Immobilization of Serratia marcescens lipase onto amino-functionalized magnetic nanoparticles for repeated use in enzymatic synthesis of Diltiazem intermediate

Hu, Bin; Pan, Jiang; Yu, Hui‐Lei; Liu, Jianwen; Xu, Jian‐He

doi:10.1016/j.procbio.2009.05.001

Cited by 145 publications

(58 citation statements)

References 26 publications

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“…Thus the enzyme was not thermostable and similar findings have also be found for Aspergillus niger, Serratia marcescens and Bacillus cereus lipases [30,38,39]. We conclude that our crude extracellular yeast lipase has the optimum activity at mild reaction conditions and has the potential to be useful in organic solvents and detergents …”

Section: Thermal Stabilitysupporting

confidence: 80%

Properties of an extracellular lipase from a traditional yoghurt yeast

Akkaya

Yenidünya

2012

Turk J Bioch

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Purpose: To produce an organic solvent tolerant extracellular lipase from a traditional yoghurt Saccharomyces cerevisiae isolate and to characterize this enzyme activity. Material and Methods: A traditional yoghurt sample collected from a farm (Sivas-Turkey) was diluted and mixed with de Man, Rogosa and Sharp Medium (MRS) and poured into Petri dishes. One hundred colonies were selected and transferred onto MRS agar plates including Tween 80 as a lipase substrate. Only four colonies with lipase activity were incubated in MRS broth for 3 days at 37 o C and the extracellular proteins were precipitated with ethanol (95%v/v) from the supernatant. The precipitate with the highest lipase activity was selected for further analysis. Results: The optimum pH and temperature were 7.0 and 37 o C, respectively. While (1 mM) Mn 2+ caused a slight increase (~8%) Hg 2+ or Zn 2+ caused a substantial activity loss (~70%). Organic solvents (5%chloroform or n-butanol, v/v) increased activity ~2.5 fold. Five percent SDS or Triton X-100 increased activity by 8%and 14%, respectively. The enzyme could hydrolyse hydroxyethyl methacrylate (HEMA) and 2,3-epoxy propyl methacrylate (GMA),retained ~83%of its activity after 1 hour at 37 o C, lost no activity when stored at pH 7.0 and at 4 degree C for 60 days. Conclusion:The properties of the extracellular yeast lipase was investigated using a number of physiological parameters. The results obtained indicated that it was an organic solvent-and detergent tolerant enzyme having the optimum activity at mild reaction conditions. Key Words: Detergent tolerance, lipase activity, organic solvent tolerance, traditional yoghurt, yeast lipase. Conflict of interest:The authors do not have a conflict of interest. o C'dir. Mn +2 iyonu enzmi aktivitesini artırırken (%8), Zn +2 and Hg +2 iyonları aktiviteyi azaltmaktadır (~%70). %5 kloroform ve n-butanol varlığında enzim aktivitesinde ~2.5 kat artış gözlendi. Enzim aynı zamanda SDS (%108 relativ aktivite) ve Triton X-100 (%114 relativ aktivite) gibi deterjanlarda kararlılığını korudu. Enzim, hidroksietil metakrilat (HEMA) ve 2,3-epoksi propil metakrilatı (GMA) da substrat olarak kullandı. Enzim bir saat süreyle, 37 o C'de bekletildiğinde, aktivitesini %83'ün üzerinde koruduğu gözlendi. Enzim pH 7.0 fosfat tamponunda 60 gün boyunca aktivitesini kaybetmeden buzdolabında saklanabildi. Sonuç: Eksrtraselüler maya lipazının özellikleri farklı fizyolojik parametreler kullanılarak incelendi. Elde edilen bulgulara göre bu enzim ılımlı tepkime koşullarında çalışan organik çözücü ve deterjan tolerant enzimdir. Anahtar Kelimeler: Deterjan tolerant, geleneksel yoğurt, lipaz aktivitesi, organik solvent tolerans, maya lipazı. Çıkar çatışması: Yazarlarların çıkar çatışması bulunmamaktadır.

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Section: Thermal Stabilitysupporting

confidence: 80%

Properties of an extracellular lipase from a traditional yoghurt yeast

Akkaya

Yenidünya

2012

Turk J Bioch

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“…A high concentration of aldehyde groups on the support surface may cause many multi-point covalent enzyme-support bonds, so as to obtain rigidity in the structure of the enzyme, favoring a high stability and a high intrinsic activity of the derivative (Betancor, et al, 2006). Hu et al (2009) reported that Serratia marcescens lipase was almost fully immobilized onto aldehydefuncionalized-APTES magnetic nanoparticles within 10 min. Contact times up to 120 minutes did not show any significant change in the lipase immobilization, in agreement with those presented in this work.…”

