scholarly journals Immobilization of a Commercial Lipase from Penicillium camembertii (Lipase G) by Different Strategies

2011 ◽  
Vol 2011 ◽  
pp. 1-8 ◽  
Author(s):  
Adriano A. Mendes ◽  
Larissa Freitas ◽  
Ana Karine F. de Carvalho ◽  
Pedro C. de Oliveira ◽  
Heizir F. de Castro
Keyword(s):  
Thermal Stability ◽  
Physical Adsorption ◽  
Hydrolytic Activity ◽  
Covalent Attachment ◽  
Immobilize Lipase ◽  
Penicillium Camembertii ◽  
Ionic Adsorption ◽  
Hydrophobic Supports ◽  
Coupling Medium ◽  
Commercial Lipase

The objective of this work was to select the most suitable procedure to immobilize lipase from Penicillium camembertii (Lipase G). Different techniques and supports were evaluated, including physical adsorption on hydrophobic supports octyl-agarose, poly(hydroxybutyrate) and Amberlite resin XAD-4; ionic adsorption on the anionic exchange resin MANAE-agarose and covalent attachment on glyoxyl-agarose, MANAE-agarose cross-linked with glutaraldehyde, MANAE-agarose-glutaraldehyde, and epoxy-silica-polyvinyl alcohol composite. Among the tested protocols, the highest hydrolytic activity (128.2 ± 8.10 IU·g−1 of support) was achieved when the lipase was immobilized on epoxy-SiO2-PVA using hexane as coupling medium. Lipase immobilized by ionic adsorption on MANAE-agarose also gave satisfactory result, attaining 55.6 ± 2.60 IU·g−1 of support. In this procedure, the maximum loading of immobilized enzyme was 9.3 mg·g−1 of gel, and the highest activity (68.8 ± 2.70 IU·g−1 of support) was obtained when 20 mg of protein·g−1 was offered. Immobilization carried out in aqueous medium by physical adsorption on hydrophobic supports and covalent attachment on MANAE-agarose-glutaraldehyde and glyoxyl-agarose was shown to be unfeasible for Lipase G. Thermal stability tests revealed that the immobilized derivative on epoxy-SiO2-PVA composite using hexane as coupling medium had a slight higher thermal stability than the free lipase.

Characterization, performance, and applications of a yeast surface display-based biocatalyst

RSC Advances ◽  
2015 ◽  
Vol 5 (25) ◽  
pp. 19166-19175 ◽  
Author(s):  
J. M. Eby ◽  
S. W. Peretti
Keyword(s):  
Cost Analysis ◽  
Copy Number ◽  
Surface Display ◽  
Hydrolytic Activity ◽  
Yeast Surface Display ◽  
Expression Level ◽  
Yeast Surface ◽  
Commercial Lipase

Yeast surface display (YSD) of two lipases. Measured expression level and copy number. Synthetic and hydrolytic activity comparable to commercial lipase. Cost analysis of YSD system vs. commercial formulations.

Immobilization of modified penicillin G acylase on Sepabeads carriers

2009 ◽  
Vol 63 (2) ◽  
Author(s):  
Milena Žuža ◽  
Nenad Milosavić ◽  
Zorica Knežević-Jugović
Keyword(s):  
Thermal Stability ◽  
Hydrolytic Activity ◽  
Covalent Immobilization ◽  
Stability Study ◽  
Penicillin G Acylase ◽  
Penicillin G ◽  
Chemically Modified ◽  
Modified Enzyme ◽  
Derivatives Of ◽  
Thermal Stability Study

AbstractAn approach to stable covalent immobilization of chemically modified penicillin G acylase from Escherichia coli on Sepabeads® carriers with high retention of hydrolytic activity and thermal stability is presented. The two amino-activated polymethacrylate particulate polymers with different spacer lengths used in the study were Sepabeads® EC EA and Sepabeads® EC HA. The enzyme was first modified by cross-linking with polyaldehyde derivatives of starch in order to provide it with new useful functions. Such modified enzyme was then covalently immobilized on amino supports. The method seems to provide a possibility to couple the enzyme without risking a reaction at the active site which might cause the loss of activity. Performances of these immobilized biocatalysts were compared with those obtained by the conventional method with respect to activity and thermal stability. The thermal stability study shows that starch-PGA immobilized on Sepabeads EC-EA was almost 4.5-fold more stable than the conventionally immobilized one and 7-fold more stable than free non-modified PGA. Similarly, starch-PGA immobilized on Sepabeads EC-HA was around 1.5- fold more stable than the conventionally immobilized one and almost 9.5-fold more stable than free non-modified enzyme.

scholarly journals Characterisation of a “green” lipase from Aspergillus niger immobilised on polyethersulfone membranes

2019 ◽  
Vol 42 ◽  
pp. e44498
Author(s):  
Fernanda Martins de Souza ◽  
Cleide Mara Faria Soares ◽  
Alvaro Silva Lima ◽  
Luciana Cristina Lins de Aquino Santana
Keyword(s):  
Thermal Stability ◽  
Aspergillus Niger ◽  
Thermal Inactivation ◽  
Physical Adsorption ◽  
Covalent Bonding ◽  
Point Of View ◽  
Thermal Stabilities ◽  
Optimum Ph ◽  
Hancornia Speciosa ◽  
Free Lipase

