Optimum Conditions for Lipase Immobilization on Halloysitum Rubrum

2013 ◽  
Vol 864-867 ◽  
pp. 465-471
Author(s):  
Tao Deng ◽  
Jun Wei Xu ◽  
Li Huang ◽  
Tao Li ◽  
Xu Ya Yu
Keyword(s):  
Response Surface Methodology ◽  
Experimental Design ◽  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Initial Activity ◽  
Optimum Conditions ◽  
Lipase Immobilization ◽  
Support Materials ◽  
Optimum Ph ◽  
Support Ratio

In this study, we use natural halloysitum rubrum as novel support materials to immobilize Candida rugosa lipase. The response surface methodology with a four-factor three-level Box-Behnken experimental design was used to evaluate the effects of immobilization parameters, such as pH (4.0 to 6.0), immobilization temperature (25 °C to 35 °C), enzyme/support ratio (0.1 to 0.3, w/w), and immobilization time (1 h to 2 h), on the activity of immobilized lipase. The optimum pH, temperature, enzyme/support ratio, and time for immobilized lipase activity (376.09 U/g) were 5.17, 29.65 °C, 0.3 (w/w), and 1.63 h, respectively. After 15 repeated uses, the immobilized lipase still retained 80% of its initial activity, which indicates good reusability.

scholarly journals Covalent immobilization of an alkaline protease from Bacillus licheniformis

2018 ◽  
Vol 43 (6) ◽  
pp. 595-604
Author(s):  
Yakup Aslan ◽  
Derya Ömerosmanoğlu ◽  
Eda Öndül Koç
Keyword(s):  
Bacillus Licheniformis ◽  
Immobilized Enzyme ◽  
Milk Proteins ◽  
Covalent Immobilization ◽  
Initial Activity ◽  
Optimum Conditions ◽  
Continuous Processes ◽  
Operational Conditions ◽  
Optimum Ph ◽  
Soluble Enzymes

Abstract Objective Since the soluble enzymes can not be used in repeated reactions and are not stable in operational conditions and not suitable for continuous processes, this study aimed the covalent immobilization of Bacillus licheniformis protease (BLP) onto Eupergit CM. Methods Optimum conditions for immobilization were determined by changing the conditions individually. The proteins and L-tyrosine were determined by UV/VIS spectrophotometer. Results The immobilization resulted in 100% immobilization and 107.7% activity yields. The optimum pH (7–8) and the optimum temperature (70°C) have not changed after immobilization. The Km values for free and immobilized enzyme were 26.53 and 37.59 g/L, while the Vmax values were 2.84 and 3.31 g L-Tyrosine/L·min, respectively. The immobilized enzyme has not lost its initial activity during the repeated 20 uses and 20 days of storage. The milk proteins were hydrolyzed in 2 h by using immobilized enzyme. The pH of the milk dropped from 6.89 to 6.53, the color was clearer but there was no change in the smell or the taste. Conclusion Consequently, it can be said that the immobilized BLP obtained can be used for industrial purposes.

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 

Optimization of Enzyme Assisted Extraction Technology of Flavonoids from Seabuckthorn Fruit Peel Marc

2012 ◽  
Vol 550-553 ◽  
pp. 1826-1830
Author(s):  
Yan Jiao ◽  
Ying Chang ◽  
Shi Feng Yu ◽  
Xiao Hong Sun ◽  
Chun Li Song
Keyword(s):  
Response Surface Methodology ◽  
Experimental Design ◽  
Ph Value ◽  
Optimal Conditions ◽  
Optimum Conditions ◽  
Fruit Peel ◽  
Extraction Technology ◽  
Assisted Extraction ◽  
Enzyme Dosage ◽  
Enzyme Assisted Extraction

Enzyme assisted extraction of flavonoids from seabuckthorn fruit peel marc was studied by response surface methodology(RSM), using a Box-Behnken experimental design. A mathematical polynomial model was proposed with regard to investigate the effect of cellulase dosage (x1), enzymolysis temperature (x2), and pH value (x3)to the flavonoids yields. These factors were further optimized using RSM. The optimal conditions were: cellulase enzyme dosage was at 73.3IU/g, temperatur was at 53.7°C and the pH was at 4.14. Under the optimum conditions, gave rise to the highest flavonoids yields, approaching 8.02 mg/g of flavonoids yields.

scholarly journals Novel amphiphilic polyvinylpyrrolidone functionalized silicone particles as carrier for low-cost lipase immobilization

2018 ◽  
Vol 5 (6) ◽  
pp. 172368 ◽  
Author(s):  
Shan Zhang ◽  
Qianchun Deng ◽  
Ya Li ◽  
Mingming Zheng ◽  
Chuyun Wan ◽  
...  
Keyword(s):  
Photoelectron Spectroscopy ◽  
Rational Design ◽  
Low Cost ◽  
Immobilized Lipase ◽  
High Catalytic Activity ◽  
Lipase Immobilization ◽  
X Ray ◽  
Support Materials ◽  
Steady Rate ◽  
Loading Amount

