The EpLL displayed a probable molecular weight of about 40 kDa. The lipase activity was optimum at a temperature of 40°C and pH 8, the specific activities of EpLL were found to be 249 ± 12.45 and 161.4 ± 8.07 U/mg when tributyrin (TC 4 ) and olive oil were used as substrate respectively. The enzyme retained 80 % of its activity when incubated for 1 h at 50°C. The EpLL was strongly destabilised by divalent metal ions (Fe 2? , Mg 2? , Zn 2? and Cu 2? ). Lipase was slightly stimulated by Triton X-100 and Tween-80, while strongly inhibited by sodium dodecyl sulfate. A good stability of the enzyme in the presence of organic solvents was reveled suggesting its industrial utility.

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Investigation of lipases from various Carica papaya varieties for hydrolysis of olive oil and kinetic resolution of (R,S)-profen 2,2,2-trifluoroethyl thioesters

Cited by 12 publications

References 15 publications

Biocatalytic Properties of Lipase from Walnut Seed (Juglans regia L.)

Biocatalytic Properties of Lipase from Walnut Seed (Juglans regia L.)

Characteristics of lipase in dormant seeds catalysed hydrolysis of olive oil in SDS‐olive oil reversed microemulsions

Purification and Biochemical Characterization of Lipase from Tunisian Euphorbia peplus Latex

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