In this work, a “green” Aspergillus niger lipase obtained from the solid-state fermentation of Hancornia speciosa (“mangaba”) seeds was efficiently immobilised on polyethersulfone membranes (PES) by physical adsorption (PES-ADS-lipase) and covalent bonding (PES-COV-lipase) (immobilisation yields of 92 and 81%, respectively). The free lipase showed an optimum pH close to neutrality, while the biocatalysts displaced the pH to the alkaline region (optimum pH 9.0 and 11.0 for PES-ADS-lipase and PES-COV-lipase, respectively). The optimum temperature of free lipase was 55°C; however, a higher thermal stability occurred at 37°C. The PES-ADS-lipase and PES-COV-lipase showed lower optimum temperatures (37 and 45°C, respectively) but higher thermal stabilities at 45 and 55°C, respectively. The lower thermal inactivation constant and higher half-life of PES-COV-lipase at 55°C confirmed the efficiency of covalent bonding in maintaining the thermal stability of the enzyme. The Michaelis–Menten constant (Km) and maximum rate of reaction (Vmax) were also determined, and the biocatalysts showed higher affinities to substrates (lower Km values) than free lipase. In this work, the biocatalysts showed good catalytic properties with future potential applications in hydrolysis reactions. The use of a “green” lipase obtained from agroindustrial residue makes this product economically attractive from an industrial point of view.

Sonochemical Functionalization of Boron Nitride Nanomaterials

MRS Advances ◽  
2019 ◽  
Vol 5 (14-15) ◽  
pp. 709-716
Author(s):  
Haley B. Harrison ◽  
Jeffrey R. Alston
Keyword(s):  
Thermal Stability ◽  
Boron Nitride ◽  
Photoelectron Spectroscopy ◽  
Colloidal Stability ◽  
Hexagonal Boron Nitride ◽  
Boron Nitride Nanotubes ◽  
Covalent Attachment ◽  
Covalent Functionalization ◽  
X Ray ◽  
Ft Ir

AbstractBoron nitride nanotubes (BNNTs) and hexagonal boron nitride platelets (h-BNs) have received considerable attention for aerospace insulation applications due to their exceptional chemical and thermal stability. Presently, making BN nanomaterials compatible with polymer and composite matrices is challenging. Due to their inert and highly stable structure, h-BN and BNNTs are difficult to covalently functionalize. In this work, we present a novel sonochemical technique that enables covalent attachment of fluoroalkoxy substituents to the surface of BN nanomaterials in a controlled and metered process. Covalent functionalization is confirmed via colloidal stability analysis, FT-IR, and x-ray photoelectron spectroscopy (XPS).

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.

scholarly journals Immobilization of Phospholipase D on Silica-Coated Magnetic Nanoparticles for the Synthesis of Functional Phosphatidylserine

Catalysts ◽  
2019 ◽  
Vol 9 (4) ◽  
pp. 361 ◽  
Author(s):  
Qingqing Han ◽  
Haiyang Zhang ◽  
Jianan Sun ◽  
Zhen Liu ◽  
Wen-can Huang ◽  
...  
Keyword(s):  
Electron Microscope ◽  
Magnetic Nanoparticles ◽  
Phospholipase D ◽  
Physical Adsorption ◽  
Catalytic Reactions ◽  
Covalent Attachment ◽  
Synthesis Process ◽  
Transmission Electron ◽  
Ft Ir ◽  
Magnetic Nanoparticles Fe3o4

In this study, silica-coated magnetic nanoparticles (Fe3O4/SiO2) were synthesized and applied in the immobilization of phospholipase D (PLDa2) via physical adsorption and covalent attachment. The immobilized PLDa2 was applied in the synthesis of functional phosphatidylserine (PS) through a transphophatidylation reaction. The synthesis process and characterizations of the carriers were examined by scanning electron microscope (SEM), transmission electron microscope (TEM), and Fourier-transform infrared spectroscopy (FT-IR). The optimum immobilization conditions were evaluated, and the thermal and pH stability of immobilized and free PLDa2 were measured and compared. The tolerance to high temperature of immobilized PLDa2 increased remarkably by 10°C. Furthermore, the catalytic activity of the immobilized PLDa2 remained at 40% after eight recycles, which revealed that silica-coated magnetic nanoparticles have potential application for immobilization and catalytic reactions in a biphasic system.

scholarly journals Building Functional Surfaces for Biosensors Development

2013 ◽  
Vol 543 ◽  
pp. 204-207
Author(s):  
Carlos Morón ◽  
Alfonso Garcia ◽  
Enrique Tremps ◽  
Jose Andrés Somolinos
Keyword(s):  
Textile Industry ◽  
Physical Adsorption ◽  
Covalent Binding ◽  
Covalent Attachment ◽  
Layer By Layer ◽  
Protein Patterns ◽  
Highly Active ◽  
Pulp Paper ◽  
Potential Applications ◽  
Protein Resistant

Polyelectrolyte multilayers (PEM) built by layer-by-layer technique have been extensively studied over the last years, resulting in a wide variety of current and potential applications. This technique can be used to construct thin films with different functionalities, or to functionalize surfaces with substantial different properties of those of the underlying substrates. The multilayering process is achieved by the alternate adsorption of oppositely charged polyelectrolytes. In this work we get advantage of the protein resistant property of the Poly (l-lysine)-graft-(polyethyleneglycol) to create protein patterns. Proteins can be immobilized on a surface by unspecific physical adsorption, covalent binding or through specific interactions. The first protein used in this work was laccase, a copper-containing redox enzyme that catalyse the oxidation of a broad range of polyphenols and aromatic substrates, coupled to the reduction of O2to H2O without need of cofactors. Applications of laccases have been reported in food, pulp, paper, and textile industry, and also in biosensor development. Some uses require the immobilization of the enzyme on solid supports by adsorption, covalent attachment, entrapment, etc, on several substrates. Especially for biosensor development, highly active, stable and reproducible immobilization of laccase is required.

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

Catalysts ◽  
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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