Section: Effect Of the Contact Timementioning

confidence: 99%

“…The half-life of derivatives was found to be 1-3.3 h, with the immobilized enzyme being 12-33 times more stable than the soluble form. Hu et al (2009) studied the effect of temperature on free and immobilized lipase (on aldehyde-functionalized magnetic Fe3O4 nanoparticles). The maximum activities of free and immobilized lipase were observed at 50 °C and 45 °C, respectively, but the immobilized lipase was more stable at higher temperatures (between 45 °C and 55 °C), in agreement with the data obtained in this work.…”

Section: Thermal Stabilities Of Soluble and Immobilized Calbmentioning

confidence: 99%

NANOBIOCATALYTIC SYSTEMS BASED ON LIPASE-Fe3O4 AND CONVENTIONAL SYSTEMS FOR ISONIAZID SYNTHESIS: A COMPARATIVE STUDY

Costa

Souza

Fechine

et al. 2016

Braz. J. Chem. Eng.

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-Superparamagnetic nanomaterials have attracted interest in many areas due to the high saturation magnetization and surface area. For enzyme immobilization, these properties favor the enzyme-support contact during the immobilization reaction and easy separation from the reaction mixture by use of low-cost magnetic processes. Iron oxide magnetic nanoparticles (Fe3O4, MNPs), produced by the co-precipitation method, functionalized with 3-aminopropyltriethoxysilane (APTES) and glutaraldehyde (GLU), were evaluated as a solid support for Candida antarctica lipase B (CALB) immobilization. The nanomagnetic derivative (11nm) obtained after CALB immobilization (MNPs/APTES/GLU/CALB) was evaluated as biocatalyst in isoniazide (INH) synthesis using ethyl isonicotinate (INE) and hydrazine hydrate (HID) as substrates, in 1,4-dioxane. The results showed that MNPs/APTES/CALB had a similar performance when compared to a commercial enzyme Novozym 435, showing significant advantages over other biocatalysts, such as Rhizhomucor miehei lipase (RML) and CALB immobilized on non-conventional, low-cost, chitosan-based supports.

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“…The immobilization efficiency of the lipase was calculated according to the following equation [12],…”

Section: Lipase Immobilizationmentioning

confidence: 99%

Lipase NS81006 immobilized on Fe₃O₄ magnetic nanoparticles for biodiesel production

Thangaraj

Jia

Dai

et al. 2016

Ovidius University Annals of Chemistry

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Abstract. Lipase-catalyzed biodiesel production is being the object of extensive research due to the demerits of chemical based catalytic system. Lipase immobilized on Fe3O4 magnetic nanoparticles has the integrated advantages of traditional immobilized lipase and free lipase for its rather fast reaction rate and easy separation. It has been demonstrated that free lipase NS81006 has potential in catalyzing the alcoholysis of renewable oils for biodiesel preparation. In this study, Fe3O4 magnetic nanoparticles functionalized with organosilane compounds like (3-aminopropyl)triethyloxysilane (APTES) and (3-mercaptopropyl)trimethoxysilane) MPTMS were used as carriers for lipase immobilization. Lipase NS81006 was covalently bound to the organosilane-functionalized magnetic nanoparticles by using glutaraldehyde cross-linking reagent. A biodiesel yield of 89% and 81% could be achieved by lipase immobilized on APTES-Fe3O4 and MPTMS-Fe3O4 magnetic nanoparticles respectively under optimized conditions of oil to methanol molar ratio 1:3 with three step addition of methanol, reaction temperature 45°C and reaction time duration 12 h. The lipases immobilized on magnetic nanoparticles could be recovered easily by external magnetic field for further use.

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Immobilization of Serratia marcescens lipase onto amino-functionalized magnetic nanoparticles for repeated use in enzymatic synthesis of Diltiazem intermediate

Cited by 145 publications

References 26 publications

Properties of an extracellular lipase from a traditional yoghurt yeast

Properties of an extracellular lipase from a traditional yoghurt yeast

NANOBIOCATALYTIC SYSTEMS BASED ON LIPASE-Fe3O4 AND CONVENTIONAL SYSTEMS FOR ISONIAZID SYNTHESIS: A COMPARATIVE STUDY

Lipase NS81006 immobilized on Fe₃O₄ magnetic nanoparticles for biodiesel production

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Immobilization of Serratia marcescens lipase onto amino-functionalized magnetic nanoparticles for repeated use in enzymatic synthesis of Diltiazem intermediate

Cited by 145 publications

References 26 publications

Properties of an extracellular lipase from a traditional yoghurt yeast

Properties of an extracellular lipase from a traditional yoghurt yeast

NANOBIOCATALYTIC SYSTEMS BASED ON LIPASE-Fe3O4 AND CONVENTIONAL SYSTEMS FOR ISONIAZID SYNTHESIS: A COMPARATIVE STUDY

Lipase NS81006 immobilized on Fe3O4 magnetic nanoparticles for biodiesel production

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Product

Resources

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Lipase NS81006 immobilized on Fe₃O₄ magnetic nanoparticles for biodiesel production