p-nitrophenyllaurate: a substrate for the high-performance liquid chromatographic determination of lipase activity

Maurich, V.; Zacchigna, Marina; Pitotti, A.

doi:10.1016/0378-4347(91)80262-b

Cited by 20 publications

(8 citation statements)

References 6 publications

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“…The characteristics of purified LipK107 were determined as previously described (Maurich et al, 1991;Prim et al, 2000). One unit of activity was defined as the amount of enzyme needed to release 1 mol of p-nitrophenol per minute under the assay conditions.…”

Section: Expression Purification and Characterization Of Lipase Lipk107mentioning

confidence: 99%

Development of recombinant Escherichia coli whole-cell biocatalyst expressing a novel alkaline lipase-coding gene from Proteus sp. for biodiesel production

Gao¹,

Su²,

Lin³

et al. 2009

Journal of Biotechnology

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Section: Expression Purification and Characterization Of Lipase Lipk107mentioning

confidence: 99%

Development of recombinant Escherichia coli whole-cell biocatalyst expressing a novel alkaline lipase-coding gene from Proteus sp. for biodiesel production

Gao¹,

Su²,

Lin³

et al. 2009

Journal of Biotechnology

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“…These authors gave details as to the specific activity and reproducibility of lauric ester alone, because palmitic ester turned out to be a very poor substrate for PPL [116].…”

Section: Chromatographic Assaysmentioning

confidence: 99%

Methods for lipase detection and assay: a critical review

Beisson¹,

Tiss

Rivière

et al. 2000

Eur. J. Lipid Sci. Technol.

335

169

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“…One unit [U] of lipase activity is defined as the amount of enzyme that causes the release of 1 lmol p-nitrophenol/min under the test conditions. The molar absorption coefficient of p-nitrophenol at 420 nm is 13.5 mol ±1 cm ±1 [3,10,11].…”

Section: Measurement Of Lipase Activitymentioning

confidence: 99%

A Novel Olive Oil Degrading Thermoactinomyces Species with a High Extremely Thermostable Lipase Activity

Al-Khudary

Hashwa²,

Mroueh

2004

Engineering in Life Sciences

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A filamentous, Gram-positive, spore forming aerobic bacterium was isolated from olive oil contaminated soil (Al Koura, Lebanon) on rhodamine agar plates at 60 C. The isolate, HRK-1 produced large quantities of an extracellular thermostable lipase which degrades olive oil. It was primarily classified as a Thermoactinomyces sp. due to the filamentous structure of its cells that bear one spore each on an un-branched sporophore, the resistance of its spores to boiling, utilisation of sucrose as a carbon source and production of dark pigments. The isolate grew optimally at a temperature of 60 C, a pH of 7.3 and an orbital shaking of 250 rpm. It showed an efficient olive oil degrading ability. No traces of triolein were detected after a 36-h cultivation. A concentration of 10 % [v/v] olive oil did not inhibit its growth. Lipase production was constitutive, and did not depend on the presence of olive oil. The optimum concentration of olive oil for lipase activity was 1 % [v/v], and the activity was not enhanced at higher concentrations, but on the contrary, a decrease in enzyme activity was recorded. The lipase of HRK-1 was preliminarily characterised in the crude cell-free supernatant with a specific activity of 0.14 U/mg. It has an optimum activity at 60 C and a pH of 8.0. This lipolytic enzyme showed resistance to boiling and to a wide range of metallic ions and inhibitors. The formation of this heat-stable lipase started in the early exponential growth phase, while a maximum extracellular enzyme activity was detected at the end of the decline phase, when most of the cells appeared as spherical spores. The exceptionally high activity of lipase (2.37 U/ml) produced by HRK-1 measured in the cell free supernatant clearly indicated the commercial importance of this isolate, especially after it showed great stability at elevated temperatures.

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p-nitrophenyllaurate: a substrate for the high-performance liquid chromatographic determination of lipase activity

Cited by 20 publications

References 6 publications

Development of recombinant Escherichia coli whole-cell biocatalyst expressing a novel alkaline lipase-coding gene from Proteus sp. for biodiesel production

Development of recombinant Escherichia coli whole-cell biocatalyst expressing a novel alkaline lipase-coding gene from Proteus sp. for biodiesel production

Methods for lipase detection and assay: a critical review

A Novel Olive Oil Degrading Thermoactinomyces Species with a High Extremely Thermostable Lipase Activity

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