Characterization of a new thermostable esterase from the moderate thermophilic bacterium Bacillus circulans

Kademi, Ali; Ait-Abdelkader, Nadra; Fakhreddine, Loubna; Baratti, J.

doi:10.1016/s1381-1177(99)00111-3

Cited by 44 publications

(22 citation statements)

References 28 publications

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“…pNFC2) and very low hydrolysis rates for fatty acid carbon chain higher than eight. 20 A similar pattern was indicated for Bacillus subtilis RRL 1789. 21 On the other hand, Sunna et al 22 described a thermoalkaliphilic lipase from Bacillus sp.…”

supporting

confidence: 70%

Evaluation of a novel Bacillus strain from a north‐western Spain hot spring as a source of extracellular thermostable lipase

Deive

Sanromán

Longo

2009

J of Chemical Tech & Biotech

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BACKGROUND: Thermophilic microorganisms are receiving significant attention as a source of useful thermostable enzymes. However, the number of known strains is still limited, and very often their most interesting biocatalysts are intracellular or membrane-bound and produced at low levels. Thus, the isolation and study of novel extracellular enzyme-producing thermophilic microorganisms is very interesting. Moreover, the assessment of bioreactor performance is crucial, given the scarce information on the large-scale culture of these strains.

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supporting

confidence: 70%

Evaluation of a novel Bacillus strain from a north‐western Spain hot spring as a source of extracellular thermostable lipase

Deive

Sanromán

Longo

2009

J of Chemical Tech & Biotech

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“…These values are close to the optima reported for Bacillus thermoleovorans ID-1 lipases [4,18], for Bacillus thermocatenulatus lipases [5,18], for the lipase produced by Thermoactinomyces vulgaris [6] and the lipase produced by Bacillus circulans [21].…”

Section: Enzyme Characterisationsupporting

confidence: 87%

“…4). This makes HRKL-1 far more stable than the secreted lipase of Bacillus circulans which exhibited 100 % and 50 % residual activity after 1 h of incubation at 70 C and 85 C, respectively [21]. The lipase produced by Bacillus thermoleovorans ID-1 exhibited 50 % of its original activity after a 30-minute incubation at 70 C [4] and another lipase BTID-A excreted by the same strain retained 75 % of its activity when incubated for 30 minutes at 60 C [18].…”

Section: Enzyme Characterisationmentioning

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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“…A number of publications describe the cloning, expression, purification and biochemical characterization of lipases from Bacillus species ( [9][10][11][12][22][23][24][25][26][27][28][29][30][31][32][33][34][35][36][37][38][39]). More recently, the first 3D structure of a Bacillus lipase was solved [41].…”

Section: Discussionmentioning

confidence: 99%

Biochemical properties and three-dimensional structures of two extracellular lipolytic enzymes from Bacillus subtilis

Eggert

Pouderoyen

Pencreach

et al. 2002

Colloids and Surfaces B: Biointerfaces

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Characterization of a new thermostable esterase from the moderate thermophilic bacterium Bacillus circulans

Cited by 44 publications

References 28 publications

Evaluation of a novel Bacillus strain from a north‐western Spain hot spring as a source of extracellular thermostable lipase

Evaluation of a novel Bacillus strain from a north‐western Spain hot spring as a source of extracellular thermostable lipase

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

Biochemical properties and three-dimensional structures of two extracellular lipolytic enzymes from Bacillus subtilis

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