Immobilization of porcine pancreatic lipase in zeolite MCM 22 with different Si/Al ratios

Calgaroto, Cléber; Scherer, Robison P.; Calgaroto, Selma; Oliveira, J. Vladimir; Oliveira, Débora de; Pergher, Sibele B. C.

doi:10.1016/j.apcata.2010.12.032

Cited by 22 publications

(10 citation statements)

References 15 publications

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“…they are resistant to biodegradation; they possess properties such as high surface areas and hydrophobic or hydrophilic behavior; they can be prepared with cavities ranging from micropore to mesopore) . Zeolites are crystalline aluminosilicates with a structure of tridimensional combination of tetrahedrons of SiO 4 and AlO 4 linked by oxygen atoms . They have microporous constitution including wide channels of different sizes that allow some molecules or ions to pass through while blocking others.…”

Section: Introductionmentioning

confidence: 99%

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Clinoptilolite particles as a carrier for biocatalysts immobilization: invertase immobilization and characterization

Bahar

2013

Asia-Pacific J Chem Eng

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Clinoptilolite, a natural zeolite, was proposed as a carrier for immobilized biocatalyst systems by polyethyleneimine and glutaraldehyde activation. Invertase (EC 3.2.1.26, beta-fructofuranosidase) as a model biocatalyst was covalently attached onto the particles by direct chemical reaction between aldehyde groups on the particles and amine groups of the enzyme. The effects of polyethyleneimine concentration, activation agent (glutaraldehyde) concentration, pH and invertase concentration on immobilization process were determined. Approximately 7 mg invertase was immobilized on a gram of clinoptilolite particles with 78% retained activity under optimum immobilization conditions. Immobilization did not affect optimum pH of the enzyme, but it brought out a wider pH-activity curve that was accepted as the indication of better pH stability. Immobilization resulted in an increase at the optimum temperature from 55 to 60 C. The K M value of immobilized invertase biosystem was found as approximately 1.5 times higher than that of the free enzyme. Immobilization provided improvement on the thermal stability of invertase, and activity half-life of the immobilized invertase was found as approximately four times longer than that of the free invertase.

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Section: Introductionmentioning

confidence: 99%

“…Zeolites also have some disadvantages, such as fragility under harsh stirring conditions, but their rigidity makes them suitable for packed bed reactor applications. Several synthetic or modified zeolites have been utilized as carrier for immobilization of different enzymes because of these properties …”

Section: Introductionmentioning

confidence: 99%

Clinoptilolite particles as a carrier for biocatalysts immobilization: invertase immobilization and characterization

Bahar

2013

Asia-Pacific J Chem Eng

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“…To enhance the properties of lipase‐catalyzed reactions, including the reusability, stability and recovery, most of the lipases used in industrial processes are immobilized on various carriers . As a result, various different kinds of supports, including synthetic resins, inorganic polymers (mesoporous silica and zeolites, etc. ), and synthetic organic polymers, have been developed to immobilize lipases.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Candida rugosa Lipase on Glutaraldehyde‐Activated Fe₃O₄@Chitosan as a Magnetically Separable Catalyst for Hydrolysis of Castor Oil

