Effect of different carbon sources on lipase production by Candida rugosa

Dalmau, E.; Montesinos, José Luis González; Lotti, Marina; Casas, C.

doi:10.1016/s0141-0229(00)00156-3

Cited by 161 publications

(99 citation statements)

References 25 publications

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“…These results were agreed with Pokorny et al (1994), Long et al (1996), Dalmau et al (2000) and Li et al (2005) reported that lipase synthesis is known to be repressed by high concentration of oleic acid. Tween 20 and 80 had inhibitory effects (54.7-31.4%) on the lipolytic activities at all levels Table 5.…”

Section: Response Of Some Additivessupporting

confidence: 92%

Optimization of lipase synthesis by Mucor racemosus - Production in a triple impeller bioreactor

Nadia¹,

Nehad²,

El-Sayed³

et al. 2010

MJM

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Fungal cultures were screened for their ability to produce extracellular lipase through different incubation periods, in spite of some Aspergillus niger gave highest lipolytic activities, Mucor racemosus was selected in this study due to its non-pathogenicity. Optimum lipase activity was obtained after 3 days incubation period at 35 °C using submerged culture technique. Using a modified complex medium (3% peptone; 0.2% KH2PO4; 0.05% KCl; 0.05% MgSO4 . 7H2O; 1% glucose; 1% olive oil and 0.01 M barium acetate as additives; pH was adjusted to 7.0 using 0.2 M phosphate buffer) stimulated M. racemosus lipase by 114.3%. The production of lipolytic enzyme by M. racemosus was up-scaled to 5 L stirred-tank bioreactor. Under optimized conditions, lipase and specific enzyme activities were improved by 2 folds (1211 U/mL and 28 U/mg protein) as compared to shake flask studies.

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Section: Response Of Some Additivessupporting

confidence: 92%

Optimization of lipase synthesis by Mucor racemosus - Production in a triple impeller bioreactor

Nadia¹,

Nehad²,

El-Sayed³

et al. 2010

MJM

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“…1) could be observed except for the F1 microorganism, which possibly is associated with the release of proteases produced during the cell growth phase (Dalmau et al, 2000). A similar fact was reported by Bussamara et al, (2010) who evidenced the presence of proteases in the medium resulting in a reduction in lipolytic activity after 19 h of fermentation of lipase from Pseudozyma hubeiensis.…”

Section: Cultivation In Liquid Medium: Lipolytic and Esterification Asupporting

confidence: 74%

Isolation of Lipase-Producing Yeasts from Industrial Oily Residues in Different Culture Media

Paludo¹,

Oliveira²,

Trevisol³

et al. 2018

Int.J.Curr.Microbiol.App.Sci

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“…Microbial lipases find many applications including organic synthesis and bioconvertions in the food and detergent industries, paper and oleochemical industries, cosmetics, medicine, and waste treatment 11,12,13 . The majority of commercially significant lipases are produced by Candida rugosa, C. antarctica, Aspergillus niger, Rhizomucor miehei and Rhizopus arrhizus 14,15 . Lipases are produced intracellularly or extracellularly, although there is a wide range of cell wall -bound enzymes 16,17,18 .…”

Section: Introductionmentioning

confidence: 99%

Study on the Properties of Immobilized Biocatalysts with Lipase Activity Produced by Yarrowia lipolytica in Batch Culture

Stolarzewicz

Zaborniak

Fabiszewska

et al. 2017

Chem.Biochem.Eng.Q.

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Three kinds of matrices (calcium alginate, gelatin, and PVA) were employed as supports to immobilize lipases from Y. lipolytica KKP 379 via physical adsorption. The stability of biocatalysts (free and immobilized) was evaluated by measuring the enzyme activity before and after treatment with the method based on the hydrolysis of p-nitrophenyl laurate. Two fractions of enzymes were immobilized: cell-bound (yeast biomass) and extracellular (supernatant). The yield of immobilization and catalytic properties of immobilized lipases were investigated. Satisfactory results for lipolytic activity and biocatalyst stability were obtained for cell-bound enzymes immobilized in alginate (0.38 U g -1 d.m.) and crosslinked gelatin (0.18 U g -1 d.m.). Immobilization of the supernatant was successful only on the alginate (0.026 U g -1 d.m.). After lyophilization, no significant difference was noticed between treated and untreated biocatalysts. Lyophilized catalysts were successfully immobilized in all three matrices, but the process reduced their lipolytic activity probably due to an insufficient amount of water in the reaction solution.

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Effect of different carbon sources on lipase production by Candida rugosa

Cited by 161 publications

References 25 publications

Optimization of lipase synthesis by Mucor racemosus - Production in a triple impeller bioreactor

Optimization of lipase synthesis by Mucor racemosus - Production in a triple impeller bioreactor

Isolation of Lipase-Producing Yeasts from Industrial Oily Residues in Different Culture Media

Study on the Properties of Immobilized Biocatalysts with Lipase Activity Produced by Yarrowia lipolytica in Batch Culture

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