Immobilized Lecitase Ultra‑catalyzed Preparation of l‑α-glycerylphosphorylcholine from Soy Phosphatidylcholine

2021 ◽  
Author(s):  
Byung Hee Kim ◽  
In-Hwan Kim ◽  
Yejin Song ◽  
Seoye Roh ◽  
Jihyun Hwang ◽  
...  
Keyword(s):  
Lecitase Ultra

A Comprehensive Study on the Activity and Deactivation of Immobilized Lecitase Ultra in Esterifications of Food Waste Streams to Monoacylglycerols

ChemSusChem ◽  
2013 ◽  
Vol 6 (5) ◽  
pp. 872-879 ◽  
Author(s):  
Karen M. Gonçalves ◽  
Felipe K. Sutili ◽  
Ivaldo I. Júnior ◽  
Marcella C. Flores ◽  
Leandro Soter de Mariz e Miranda ◽  
...  
Keyword(s):  
Food Waste ◽  
Waste Streams ◽  
Lecitase Ultra ◽  
Comprehensive Study

Emulsifying Properties of Lecithin Containing Different Fatty Acids Obtained by Immobilized Lecitase Ultra-Catalyzed Reaction

2013 ◽  
Vol 91 (4) ◽  
pp. 579-590 ◽  
Author(s):  
Lu-Jing Gan ◽  
Xiang-Yu Wang ◽  
Dan Yang ◽  
Hua Zhang ◽  
Jung-Ah Shin ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Emulsifying Properties ◽  
Lecitase Ultra

scholarly journals Multi-Combilipases: Co-Immobilizing Lipases with Very Different Stabilities Combining Immobilization via Interfacial Activation and Ion Exchange. The Reuse of the Most Stable Co-Immobilized Enzymes after Inactivation of the Least Stable Ones

Catalysts ◽  
2020 ◽  
Vol 10 (10) ◽  
pp. 1207
Author(s):  
Sara Arana-Peña ◽  
Diego Carballares ◽  
Vicente Cortés Corberan ◽  
Roberto Fernandez-Lafuente
Keyword(s):  
Ammonium Sulfate ◽  
Rhizomucor Miehei ◽  
Immobilized Enzymes ◽  
The Other ◽  
Thermomyces Lanuginosus ◽  
Vinyl Sulfone ◽  
Interfacial Activation ◽  
Agarose Beads ◽  
Immobilized Biocatalyst ◽  
Lecitase Ultra

The lipases A and B from Candida antarctica (CALA and CALB), Thermomyces lanuginosus (TLL) or Rhizomucor miehei (RML), and the commercial and artificial phospholipase Lecitase ultra (LEU) may be co-immobilized on octyl agarose beads. However, LEU and RML became almost fully inactivated under conditions where CALA, CALB and TLL retained full activity. This means that, to have a five components co-immobilized combi-lipase, we should discard 3 fully active and immobilized enzymes when the other two enzymes are inactivated. To solve this situation, CALA, CALB and TLL have been co-immobilized on octyl-vinyl sulfone agarose beads, coated with polyethylenimine (PEI) and the least stable enzymes, RML and LEU have been co-immobilized over these immobilized enzymes. The coating with PEI is even favorable for the activity of the immobilized enzymes. It was checked that RML and LEU could be released from the enzyme-PEI coated biocatalyst, although this also produced some release of the PEI. That way, a protocol was developed to co-immobilize the five enzymes, in a way that the most stable could be reused after the inactivation of the least stable ones. After RML and LEU inactivation, the combi-biocatalysts were incubated in 0.5 M of ammonium sulfate to release the inactivated enzymes, incubated again with PEI and a new RML and LEU batch could be immobilized, maintaining the activity of the three most stable enzymes for at least five cycles of incubation at pH 7.0 and 60 °C for 3 h, incubation on ammonium sulfate, incubation in PEI and co-immobilization of new enzymes. The effect of the order of co-immobilization of the different enzymes on the co-immobilized biocatalyst activity was also investigated using different substrates, finding that when the most active enzyme versus one substrate was immobilized first (nearer to the surface of the particle), the activity was higher than when this enzyme was co-immobilized last (nearer to the particle core).

USO DE POLÍMEROS IÔNICOS PARA ESTABILIZAR ESTRUTURAS HIPERATIVADAS DE LECITASE ULTRA

2015 ◽  
Author(s):  
José Cleiton Sousa dos Santos ◽  
Roberto Fernandez-LaFuente ◽  
Luciana Rocha Barros Gonçalves
Keyword(s):  
Lecitase Ultra

Preparation of Diacylglycerol-Enriched Oil from Free Fatty Acids Using Lecitase Ultra-Catalyzed Esterification

