Effect of support surface chemistry on lipase adsorption and activity

Esters, such as methyl oleate, are functionally important compounds in many industrial sectors, mainly as components for manufacturing of emulsifiers, detergents, intermediate stabilizers and wetting agents. Acid functionalization of multiwalled carbon nanotubes (F-MWCNTs) by using a mixture of HNO 3 and H 2 SO 4 (1:3, v:v) was employed as the matrix for the adsorption of Candida rugosa lipase (CRL) as nanobioconjugates (CRL-MWCNTs) for the production of methyl oleate. Structural information of the developed CRL-MWCNTs was confirmed using Fourier Transform Infrared spectroscopy, thermogravimetric analysis and transmission electron microscopy, which revealed a successful attachment of CRL onto the F-MWCNTs. Process parameters (reaction time, temperature and alcohol:acid molar ratio) were optimized for high percent conversion of methyl oleate. Structural analysis established that CRL was successfully attached to the surface of the F-MWCNTs. Under the optimized conditions, which were 13.87 h, 51 C, molar ratio oleic acid: methanol (1:3.80), a high ester yield of 90.90% was attained. Also, under conditions of the shortest reaction time of 6 h, 47.07 C and acid:methanol ratio of 1:2.54, the CRL-MWCNTs catalysed a 74.51% ester yield. Hence, we established that response surface methodology (RSM) can be a practical technique for the prediction of the conditions that favour the high yield production of methyl oleate. Under optimized conditions, the CRL-MWCNTs nanobioconjugates are potentially good and economical biocatalysts for the production of methyl oleate, as well as other types of commercially important fatty-acid methyl esters.

show abstract

“…The CRL-MWCNTs were lyophilized overnight and stored at 4 C until further use. [23,24] Determination of the protein concentration…”

Section: Immobilization Of Crl Onto F-mwcntsmentioning

confidence: 99%

Modelling and optimization ofCandida rugosananobioconjugates catalysed synthesis of methyl oleate by response surface methodology

Marzuki

Huyop

Aboul‐Enein

et al. 2015

Biotechnology & Biotechnological Equipment

View full text Add to dashboard Cite

show abstract

“…The most relevant are those related to the active phase, i.e. nanoparticles (NPs) size [5][6][7][8] and shape [9][10][11][12], and to the support, mainly pore size [13][14][15][16] and surface chemistry [17][18][19][20], but also the way of catalysts synthesis can affect the activity and/or selectivity [21,22].…”

Section: Introductionmentioning

confidence: 99%

Catalysts based on large size-controlled Pd nanoparticles for aqueous-phase hydrodechlorination

Baeza

Calvo

Rodrı́guez

et al. 2016

Chemical Engineering Journal

View full text Add to dashboard Cite

“…Hydrophobic surfaces tend to promote the interfacial activation of lipases, which is crucial for their catalytic efficiency [10,11,12,13,14]. Nevertheless, Ye and coworkers observed that although the adsorption of lipase onto bare polystyrene (PS), a hydrophobic polymer, was more pronounced than onto hydrophilically modified PS, the activity retention of immobilized lipases was higher on the hydrophilic surfaces [15].…”

Section: Introductionmentioning

confidence: 99%

“…In the present work the immobilization of Candida rugosa lipases onto hydrophilic PS/PEG or hydrophobic PS/PEG/CR particles was investigated by adsorption isotherms, light scattering and zeta-potential ( ζ ) measurements. Although the adsorption of lipases onto hydrophobic surfaces tends to be more favorable than onto hydrophilic supports, the dependence of activity retention on the surface hydrophobicity seems controversial [15]. C. rugosa lipase was chosen because it is one of the most frequently used enzymes in biotechnological processes.…”

Section: Introductionmentioning

confidence: 99%

Catalytic Behavior of Lipase Immobilized onto Congo Red and PEG-Decorated Particles

2014

View full text Add to dashboard Cite

Poly(ethylene glycol) (PEG)-decorated polystyrene (PS) nanoparticles with mean hydrodynamic diameter (D) and zeta-potential (ζ) of (286 ± 15) nm and (−50 ± 5) mV, respectively, were modified by the adsorption of Congo red (CR). The PS/PEG/CR particles presented D and ζ values of (290 ± 19) nm and (−36 ± 5) mV, respectively. The adsorption of lipase onto PS/PEG or PS/PEG/CR particles at (24 ± 1) °C and pH 7 changed the mean D value to (380 ± 20) and (405 ± 11) nm, respectively, and ζ value to (−32 ± 4) mV and (−25 ± 2) mV, respectively. The kinetic parameters of the hydrolysis of p-nitrophenyl butyrate were determined for free lipase, lipase immobilized onto PS/PEG and PS/PEG/CR particles. Lipase on PS/PEG/CR presented the largest Michaelis-Menten constant (K M ), but also the highest V max and k cat values. Moreover, it could be recycled seven times, losing a maximum 10% or 30% of the original enzymatic activity at 40 °C or 25 °C, respectively. Although lipases immobilized onto PS/PEG particles presented the smallest K M values, the reactions were comparatively the slowest and recycling was not possible. Hydrolysis reactions performed in the temperature range of 25 °C to 60 °C with free lipases and lipases immobilized onto PS/PEG/CR particles presented an optimal temperature at 40 °C. At 60 °C free lipases and lipases immobilized onto PS/PEG/CR presented ~80% and ~50% of the activity measured at 40 °C, indicating good thermal stability. Bioconjugation effects between CR and lipase were evidenced by circular dichroism spectroscopy and spectrophotometry. CR molecules mediate the open state conformation of the lipase lid and favor the substrate approaching.

show abstract

Effect of support surface chemistry on lipase adsorption and activity

Cited by 21 publications

References 49 publications

Modelling and optimization ofCandida rugosananobioconjugates catalysed synthesis of methyl oleate by response surface methodology

Modelling and optimization ofCandida rugosananobioconjugates catalysed synthesis of methyl oleate by response surface methodology

Catalysts based on large size-controlled Pd nanoparticles for aqueous-phase hydrodechlorination

Catalytic Behavior of Lipase Immobilized onto Congo Red and PEG-Decorated Particles

Contact Info

Product

Resources

About