Lipase activity of thermophilic bacteria from icelandic hot springs

Sigurgísladóttir, Sjöfn; Konráòsdóttir, Malta; Jónsson, Ásbjörn; Kristjánsson, Jakob K.; Matthiasson, Einar

doi:10.1007/bf00128277

Cited by 90 publications

(34 citation statements)

References 10 publications

(14 reference statements)

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“…The activity of lipase N435 used in the enzymatic prepolymerization step was determined according to the method of Sigurgisladottir et al 35 with slight modifications. Lipase activity was assayed using 9.33 mM p-nitrophenol-palmitate in 50 mM phosphate buffer (pH 7) containing 6.8 mM of TritonX and 0.11% (w/v) gum Arabic.…”

Section: Assay Of Lipase Activitymentioning

confidence: 99%

Production of biodegradable polyesters via enzymatic polymerization and solid state finishing

Kanelli

Douka

Vouyiouka

et al. 2014

J of Applied Polymer Sci

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The synthesis of aliphatic polyesters (PEs) derived from diols (1,4-butanediol and 1,8-octanediol) and diacids or their derivatives (diethyl succinate, sebacic acid, 1,12-dodecanedioic acid, and 1,14-tetradecanedioic acid) was achieved in order to produce poly(butylene succinate) (PE 4.4), poly(octylene sebacate) (PE 8.10), poly(octylene dodecanate) (PE 8.12), and poly(octylene tetradecanate) (PE 8.14). The herein suggested procedure involved two stages, both sustainable and in accordance with the principles of "green" polymerization. The first comprised an enzymatic prepolymerization under vacuum, in the presence of diphenylether as solvent using Candida antarctica lipase B as biocatalyst, whereas a low-temperature postpolymerization step [solid state polymerization (SSP)] followed in order to upgrade the PEs quality. In the enzymatically synthesized prepolymers, the range of number-average molecular weight attained was from 3700 to 8000 g/mol with yields reaching even 97%. Subsequently, SSP of PE 4.4 and 8.12 took place under vacuum or flowing nitrogen and lasted 10-48 h, at temperatures close to the prepolymer melting point (T m 2 T SSP varied between 4 C and 14 C). The solid state finishing led to increase in the molecular weight depending on the prepolymer type, and it also contributed to improvement of the physical characteristics and the thermal properties of the enzymatically synthesized PEs.

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Section: Assay Of Lipase Activitymentioning

confidence: 99%

Production of biodegradable polyesters via enzymatic polymerization and solid state finishing

Kanelli

Douka

Vouyiouka

et al. 2014

J of Applied Polymer Sci

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“…Lipolytic activity assays Lipolytic activity was routinely determined spectrophotometrically using 2.5 mmol dm −3 p-nitrophenyl laurate as substrate, 14 at pH 8.0, 55…”

Section: Cell Growth Determinationmentioning

confidence: 99%

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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“…The activity of free and immobilized lipase was determined according to the method of Sigurgisladottir et al with slight modification using 0.5 g of p-nitrophenyl palmitate (p-NPP) dissolved in 100 mL of ethanol as substrate 29 . The increase in absorbance at 410 nm caused by the release of p-nitrophenol in the hydrolysis of p-NPP was measured spectrophotometrically.…”

Section: Activity Assay Of Free and Immobilized Lipasementioning

confidence: 99%

Methacrylated Chitosan Based UV Curable Support for Enzyme Immobilization

Bayramoğlu

2017

Mat. Res.

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UV curing is simple, fast and effective procedure for enzyme immobilization with minimized enzymatic activity. UV-curable methacrylated chitosan is here proposed as a support material for immobilization of lipase. The morphology of the polymeric support was characterized by scanning electron microscopy (SEM). Both covalently (CIL) and physically (PIL) immobilized enzyme is analyzed in terms of enzymatic activity as a function of reusability, pH, storage, as well as stability under various experimental conditions. The recovery of activity of lipases immobilized onto a photocrosslinked polymer network was 82.0% and 70.0% for CIL and PIL, respectively. The optimum pH value for the free lipase was at pH 6.0. The optimum pH of the both CIL and PIL was shifted to pH 7.0. Immobilization increased the thermostability of the lipase from 50 ºC to 62 ºC. The free enzyme lost all its activity within 15 days. Repeated batch experiments show that about 61% of the enzyme activity of CIL and 41% of PIL was retained after 8 cycles.

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Lipase activity of thermophilic bacteria from icelandic hot springs

Cited by 90 publications

References 10 publications

Production of biodegradable polyesters via enzymatic polymerization and solid state finishing

Production of biodegradable polyesters via enzymatic polymerization and solid state finishing

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

Methacrylated Chitosan Based UV Curable Support for Enzyme Immobilization

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