One Biocatalyst–Many Applications: The Use of Candida Antarctica B-Lipase in Organic Synthesis

Anderson, Emily M.; Larsson, Karin; Kirk, Ole

doi:10.3109/10242429809003198

Cited by 645 publications

(364 citation statements)

References 144 publications

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“…A simple and reliable method for detecting lipase activity in microorganisms has been described by different researchers. Tween 80 (surfactant) in a solid substrate has been used extensively to identify a lipolytic activity by those researchers [19][20][21]. Lipase preparation by the organisms can be specified by the formation of dark zones around the colonies.…”

Section: Introductionmentioning

confidence: 99%

Effect of Environmental and Nutritional Parameters on the Extracellular Lipase Production by <i>Aspergillus niger</i>

El-Batal

Farrag

Elsayed

et al. 2016

ILNS

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Abstract. The present investigation was carried out to evaluate the effect of different growth conditions on lipase production by Aspegillus niger. The extracellular lipase producing fungus was isolated from spent bleaching earths. Optimizations of physical and chemical parameters were done for maximum lipase production using this isolate. Growth of the organism and lipase production were measured usig varying pH (4 -9), incubation temperature (20 -30 °C), incubation time (8 -80 hrs.), carbon sources, nitrogen sources, and shaking speed. Enhanced lipase production was observed at 24 °C, pH 7 and after 72hrs of incubation. Olive oil 5 % was observed as the most effective carbon source and Yeast extract 1.0 % as the most effective nitrogen source for lipase production. The optimum shaking value to get maximum lipase activity by Aspergillus niger was 200 rpm.

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Section: Introductionmentioning

confidence: 99%

Effect of Environmental and Nutritional Parameters on the Extracellular Lipase Production by <i>Aspergillus niger</i>

El-Batal

Farrag

Elsayed

et al. 2016

ILNS

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“…This lipase catalyzes the hydrolysis of esters in aqueous solution following the same reaction mechanism as that of a serine protease (17). To study the catalysis by single lipase, we used a fluorogenic substrate, namely the nonf luorescent ester 2Ј,7Ј-bis-(2-carboxyethyl)-5-(and-6)-carboxyfluorescein acetoxymethyl ester, which upon hydrolysis forms a highly fluorescent carboxylic acid product (18,19).…”

mentioning

confidence: 99%

Stretched exponential decay and correlations in the catalytic activity of fluctuating single lipase molecules

Flomenbom

Velonia²,

Loos³

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

287

261

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Single-molecule techniques offer a unique tool for studying the dynamical behavior of individual molecules and provide the possibility to construct distributions from individual events rather than from a signal stemming from an ensemble of molecules. In biological systems, known for their complexity, these techniques make it possible to gain insights into the detailed spectrum of molecular conformational changes and activities. Here, we report on the direct observation of a single lipase-catalyzed reaction for extended periods of time (hours), by using confocal fluorescence microscopy. When adding a profluorescent substrate, the monitored enzymatic activity appears as a trajectory of ''on-state'' and ''off-state'' events. The waiting time probability density function of the off state and the state-correlation function fit stretched exponentials, independent of the substrate concentration in a certain range. The data analysis unravels oscillations in the logarithmic derivative of the off-state waiting time probability density function and correlations between off-state events. These findings imply that the fluctuating enzyme model, which involves a spectrum of enzymatic conformations that interconvert on the time scale of the catalytic activity, best describes the observed enzymatic activity. Based on this model, values for the coupling and reaction rates are extracted.single enzyme activity ͉ two-state trajectories D ynamics of chemical reactions are conventionally investigated by ensemble measurements. Recent advances in single-molecule spectroscopy have enabled the real-time study of biophysical processes (1-10) and conformational changes (11, 12) of single biomolecules. These studies have demonstrated that new information about such processes can be extracted from single-molecule measurements. In particular, deviations from the standard Michaelis-Menten behavior (13,14), which is expected for bulk enzymatic activity, have been observed (6 -8, 12).Motivated by these findings, we examined the enzymatic activity of individual molecules of the 33-kDa lipase B from Candida antarctica molecules (15, 16) by using confocal fluorescence microscopy. This lipase catalyzes the hydrolysis of esters in aqueous solution following the same reaction mechanism as that of a serine protease (17). To study the catalysis by single lipase, we used a fluorogenic substrate, namely the nonf luorescent ester 2Ј,7Ј-bis-(2-carboxyethyl)-5-(and-6)-carboxyfluorescein acetoxymethyl ester, which upon hydrolysis forms a highly fluorescent carboxylic acid product (18,19). This method enabled us to probe the enzymatic activity by monitoring the fluorescence emission from single enzymes. The fluorescence emission displayed blinking of ''on'' and ''off'' events depending on the presence (or absence) of the fluorescent product in the confocal focus (20). By using this approach, we have been able to obtain long trajectories (for time periods of hours) suitable for reliable statistical analysis while varying the concentration of the substrate, thus ...

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“…For example, Pseudozyma flocculosa (Traquair, L. A. Shaw & Jarvis) Boekhout & Traquair is a well-documented biocontrol agent of powdery mildew (Paulitz & Belangér, 2001). Other interesting applied features of smut anamorphs are the accumulation of lipids (~41 % of the dry weight) by Candida 107 (Gill et al, 1977), which seems closely related to Pseudozyma antarctica (Goto et al) Boekhout (T. Boekhout, unpublished), and the production of extracellular mannosylerythritol lipids and commercially exploited B-lipase by P. antarctica (Anderson et al, 1998;Kitamoto et al, 1990). We do not know whether the currently described fungi also share these properties, but it may be very interesting to explore this in the future.…”

Section: Applied Aspectsmentioning

confidence: 99%

Novel anamorphic mite-associated fungi belonging to the Ustilaginomycetes: Meira geulakonigii gen. nov., sp. nov., Meira argovae sp. nov. and Acaromyces ingoldii gen. nov., sp. nov.

Boekhout

Theelen

Houbraken

et al. 2003

International Journal of Systematic and Evolutionary Microbiology

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One Biocatalyst–Many Applications: The Use of Candida Antarctica B-Lipase in Organic Synthesis

Cited by 645 publications

References 144 publications

Effect of Environmental and Nutritional Parameters on the Extracellular Lipase Production by <i>Aspergillus niger</i>

Effect of Environmental and Nutritional Parameters on the Extracellular Lipase Production by <i>Aspergillus niger</i>

Stretched exponential decay and correlations in the catalytic activity of fluctuating single lipase molecules

Novel anamorphic mite-associated fungi belonging to the Ustilaginomycetes: Meira geulakonigii gen. nov., sp. nov., Meira argovae sp. nov. and Acaromyces ingoldii gen. nov., sp. nov.

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