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

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.

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Enhanced biological activity of Candida rugosa lipase via immobilization on magnetic nanoparticles

Egyptian Journal of Chemistry ◽

10.21608/ejchem.2020.25662.2512 ◽

2020 ◽

Vol 0 (0) ◽

pp. 0-0

Author(s):

Miaad Adnan ◽

Sahar Gazi Imran ◽

Adel Saadi Alsaadi ◽

Mohammed Hasan Allawi

Keyword(s):

Biological Activity ◽

Magnetic Nanoparticles ◽

Candida Rugosa ◽

Candida Rugosa Lipase

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Investigating Enzyme Activity of Immobilized Candida rugosa Lipase

Journal of Food Quality ◽

10.1155/2018/1618085 ◽

2018 ◽

Vol 2018 ◽

pp. 1-9 ◽

Cited By ~ 5

Author(s):

Bhagya Sri Kaja ◽

Stephen Lumor ◽

Samuel Besong ◽

Bettina Taylor ◽

Gulnihal Ozbay

Keyword(s):

Milk Fat ◽

Candida Rugosa ◽

Catalytic Efficiency ◽

Hydrolytic Activity ◽

Candida Rugosa Lipase ◽

Support Materials ◽

Fatty Acid Chain ◽

Hydrolytic Activities ◽

Immobilized Candida Rugosa Lipase ◽

Immobilization Techniques

Candida rugosa lipase is a food-grade enzyme that is extensively utilized in the dairy processing industry for milk fat hydrolysis. The enzyme is mainly employed to modify the fatty acid chain length that results in the enhancement of flavors. The hydrolytic activities of C. rugosa lipase (fungal source) in its free and immobilized forms were investigated at different pH and temperature settings. The main objective of this study was to understand how different support materials (Celite-545, Sephadex G-25, and chitosan) and immobilization techniques alter lipase activity and stability. Our results indicated that hydrolytic activity increased significantly with immobilization on Celite-545. In general, immobilization resulted in considerable improvements in the stability of the enzyme with variations in pH and temperature. Immobilization on Celite-545 led to the highest catalytic efficiency. Remarkable improvements in the recovery and reusability of the immobilized lipases were noted. Comparatively, the acetone immobilization procedure resulted in higher activities than alcohol immobilization. In conclusion, the activity of C. rugosa lipase was enhanced most significantly when immobilized on Celite-545 using acetone as an adsorption solvent.

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Utilization of Clay Materials as Support for Aspergillus japonicus Lipase: An Eco-Friendly Approach

Catalysts ◽

10.3390/catal11101173 ◽

2021 ◽

Vol 11 (10) ◽

pp. 1173

Author(s):

Daniela Remonatto ◽

Bárbara Ribeiro Ferrari ◽

Juliana Cristina Bassan ◽

Cassamo Ussemane Mussagy ◽

Valéria de Carvalho Santos-Ebinuma ◽

...

Keyword(s):

Physical Adsorption ◽

Immobilized Lipase ◽

Cost Effective ◽

Hydrolytic Activity ◽

Catalytic Performance ◽

Submerged Cultivation ◽

Industrial Processes ◽

Adsorption Method ◽

Aspergillus Japonicus ◽

Clay Materials

Lipase is an important group of biocatalysts, which combines versatility and specificity, and can catalyze several reactions when applied in a high amount of industrial processes. In this study, the lipase produced by Aspergillus japonicus under submerged cultivation, was immobilized by physical adsorption, using clay supports, namely, diatomite, vermiculite, montmorillonite KSF (MKSF) and kaolinite. Besides, the immobilized and free enzyme was characterized, regarding pH, temperature and kinetic parameters. The most promising clay support was MKSF that presented 69.47% immobilization yield and hydrolytic activity higher than the other conditions studied (270.7 U g−1). The derivative produced with MKSF showed high stability at pH and temperature, keeping 100% of its activity throughout 12 h of incubation in the pH ranges between 4.0 and 9.0 and at a temperature from 30 to 50 °C. In addition, the immobilized lipase on MKSF support showed an improvement in the catalytic performance. The study shows the potential of using clays as support to immobilized lipolytic enzymes by adsorption method, which is a simple and cost-effective process.

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Candida Rugosa Lipase Immobilized on Hydrophobic Support Accurel MP 1000 in the Synthesis of Emollient Esters

10.21203/rs.3.rs-509734/v1 ◽

2021 ◽

Author(s):

Luiz Henrique Sales de Menezes ◽

Eliezer Luz do Espírito Santo ◽

Marta Maria Oliveira dos Santos ◽

Iasnaia Maria de Carvalho Tavares ◽

Adriano Aguiar Mendes ◽

...