The high catalytic activity, specificity and stability of immobilized lipase have been attracting great interest. How to reduce the cost of support materials has always been a hot topic in this field. Herein, for the development of low-cost immobilized lipase, we demonstrate an amphiphilic polyvinylpyrrolidone (PVP) grafted on silicone particle (SP) surface materials (SP-PVP) with a rational design based on interfacial activation and solution polymerization. Meanwhile, hydrophilic pristine SP and hydrophobic polystyrene-corded silicone particles (SP-Pst) were also prepared for lipase immobilization. SP-PVP was characterized by X-ray diffraction, scanning electron microscopy, X-ray photoelectron spectroscopy, Fourier transform infrared spectroscopy and thermogravimetry. Our results indicated that the lipase loading amount on the SP-PVP composites was about 215 mg of protein per gram. In the activity assay, the immobilized lipase SP-PVP@CRL exhibited higher catalysis activity and better thermostability and reusability than SP@CRL and SP-Pst@CRL. The immobilized lipase retained more than 54% of its initial activity after 10 times of re-use and approximately trended to a steady rate in the following cycles. By introducing the interesting amphiphilic polymer to this cheap and easily obtained SP surface, the relative performance of the immobilized lipase can be significantly improved, facilitating interactions between the low-cost support materials and lipase.

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.

scholarly journals Obtaining process of interpolymeric complexes from lactalbumin, xanthan gum and pectin

2014 ◽  
Vol 17 (3) ◽  
pp. 213-220 ◽  
Author(s):  
Virginia Coimbra Zuvanov ◽  
Edwin Elard Garcia-rojas ◽  
Clitor Júnior Fernandes de Souza ◽  
Eliana da Silva Gulão ◽  
Luciano José Barreto Pereira
Keyword(s):  
Experimental Data ◽  
Response Surface Methodology ◽  
Experimental Design ◽  
Response Surface ◽  
Xanthan Gum ◽  
Optimization Process ◽  
Coefficient Of Determination ◽  
Optimum Conditions ◽  
Independent Variables ◽  
Nacl Concentration

In this work, the optimization process of interpolymeric complexes formation between lactalbumin and the polysaccharides xanthan gum and pectin was studied in order to define the optimum conditions for the complexes formation. For the experimental design, response surface methodology (RSM) for three independent variables was used. The optimum conditions for the complexes formation between lactalbumin and xanthan gum were: pH 6.6, NaCl concentration of 0.6 mol/L and xanthan gum concentration 0.083% w/v. And for the complexes formed between pectin and lactalbumin the conditions were: pH 6.6, NaCl concentration of 0.25 mol/L and pectin concentration of 0.113% w/v. The best fitted model for the experimental data was that corresponding to the complex xanthan gum-lactalbumin, whose coefficient of determination (R²) was 0.97.

scholarly journals Novel approaches to immobilize Candida rugosa lipase on nanocomposite membranes prepared by covalent attachment of magnetic nanoparticles on poly acrylonitrile membrane

RSC Advances ◽  
2018 ◽  
Vol 8 (9) ◽  
pp. 4561-4570 ◽  
Author(s):  
Marzieh Aghababaie ◽  
Masoud Beheshti ◽  
Abdol-Khalegh Bordbar ◽  
Amir Razmjou
Keyword(s):  
Magnetic Nanoparticles ◽  
Immobilized Lipase ◽  
Candida Rugosa ◽  
Candida Rugosa Lipase ◽  
Covalent Attachment ◽  
Lipase Immobilization ◽  
Nanocomposite Membranes ◽  
Novel Approaches ◽  
Novel Methods ◽  
Poly Acrylonitrile

Novel methods have been developed for lipase immobilization on poly acrylonitrile (PAN) membranes to increase the activity and stability of the immobilized lipase.

scholarly journals Modeling and Sensitivity Analysis of the Forward Osmosis Process to Predict Membrane Flux Using a Novel Combination of Neural Network and Response Surface Methodology Techniques

Membranes ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 70
Author(s):  
Jasir Jawad ◽  
Alaa H. Hawari ◽  
Syed Javaid Zaidi
Keyword(s):  
Response Surface Methodology ◽  
Experimental Design ◽  
Response Surface ◽  
Forward Osmosis ◽  
Feed Solution ◽  
Operating Conditions ◽  
Ann Model ◽  
Membrane Flux ◽  
Input Variables ◽  
Rsm Model

The forward osmosis (FO) process is an emerging technology that has been considered as an alternative to desalination due to its low energy consumption and less severe reversible fouling. Artificial neural networks (ANNs) and response surface methodology (RSM) have become popular for the modeling and optimization of membrane processes. RSM requires the data on a specific experimental design whereas ANN does not. In this work, a combined ANN-RSM approach is presented to predict and optimize the membrane flux for the FO process. The ANN model, developed based on an experimental study, is used to predict the membrane flux for the experimental design in order to create the RSM model for optimization. A Box–Behnken design (BBD) is used to develop a response surface design where the ANN model evaluates the responses. The input variables were osmotic pressure difference, feed solution (FS) velocity, draw solution (DS) velocity, FS temperature, and DS temperature. The R2 obtained for the developed ANN and RSM model are 0.98036 and 0.9408, respectively. The weights of the ANN model and the response surface plots were used to optimize and study the influence of the operating conditions on the membrane flux.

Sign in / Sign up

Export Citation Format

Share Document