A serine protease triad forms the catalytic centre of a triacylglycerol lipase

Brady, Leo; Brzozowski, A.M.; Derewenda, Zygmunt S.; Dodson, E.J.; Dodson, Guy; Tolley, Shirley P.; Turkenburg, J.P.; Christiansen, Lars; Huge-Jensen, Birgitte; Nørskov, Leif; Thim, Lars; Menge, Ulrich

doi:10.1038/343767a0

Cited by 1,187 publications

(612 citation statements)

References 20 publications

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“…The "open state" conformation would render the active site with a deformed structure more susceptible to the external environment, attributed to the loss of the shield provided by the lid in the "close state". 9 In brief, the above discussion clarifies a correlation between the support hydrophobicity and the thermal stability of the immobilized PCL. The support with MHM is preferable for an improvement in PCL thermal stability.…”

Section: Resultsmentioning

confidence: 90%

Improved Catalytic Performance of Lipase Accommodated in the Mesoporous Silicas with Polymer-Modified Microenvironment

et al. 2012

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The highly ordered mesoporous silicas with elaborately controlled microenvironment were synthesized via covalent incorporation of long-chain polymers (M w = 2000 g mol −1 ) bearing specific hydrophilic/hydrophobic balance. The microenvironment (hydrophilicity/hydrophobicity) of the mesoporous silicas was quantitatively determined by gas adsorption experiments and investigated by lysozyme (LYZ) adsorption. The relative activity of lipase from Pseudomonas cepacia (PCL) encapsulated in the mesoporous silica with moderate hydrophobic microenvironment (hereafter denoted as MHM) reaches up to 281% compared with the free PCL, notably higher than that of PCL accommodated in the mesoporous silicas with hydrophilic or strong hydrophobic microenvironment (20.7−26.2% relative to the free PCL). Moreover, PCL entrapped in the nanochannels with MHM affords the highest initial rate in the kinetic resolution of (R,S)-1-phenylethanol relative to other immobilized PCL. The above results suggest that the MHM could render the active center of PCL entirely exposed to the substrates without interrupting its native conformation in the "interfacial activation". In addition, the nanochannels with MHM could markedly improve the thermal stability of PCL (preserving nearly 60% of the initial activity after the incubation at 70°C for 2 h) and facilitate the recycling of the immobilized PCL in both aqueous and organic media. Our work demonstrates that the subtle modulation of the microenvironment of mesoporous silicas for enzyme immobilization designates a very promising strategy to fabricate the highly active and stable heterogeneous biocatalysts for industrial application.

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Section: Resultsmentioning

confidence: 90%

Improved Catalytic Performance of Lipase Accommodated in the Mesoporous Silicas with Polymer-Modified Microenvironment

et al. 2012

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“…No active enzyme was thought to occur in solution. Recent X-ray structure analyses of native and inhibitor -complexed Rhizomucor miehi lipase have revealed that a short peptide segment covering the active site in the absence of the substrate move in complexed enzyme so that the active site is exposed to the solvent [45,46]. Concomitantly the hydrophobicity of the surface area around the active site increases, which should contribute to the strong binding of the enzyme to the interface.…”

Section: Characterization Of Lipase From Aspergillus Niger Nrrl3mentioning

confidence: 99%

Extracellular lipase of Aspergillus niger NRRL3; production, partial purification and properties

Adham

Ahmed

2009

Indian J Microbiol

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Four strains of Aspergillus niger were screened for lipase production. Each was cultivated on four different media differing in their contents of mineral components and sources of carbon and nitrogen. Aspergillus niger NRRL3 produced maximal activity (325U/ml) when grown in 3% peptone , 0.05% MgSO 4 .7H 2 O, 0.05% KCl, 0.2% K 2 HPO 4 and 1% olive oil:glucose (0.5:0.5). A. niger NRRL3 lipase was partially purifi ed by ammonium sulphate precipitation. The majority of lipase activity (48%) was located in fraction IV precipitated at 50-60% of saturation with a 18-fold enzyme purifi cation. The optimal pH of the partial purifi ed lipase preparation for the hydrolysis of emulsifi ed olive oil was 7.2 and the optimum temperature was 60°C. At 70°C, the enzyme retained more than 90% of its activity. Enzyme activity was inhibited by Hg 2+ and K + , whereas Ca 2+ and Mn 2+ greatly stimulated its activity. Additionally, the formed lipase was stored for one month without any loss in the activity.

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“…The same results were obtained with respect to Mucor miehei lipase. 14 ) Ester bonds of long and middle chain fatty acids (C s " CIS) were hydrolyzed by the lipase but the ester bond of a short chain fatty acid (C 4 ) resisted cleavage by the enzyme's lipolysis (Fig. 3).…”

Section: Enzymic Properties Of Lipasementioning

confidence: 99%

Purification and Some Characteristics of Extracellular Lipase fromFusarium oxysporumf. sp.lini

Hashizume

Sasaki

Watanabe

et al. 1992

Bioscience, Biotechnology, and Biochemistry

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A serine protease triad forms the catalytic centre of a triacylglycerol lipase

Cited by 1,187 publications

References 20 publications

Improved Catalytic Performance of Lipase Accommodated in the Mesoporous Silicas with Polymer-Modified Microenvironment

Improved Catalytic Performance of Lipase Accommodated in the Mesoporous Silicas with Polymer-Modified Microenvironment

Extracellular lipase of Aspergillus niger NRRL3; production, partial purification and properties

Purification and Some Characteristics of Extracellular Lipase fromFusarium oxysporumf. sp.lini

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