Zhao

Chen

et al. 2017

Euro J Lipid Sci & Tech

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In this study, the catalyzed hydrolysis of castor oil by Candida rugosa lipase (CRL) immobilized on glutaraldehyde‐activated magnetic Fe3O4@chitosan is investigated. Magnetic Fe3O4 is prepared by hydrothermal method and coated with chitosan (CS). Next, CRL is immobilized on Fe3O4@chitosan using glutaraldehyde as a cross‐linking reagent. The prepared Fe3O4@CS@CRL is confirmed by scanning electron microscopy (SEM), X‐ray powder diffraction (XRD), vibrating sample magnetometry (VSM), Fourier transform infrared (FTIR) spectroscopy, and thermogravimetric analysis (TGA). The response surface methodology (RSM) based on the Box–Behnken design is used to evaluate and optimize the hydrolysis reaction variables. The optimum reaction conditions for the hydrolysis of castor oil by the Fe3O4@CS@CRL heterogeneous catalyst are found to be a water/oil ratio of 1.60:1, pH of 7.05, reaction temperature of 34 °C, and lipase concentration of 3.27%; under these conditions, the hydrolysis conversion of castor oil reached 46.81%. Moreover, the immobilized lipase showed high stability with no appreciable loss in its activity after three consecutive cycles. Practical Applications: RSM is found to be a useful technique for optimizing hydrolysis of castor oil. The high conversion of the hydrolysis of castor oil indicates that the Fe3O4@CS@CRL have potential to be used in preparing ricinoleic acid from castor oil. Ricinoleic acid have the potential to be used in printing ink as a pigment and dye disperser, plasticizers, surfactants, lubricants, and other valuable products. Ricinoleic acid can be used in pigment and dye disperser in printing ink, sebacic acid, azelaic acid, heptaldehyde, plasticizers, surfactants, lubricants, and other valuable products. Hydrolysis of castor oil catalyzed by Candida rugosa lipase (CRL) immobilized on glutaraldehyde‐activated magnetic Fe3O4@chitosan is investigated. The response surface methodology (RSM) based on the Box–Behnken design is used to evaluate and optimize the hydrolysis reaction variables. Fe3O4@CS@CRL can be easily separated from the suspension using an external strong magnet. Fe3O4@CS@CRL have potential to be used in preparing ricinoleic acid from castor oil.

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“…Calgaroto et al 39 used the MCM 22 zeolite with different Si/Al ratios (15, 25 and 50) as support for immobilization of porcine pancreatic lipase, assessing the effect of its structure on the immobilization yield and enzyme activity. Results showed that the material composition influenced significantly the immobilization process.…”

Section: Zeolitesmentioning

confidence: 99%

Screening of supports for immobilization of commercial porcine pancreatic lipase

et al. 2011

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The aim of this work is to report the performance of different supports for the immobilization of commercial porcine pancreatic lipase. The immobilization tests were carried out in several types of Accurel, activated alumina, kaolin, montmorillonite, ion exchange resins and zeolites. The characterization of the supports showed differences in terms of specific area and morphology. The characteristics of the supports influenced the amount of enzyme adsorbed, yield of immobilization and esterification activity of the resulting immobilized catalyst. The clays KSF and natural and pillared montmorillonites presented potential for use as support for lipase immobilization in terms of yield and esterification activity. Yields of immobilization of 76.32 and 52.01% were achieved for clays KSF and natural montmorillonite, respectively. Esterification activities of 754.03, 595.51, 591.88 and 515.71 U.g -1 were obtained for lipases immobilized in Accurel MP-100, Amberlite XAD-2, mordenite and pillared montmorillonite, respectively.

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Immobilization of porcine pancreatic lipase in zeolite MCM 22 with different Si/Al ratios

Cited by 22 publications

References 15 publications

Clinoptilolite particles as a carrier for biocatalysts immobilization: invertase immobilization and characterization

Clinoptilolite particles as a carrier for biocatalysts immobilization: invertase immobilization and characterization

Immobilization of Candida rugosa Lipase on Glutaraldehyde‐Activated Fe₃O₄@Chitosan as a Magnetically Separable Catalyst for Hydrolysis of Castor Oil

Screening of supports for immobilization of commercial porcine pancreatic lipase

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Immobilization of porcine pancreatic lipase in zeolite MCM 22 with different Si/Al ratios

Cited by 22 publications

References 15 publications

Clinoptilolite particles as a carrier for biocatalysts immobilization: invertase immobilization and characterization

Clinoptilolite particles as a carrier for biocatalysts immobilization: invertase immobilization and characterization

Immobilization of Candida rugosa Lipase on Glutaraldehyde‐Activated Fe3O4@Chitosan as a Magnetically Separable Catalyst for Hydrolysis of Castor Oil

Screening of supports for immobilization of commercial porcine pancreatic lipase

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Immobilization of Candida rugosa Lipase on Glutaraldehyde‐Activated Fe₃O₄@Chitosan as a Magnetically Separable Catalyst for Hydrolysis of Castor Oil