2011 ◽  
Vol 88 (10) ◽  
pp. 1557-1565 ◽  
Author(s):  
Lili Wang ◽  
Yong Wang ◽  
Changying Hu ◽  
Qian Cao ◽  
Xiaohui Yang ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Free Fatty Acids ◽  
Lecitase Ultra

scholarly journals Reuse of Lipase from Pseudomonas fluorescens via Its Step-by-Step Coimmobilization on Glyoxyl-Octyl Agarose Beads with Least Stable Lipases

Catalysts ◽  
2019 ◽  
Vol 9 (5) ◽  
pp. 487 ◽  
Author(s):  
Nathalia Rios ◽  
Sara Arana-Peña ◽  
Carmen Mendez-Sanchez ◽  
Claudia Ortiz ◽  
Luciana Gonçalves ◽  
...  
Keyword(s):  
Pseudomonas Fluorescens ◽  
Rhizomucor Miehei ◽  
The Other ◽  
Initial Activity ◽  
Interfacial Activation ◽  
Full Activity ◽  
Agarose Beads ◽  
Lecitase Ultra ◽  
The Stability ◽  
Triton X

Coimmobilization of lipases may be interesting in many uses, but this means that the stability of the least stable enzyme determines the stability of the full combilipase. Here, we propose a strategy that permits the reuse the most stable enzyme. Lecitase Ultra (LU) (a phospholipase) and the lipases from Rhizomucor miehei (RML) and from Pseudomonas fluorescens (PFL) were immobilized on octyl agarose, and their stabilities were studied under a broad range of conditions. Immobilized PFL was found to be the most stable enzyme under all condition ranges studied. Furthermore, in many cases it maintained full activity, while the other enzymes lost more than 50% of their initial activity. To coimmobilize these enzymes without discarding fully active PFL when LU or RML had been inactivated, PFL was covalently immobilized on glyoxyl-agarose beads. After biocatalysts reduction, the other enzyme was coimmobilized just by interfacial activation. After checking that glyoxyl-octyl-PFL was stable in 4% Triton X-100, the biocatalysts of PFL coimmobilized with LU or RML were submitted to inactivation under different conditions. Then, the inactivated least stable coimmobilized enzyme was desorbed (using 4% detergent) and a new enzyme reloading (using in some instances RML and in some others employing LU) was performed. The initial activity of immobilized PFL was maintained intact for several of these cycles. This shows the great potential of this lipase coimmobilization strategy.

Prolongation of secondary drying step of phospholipid lyophilization greatly improves acidolysis reactions catalyzed by immobilized lecitase ultra

2020 ◽  
Vol 132 ◽  
pp. 109388 ◽  
Author(s):  
Carlos M. Verdasco-Martín ◽  
Carlos Corchado-Lopo ◽  
Roberto Fernández-Lafuente ◽  
Cristina Otero
Keyword(s):  
Secondary Drying ◽  
Lecitase Ultra

Use of Lecitase-Ultra immobilized on styrene-divinylbenzene beads as catalyst of esterification reactions: Effects of ultrasounds

2015 ◽  
Vol 255 ◽  
pp. 27-32 ◽  
Author(s):  
Joana S. Alves ◽  
Cristina Garcia-Galan ◽  
Daiane Danelli ◽  
Natália Paludo ◽  
Oveimar Barbosa ◽  
...  
Keyword(s):  
Styrene Divinylbenzene ◽  
Lecitase Ultra ◽  
Esterification Reactions

scholarly journals Stabilization of Lecitase Ultra® by Immobilization and Fixation of Bimolecular Aggregates. Release of Omega-3 Fatty Acids by Enzymatic Hydrolysis of Krill Oil

Catalysts ◽  
2021 ◽  
Vol 11 (9) ◽  
pp. 1067
Author(s):  
Daniel Andrés-Sanz ◽  
Cristina Fresan ◽  
Gloria Fernández-Lorente ◽  
Javier Rocha-Martín ◽  
Jose M. Guisán
Keyword(s):  
Covalent Immobilization ◽  
Omega 3 Fatty Acids ◽  
Krill Oil ◽  
Omega 3 ◽  
Open Structures ◽  
Lecitase Ultra ◽  
Support Surfaces ◽  
Hydrophobic Supports ◽  
Hydrolysis Of ◽  
Derivatives Of

Lecitase Ultra® solutions are mainly composed of bimolecular aggregates of two open structures of the enzyme. The immobilization and fixation of these bimolecular aggregates onto support surfaces is here proposed as a novel protocol for the immobilization and stabilization of Lecitase. The resulting derivatives of Lecitase aggregates were much more stable than the diluted solutions of the enzyme. The most stable of them was obtained by covalent immobilization of the bimolecular aggregate: 300-fold more stable than the diluted enzyme and 75-fold more stable than open Lecitase adsorbed onto hydrophobic supports. The bimolecular aggregate that adsorbed onto polyethyleneimine-agarose exhibited the best combination of activity and stability for the hydrolysis of krill oil. Omega-3 acids are in the sn-2 position of the krill oil, but they are also released by a phospholipase A1 because of migration issues.

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