Candida rugosa lipase immobilization on magnetic silica aerogel nanodispersion

RSC Advances ◽  
2016 ◽  
Vol 6 (15) ◽  
pp. 12676-12687 ◽  
Author(s):  
Leila Amirkhani ◽  
Jafarsadegh Moghaddas ◽  
Hoda Jafarizadeh-Malmiri
Keyword(s):  
Silica Aerogel ◽  
Physical Adsorption ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Lipase Immobilization ◽  
Magnetic Silica

C. rugosalipase was successfully immobilized on hydrophobic magnetic silica aerogel nanodispersion by simple physical adsorption.

scholarly journals Preparation and Candida rugosa Lipase Immobilization on Nylon-6 Grafted and Aminated (Polyvinyl Benzyl Chloride) Microfibers

2019 ◽  
Vol 14 (2) ◽  
pp. 369
Author(s):  
Nur Iilani Abd Halin ◽  
Maan Fahmi Rashid Al-Khatib ◽  
Hamzah Mohd. Salleh ◽  
Mohamed Mahmoud Nasef
Keyword(s):  
Benzyl Chloride ◽  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Nylon 6 ◽  
Covalent Attachment ◽  
Effect Of Temperature ◽  
P Value ◽  
Lipase Immobilization ◽  
The Stability

This paper demonstrates a simplified procedure for the preparation of a nylon-6 microfibers based support for the immobilization of Candida rugosa lipase via covalent attachment to enhance the stability and reusability of lipase. The preparation of the support was done by radiation induced graft copolymerization (RIGC) of vinyl benzyl chloride (VBC) onto nylon-6 microfibers followed by amination with ethanolamine to facilitate the immobilization of lipase. Fourier transfer infra red (FTIR) and scanning electron microscope (SEM) were used to study the chemical and physical changes following grafting, amination and immobilization. Response surface methodology (RSM) was applied for the optimization of lipase immobilization on the aminated microfibers. The optimization parameters were incubation time, pH, and lipase concentration. Moreover, this study investigated the effect of temperature, pH, and storage stability and reusability on the lipase in its immobilized and free forms. The developed model from RSM showed an R2 value of 0.9823 and P-value < 0.001 indicating that the model is significant. The optimum temperatures for both immobilized and free lipases were 45 °C, whereas the best pH values for lipase activity were at pH 8 and pH 7, respectively. This study also identifies values for KM and Vmax for both immobilized and free lipase accordingly. Based on the results, immobilized lipase had significantly improved the stability and reusability of lipase compared to that in free forms. Copyright © 2019 BCREC Group. All rights reserved 

scholarly journals Activity and stability of immobilized Candida rugosa lipase on chitosan coated Fe3O4 nanoparticles in aqueous and organic media

2014 ◽  
Vol 10 (3) ◽  
pp. 2478-2483 ◽  
Author(s):  
Mohamed A. Abd-Elhakeem ◽  
Ahmed M. Elsayed ◽  
Taher A. Alkhulaqi
Keyword(s):  
Storage Stability ◽  
Immobilized Enzyme ◽  
Candida Rugosa ◽  
Chitosan Nanoparticles ◽  
Candida Rugosa Lipase ◽  
Initial Activity ◽  
Lipase Immobilization ◽  
Lipase Enzyme ◽  
Immobilized Candida Rugosa Lipase ◽  
And Storage

Fe3O4 (magnetite) nanoparticles were prepared by coprecipitation method, coated by chitosan and functionalized by glutaraldehyde. Lipase enzyme from Candida rugosa was immobilized on the prepared particles via cross linking reaction. Synthesis steps and characterization were examined by XRD, TEM, and FTIR.  The immobilization conditions were 10 mL of phosphate buffer (0.1 M, pH 6.5) containing 30 mg of  functionalized magnetic chitosan nanoparticles and 2.0 mg·mL-1 of lipase, immobilization temperature of 4 ℃ and immobilization time of 1 h. Under these conditions, lipase was successfully immobilized with loading capacity of 87 mg/g. The immobilized enzyme showed good operational and storage stability, where it remained stable after 30 days of storage at 4◦C.and retained about 61% of its initial activity after twenty repeated uses. Finally enzymatic catalyze synthesis of butyl and hexyl oleate at 40 ◦C with shaking (200 rpm) was realized in n-hexane and confirmed by GC analysis.