Keyword(s):

Specific Activity ◽

Physical Adsorption ◽

Candida Rugosa ◽

Candida Rugosa Lipase ◽

Wax Esters ◽

Molar Ratio ◽

Original Activity ◽

The Stability ◽

Esterification Reactions ◽

Reaction Cycles

Abstract In the present work, Candida rugosa lipase (CRL) was immobilized by physical adsorption in organic medium on Accurel MP 1000 (AMP) with a protein load of 6.5 mg g-1 (mg protein/g support). CRL-AMP was applied with 5 and 10% of catalyst/volume of medium (m v-1) in esterification reactions of stearic acid with lauryl and cetyl alcohols producing the wax esters such as dodecanoyl octadecanoate 1 and hexadecanoyl octadecanoate 2 in a heptane medium. Six reaction cycles were studied to evaluate the stability and recyclability of the prepared biocatalyst. The specific activity (Asp) for CRL-AMP was 200 ± 20 U mg-1. Its catalytic activity was 1300 ± 100 U g-1. CRL-AMP was used in the synthesis of esters in heptane medium with a 1:1 acid:alcohol molar ratio at 45°C and 200 rpm. In synthesis 1, conversion was 62.5 ± 3.9% in 30 min at 10% m v-1 and 56.9 ± 2.8% in 54 min at 5% m v-1, while in synthesis 2, conversion was 79.0 ± 3.9% in 24 min at 10% m v-1, and 46.0 ± 2.4% in 54 min at 5% m v-1. Reuse tests after 6 consecutive cycles of reaction showed that the biocatalyst retained approximately 50% of its original activity for both reaction systems. CRL-AMP showed a high potential in the production of wax esters, since it started from low enzymatic load and high specific activities and conversions were obtained, in addition to allowing an increase in stability and recyclability of the prepared biocatalyst.

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2-Propanol treatment of Candida rugosa lipase and its hydrolytic activity

Journal of Molecular Catalysis B Enzymatic ◽

10.1016/s1381-1177(03)00110-3 ◽

2003 ◽

Vol 24-25 ◽

pp. 67-73 ◽

Cited By ~ 6

Author(s):

Michimasa Goto ◽

Hisato Ogawa ◽

Takahiro Isobe ◽

Masashi Kawasaki ◽

Tadashi Kometani

Keyword(s):

Candida Rugosa ◽

Hydrolytic Activity ◽

Candida Rugosa Lipase

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Candida rugosa lipase immobilization on magnetic silica aerogel nanodispersion

RSC Advances ◽

10.1039/c5ra24441b ◽

2016 ◽

Vol 6 (15) ◽

pp. 12676-12687 ◽

Cited By ~ 29

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.

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

RSC Advances ◽

10.1039/c7ra11866j ◽

2018 ◽

Vol 8 (9) ◽

pp. 4561-4570 ◽

Cited By ~ 7

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.

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Effect of Temperature on Fe3O4 Magnetic Nanoparticles Prepared by Coprecipitation Method

Advanced Materials Research ◽

10.4028/www.scientific.net/amr.900.172 ◽

2014 ◽

Vol 900 ◽

pp. 172-176 ◽

Cited By ~ 6

Author(s):

Ji Mei Niu ◽

Zhi Gang Zheng

Keyword(s):

Magnetic Nanoparticles ◽

Coprecipitation Method ◽

Effect Of Temperature ◽

Vibrating Sample Magnetometer ◽

X Ray Diffraction ◽

X Ray ◽

Magnetic Carriers ◽

Average Grain Size ◽

Or Gene ◽

Block Temperature

The Fe3O4 magnetic nanoparticles obtained by the aqueous coprecipitation method are characterized systematically using scanning electron microscope, X-ray diffraction and vibrating sample magnetometer. These magnetic nanoparticles are spheric, dispersive, and have average grain size of 50 nm. The size and magnetic properties of Fe3O4 nanoparticles can be tuned by the reaction temperature. All samples exhibit high saturation magnetization (Ms=53.4 emu·g-1) and superparamagnetic behavior with a block temperature (TB) of 215K. These properties make such Fe3O4 magnetic nanoparticles worthy candidates for the magnetic carriers of targeted-drug or gene therapy in future.

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