Synthesis of Fe3O4/P(St-AA) nanoparticles for enhancement of stability of the immobilized lipases

RSC Advances ◽  
2016 ◽  
Vol 6 (110) ◽  
pp. 108583-108589 ◽  
Author(s):  
Zhiming Chen ◽  
Leilei Liu ◽  
Xiaodong Wu ◽  
Renchun Yang
Keyword(s):  
Immobilized Lipase ◽  
Core Shell ◽  
Magnetic Carrier ◽  
Lipase Immobilization ◽  
Immobilized Lipases

Core–shell Fe3O4/P(St-AA) nanoparticles were synthesized and employed as a magnetic carrier for lipase immobilization, and the properties of the immobilized lipase were studied.

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.

A Core–Shell Structured Immobilized Lipase and Its Application in High-Temperature Reactions

2019 ◽  
Vol 189 (3) ◽  
pp. 774-786 ◽  
Author(s):  
Li Deng ◽  
Jiaojiao Tian ◽  
Juntao Xu ◽  
Fang Wang ◽  
Kaili Nie ◽  
...  
Keyword(s):  
High Temperature ◽  
Immobilized Lipase ◽  
Core Shell ◽  
High Temperature Reactions

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.

Monodisperse core-shell magnetic organosilica nanoflowers with radial wrinkle for lipase immobilization

2017 ◽  
Vol 309 ◽  
pp. 70-79 ◽  
Author(s):  
Jing Gao ◽  
Weixi Kong ◽  
Liya Zhou ◽  
Ying He ◽  
Li Ma ◽  
...  
Keyword(s):  
Core Shell ◽  
Lipase Immobilization

Adsorptive removal of Ni(ii) ions from aqueous solution and the synthesis of a Ni-doped ceramic: an efficient enzyme carrier exhibiting enhanced activity of immobilized lipase

RSC Advances ◽  
2016 ◽  
Vol 6 (69) ◽  
pp. 64581-64588 ◽  
Author(s):  
Yanning Qu ◽  
Zhongjie Wu ◽  
Renliang Huang ◽  
Wei Qi ◽  
Rongxin Su ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Immobilized Lipase ◽  
Chitosan Nanoparticles ◽  
Ceramic Matrix ◽  
Lipase Immobilization ◽  
Adsorptive Removal ◽  
Enhanced Activity ◽  
Successful Removal

We report the successful removal of Ni2+ from aqueous solution via entrapment by chitosan nanoparticles, followed by calcination with a ceramic matrix to construct a novel carrier for lipase immobilization with enhanced activity.

scholarly journals INVESTIGATION OF ENZYMATIC HYDROLYSIS OF FATTY WASTE PROCESSING OF SUNFLOWER SEEDS BY IMMOBILIZED LIPASE

2020 ◽  
Vol 20 (1) ◽  
pp. 5-11
Author(s):  
V. Skliar ◽  
G. Krusir ◽  
V. Zakharchuk
Keyword(s):  
Crop Production ◽  
Agricultural Sector ◽  
Lipolytic Activity ◽  
Immobilized Lipase ◽  
Immobilized Enzymes ◽  
Lipase Immobilization ◽  
Ph Optimum ◽  
Prolonged Incubation ◽  
Physical And Chemical ◽  
Hydrolysis Of

Ukraine has a developed agricultural sector, in particular crop production, which is a source of large quantities of production residues and waste. One of the most promising areas for solving environmental problems in the production of grain products is the processing of industrial waste by enzymes and the use of processing products in other industries. The current needs of sustainable environmental practices have increased the use of enzymatic technologies in production processes. Lipases be used in the processing of waste from oil and fat enterprises, namely, waste from the stage of demetallization of hydrogenated fat from vegetable oils by enzymatic hydrolysis.The work is devoted to the study of conditions of enzyme Rhizopus japonicus lipase immobilization and its physical and chemical characteristics. Factors for obtaining immobilized biocatalysts, methods and conditions for determining the activity and stability of immobilized enzymes are highlighted. Lipolytic activity of the enzyme immobilized under these conditions remains more than 30% compared to native, which is a high indicator of activity retention. It has been shown that immobilization promotes the expansion of the pH- and thermo-optimum of the lipase. It was determined that for the Rhizopus japonicus immobilized lipase, the pH optimum increased with a shift from 7.0 to 6.5, and there was an increase in pH stability during prolonged incubation of the immobilized enzyme for alkaline and acidic pH values. It has been established that lipase immobilization leads to expansion of the thermo-optimum, as well as stabilization of the enzyme during prolonged incubation at 40 ° C and at higher temperatures (+60-80 ° C), which are possible when drying the final product. The high activity and stability of the immobilized lipase make it possible to recommend it for biotechnological processing ofoil-fat waste.

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 

Alginate–poly(vinyl alcohol) core–shell microspheres for lipase immobilization

2006 ◽  
Vol 102 (2) ◽  
pp. 1553-1560 ◽  
Author(s):  
Álvaro A. A. De Queiroz ◽  
Esdras D. Passos ◽  
Sdnei De Brito Alves ◽  
Gerald S. Silva ◽  
Olga Z. Higa ◽  
...  
Keyword(s):  
Vinyl Alcohol ◽  
Poly Vinyl Alcohol ◽  
Core Shell ◽  
Lipase Immobilization
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