scholarly journals Activated Carbon as Support for Lipase Immobilization

2007 ◽  
Vol 5 (2) ◽  
pp. 115
Author(s):  
Mohd Basyaruddin Abdul Rahman ◽  
Mahiran Basri, Mohd Zobir Hussein ◽  
Raja Nor Zaliha Raja Abdul Rahman ◽  
Yau Kim Yan ◽  
Abu Bakar Salleh
Keyword(s):  
Activated Carbon ◽  
Room Temperature ◽  
Storage Stability ◽  
Physical Adsorption ◽  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Lipase Immobilization ◽  
Immobilized Lipases ◽  
Different Types ◽  
Native Lipase

Lipase from<em> Candida rugosa</em> was immobilized onto four different types of activated carbon; KI/2030, KI/3040, KI/5060 and KI/6070. The immobilized lipase was used in the esterification of oleic acid and 1-butanol in hexane. The effects of difference pore sizes, surface area, reaction temperature, thermostability of the immobilized lipases, storage stability in organic solvent and leaching studies were investigated. Among the four samples, KI/6070 gave the highest activities and stability in all the parameters investigated. Immobilized lipases generally exhibit activities higher than the native lipase for the parameters studied, with optimum temperature of 40°C. Immobilized lipases are more stable than native lipase in hexane at room temperature up to 12 days. Leaching study proved that the immobilization of lipase using physical adsorption is cheap and easy. This method was found to be suitable for the attachment of enzyme on the support.

Efficient Candida rugosa lipase immobilization on Maghnite clay and application for the production of (1R)-(−)-Menthyl acetate

2016 ◽  
Vol 71 (4) ◽  
pp. 785-793 ◽  
Author(s):  
Fatiha Benamia ◽  
Sabrina Benouis ◽  
Abderahmane Belafriekh ◽  
Noura Semache ◽  
Nacer Rebbani ◽  
...  
Keyword(s):  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Lipase Immobilization

Candida rugosa lipase immobilization on hydrophilic charged gold nanoparticles as promising biocatalysts: Activity and stability investigations

2015 ◽  
Vol 131 ◽  
pp. 93-101 ◽  
Author(s):  
Iole Venditti ◽  
Cleofe Palocci ◽  
Laura Chronopoulou ◽  
Ilaria Fratoddi ◽  
Laura Fontana ◽  
...  
Keyword(s):  
Gold Nanoparticles ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Lipase Immobilization

scholarly journals Evaluation of magnetic carriers employed for immobilization of lipase from candida rugosa

2020 ◽  
Vol 6 (4) ◽  
pp. 0498-0504
Author(s):  
Otávio Domingues ◽  
Letícia Karen dos Santos ◽  
Rondinelli Donizetti Herculano ◽  
Danilo Luiz Flumignan ◽  
Ariela Veloso de Paula
Keyword(s):  
Magnetic Nanoparticles ◽  
Physical Adsorption ◽  
Candida Rugosa ◽  
Reaction Medium ◽  
Covalent Bond ◽  
Hydrolytic Activity ◽  
Candida Rugosa Lipase ◽  
Activity Analysis ◽  
Industrial Processes ◽  
Magnetic Carriers

Currently, the use of magnetic nanoparticles has aroused interest in industrial processes, and the combination of their properties with the immobilization of lipases has been developed in order to produce carriers of easy separation of the reaction medium. In this context, the objective of the present study was to immobilize Candida rugosa lipase in magnetic nanoparticles, such as magnetite and maghemite, by physical adsorption and covalent bonding. The biocatalysts were evaluated by infrared spectroscopy (FTIR) and hydrolytic activity analysis. Thus, from the analyses performed, the best biocatalyst obtained was the immobilized by covalent bond in maghemite, presenting a hydrolytic activity of 174.67 U/g.

The optimization of glycidyl methacrylate based terpolymer monolith synthesis: an effective Candida rugosa lipase immobilization support

2020 ◽  
Vol 27 (5) ◽  
Author(s):  
Zorica Veličić ◽  
Jelena Rusmirović ◽  
Nevena Prlainović ◽  
Nataša Tomić ◽  
Zlate Veličković ◽  
...  
Keyword(s):  
Glycidyl Methacrylate ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Lipase Immobilization
Sign in / Sign up

Export Citation Format

Share Document