Improved esterification activity of Candida rugosa lipase in organic solvent by immobilization as Cross-linked enzyme aggregates (CLEAs)

2011 ◽  
Vol 71 (3-4) ◽  
pp. 85-89 ◽  
Author(s):  
Funda Kartal ◽  
Michiel H.A. Janssen ◽  
Frank Hollmann ◽  
Roger A. Sheldon ◽  
Ali Kılınc
Keyword(s):  
Organic Solvent ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Esterification Activity

scholarly journals Structure and dynamics of Candida rugosa lipase: the role of organic solvent

2004 ◽  
Vol 10 (5-6) ◽  
pp. 358-366 ◽  
Author(s):  
Bimo Ario Tejo ◽  
Abu Bakar Salleh ◽  
Juergen Pleiss
Keyword(s):  
Organic Solvent ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Structure And Dynamics

Esterification Activity and Stability of Candida rugosa Lipase Immobilized into Chitosan

2002 ◽  
pp. 977-986
Author(s):  
Ernandes B. Pereira ◽  
Heizir F. de Castro ◽  
Flávio F. De Moraes ◽  
Gisella M. Zanin
Keyword(s):  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Esterification Activity

scholarly journals Lipase-Catalyzed Chemoselective Ester Hydrolysis of Biomimetically Coupled Aryls for the Synthesis of Unsymmetric Biphenyl Esters

Molecules ◽  
2019 ◽  
Vol 24 (23) ◽  
pp. 4272
Author(s):  
Janna Ehlert ◽  
Jenny Kronemann ◽  
Nadine Zumbrägel ◽  
Matthias Preller
Keyword(s):  
Organic Solvent ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Chemical Transformations ◽  
Reaction Conditions ◽  
Preparative Scale ◽  
Mammalian Origin ◽  
Miehei Lipase ◽  
High Yields ◽  
Rhizopus Niveus

Lipases are among the most frequently used biocatalysts in organic synthesis, allowing numerous environmentally friendly and inexpensive chemical transformations. Here, we present a biomimetic strategy based on iron(III)-catalyzed oxidative coupling and selective ester monohydrolysis using lipases for the synthesis of unsymmetric biphenyl-based esters under mild conditions. The diverse class of biphenyl esters is of pharmaceutical and technical relevance. We explored the potency of a series of nine different lipases of bacterial, fungal, and mammalian origin on their catalytic activities to cleave biphenyl esters, and optimized the reaction conditions, in terms of reaction time, temperature, pH, organic solvent, and water–organic solvent ratios, to improve the chemoselectivity, and hence control the ratio of unsymmetric versus symmetric products. Elevated temperature and increased DMSO content led to an almost exclusive monohydrolysis by the four lipases Candida rugosa lipase (CRL), Mucor miehei lipase (MML), Rhizopus niveus lipase (RNL), and Pseudomonas fluorescens lipase (PFL). The study was complemented by in silico binding predictions to rationalize the observed differences in efficacies of the lipases to convert biphenyl esters. The optimized reaction conditions were transferred to the preparative scale with high yields, underlining the potential of the presented biomimetic approach as an alternative strategy to the commonly used transition metal-based strategies for the synthesis of diverse biphenyl esters.

Application of partially concentrated Candida rugosa lipase in the enzymatic synthesis of geranyl acetate in organic solvent

2017 ◽  
Vol 12 ◽  
pp. 90-95 ◽  
Author(s):  
B.H. Rosa ◽  
G.S. Silva ◽  
G.J.A. Conceição ◽  
R.A. Carvalho ◽  
E. Aguiar-Oliveira ◽  
...  
Keyword(s):  
Organic Solvent ◽  
Enzymatic Synthesis ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Geranyl Acetate

scholarly journals Micro-Aqueous Organic System: A Neglected Model in Computational Lipase Design?

Biomolecules ◽  
2021 ◽  
Vol 11 (6) ◽  
pp. 848
Author(s):  
Shang Wang ◽  
Yan Xu ◽  
Xiao-Wei Yu
Keyword(s):  
Organic Solvent ◽  
Minimum Energy ◽  
Candida Rugosa ◽  
Md Simulations ◽  
Candida Rugosa Lipase ◽  
Organic Media ◽  
Organic System ◽  
System A ◽  
Catalyzed Reactions ◽  
Open States

Water content is an important factor in lipase-catalyzed reactions in organic media but is frequently ignored in the study of lipases by molecular dynamics (MD) simulation. In this study, Candida antarctica lipase B, Candida rugosa lipase and Rhizopus chinensis lipase were used as research models to explore the mechanisms of lipase in micro-aqueous organic solvent (MAOS) media. MD simulations indicated that lipases in MAOS systems showed unique conformations distinguished from those seen in non-aqueous organic solvent systems. The position of water molecules aggregated on the protein surface in MAOS media is the major determinant of the unique conformations of lipases and particularly impacts the distribution of hydrophilic and hydrophobic amino acids on the lipase surface. Additionally, two maxima were observed in the water-lipase radial distribution function in MAOS systems, implying the formation of two water shells around lipase in these systems. The energy landscapes of lipases along solvent accessible areas of catalytic residues and the minimum energy path indicated the dynamic open states of lipases in MAOS systems differ from those in other solvent environments. This study confirmed the necessity of considering the influence of the microenvironment on MD simulations of lipase-catalyzed reactions in organic media.

Esterification activity and stability of Candida rugosa lipase in AOT microemulsion-based organogels

1998 ◽  
Vol 2 (2) ◽  
pp. 121-126 ◽  
Author(s):  
Kazuhito Nagayama ◽  
Katsunori Karaiwa ◽  
Toshifusa Doi ◽  
Masanao Imai
Keyword(s):  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Esterification Activity

Preparation of (S)-2-Phenylpropionic Acid by CaCl2/CMC Nanoparticles Immobilized Candida rugosa Lipase-Catalyzed Hydrolysis in Micro Aqueous Mixed Organic Solvent Systems

2020 ◽  
Vol 20 (3) ◽  
pp. 1899-1906 ◽  
Author(s):  
Xueying Liu ◽  
Dongsheng He ◽  
Xiaojuan Li ◽  
Yan Deng ◽  
Jing Deng ◽  
...  
Keyword(s):  
Organic Solvent ◽  
Candida Rugosa ◽  
Enantiomeric Excess ◽  
Candida Rugosa Lipase ◽  
Methyl Tert Butyl Ether ◽  
Isopropyl Ester ◽  
Butyl Ether ◽  
Lipase Hydrolysis ◽  
Phenylpropionic Acid ◽  
Immobilized Candida Rugosa Lipase

Candida rugosa lipase was immobilized in this study using CaCl2/CMC nanoparticles that yielded a lipase loading capacity of 127 mg/g, with better thermal stability and activity of 91.8%. The hydrolysis of racemic 2-phenylpropionic acid isopropyl ester by free and immobilized Candida rugosa lipase was investigated in the mixed organic-solvent composed of isooctane and methyl tert-butyl ether (9.5:0.5, V/V). The optimal conditions were 35 °C and pH 7.5 for free Candida rugosa lipase hydrolysis. We obtained (S)-2-phenylpropionic acid with 44.85% conversion, 95.75% enantiomeric excess and enantiomeric ratio of 112. The CaCl2/CMC nanoparticles immobilized Candida rugosa lipase possesses high enantioselectivity, with E = 237 at 40 °C and pH 7.5. It was efficiently reusable in four cycles and appropriately enhanced enantioselectivity within 120–240.

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