Immobilization of papain on mesoporous silica: pH effect

Solís, S.; Paniagua, Jaime Chincheros; Martínez, Juan Carlos; Asomoza, M.

doi:10.1007/s10971-006-6431-1

Cited by 20 publications

(10 citation statements)

References 10 publications

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“…Silica particles are hydrophilic, biocompatible, and stable in most biosystems [24]. Moreover, silica chemistry is fairly well known, and standard chemical protocols can be followed to conjugate various biomolecules to the silica surface [18,29], which is an excellent solid support for enzyme immobilization [30,31]. NH 2 -modified SiO 2 particles were chosen for the immobilization experiment in this study, and the immobilization conditions, including the dosage of the crosslinking agent, reaction pH, reaction temperature, and enzyme dosage were optimized.…”

Section: Resultsmentioning

confidence: 99%

Immobilization of Cyclooxygenase-2 on Silica Gel Microspheres: Optimization and Characterization

et al. 2015

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Abstract:In this study, immobilized COX-2 was successfully constructed through glutaraldehyde-mediated covalent coupling on functional silica gel microspheres. The optimum conditions, properties, and morphological characteristics of the immobilized COX-2 were investigated. The optimal immobilization process was as follows: about 0.02 g of aminated silica gel microspheres was activated by 0.25% GA solution for 6 h and mixed with 5 U of free recombinant COX-2 solution. Then, the mixture was shaken for 8 h at 20˝C. Results showed that the immobilized COX-2 produced by this method exhibited excellent biocatalytic activity, equivalent to that of free COX-2 under the test conditions employed. The best biocatalytic activity of immobilized COX-2 appeared at pH 8.0 and still maintained at about 84% (RSD < 7.39%, n = 3) at pH 10.0. For temperature tolerance, immobilized COX-2 exhibited its maximum biocatalytic activity at 40˝C and about 68% (RSD < 6.99%, n = 3) of the activity was maintained at 60˝C. The immobilized COX-2 retained over 85% (RSD < 7.26%, n = 3) of its initial biocatalytic activity after five cycles, and after 10 days storage, the catalytic activity of immobilized COX-2 still maintained at about 95% (RSD < 3.08%, n = 3). These characteristics ensured the convenient use of the immobilized COX-2 and reduced its production cost.

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Section: Resultsmentioning

confidence: 99%

Immobilization of Cyclooxygenase-2 on Silica Gel Microspheres: Optimization and Characterization

et al. 2015

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“…Figure 1 shows the chemical route of the immobilization of papain. It is believed that the attachment of the papain is achieved through the amino groups on the papain as reported previously 11. The morphology of the carriers before and after immobilization was observed using SEM.…”

Section: Resultsmentioning

confidence: 76%

“…In general, there are four basic groups: adsorption to solid supports (e.g. using mesoporous silica11, 12), covalent attachment to solid supports,1, 2, 13, 14 cross‐linking to solid supports with bifunctional reagents (e.g. using glutaraldehyde3, 4), entrapment within polymeric gels (e.g.…”

Section: Introductionmentioning

confidence: 99%

Study on a carboxyl‐activated carrier and its properties for papain immobilization

Sun

Liang

Yuan

et al. 2012

J of Chemical Tech & Biotech

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“…It has been reported that the isoelectric point of papain is pH 8.6 [13]. Meanwhile, we noticed that the adsorption amount of papain on three adsorbents increased with the rising of pH value, especially when it was close to the isoelectric point of papain.…”

Section: Effect Of Phmentioning

confidence: 63%

Preparation of lignin derivatives and their application as protease adsorbents

Fang¹,

Yin²,

Cheng³

2009

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Synthesis of two lignin derivatives, lignophenol and lignin-aminophenol, were presented in this article. The chemical structure and the func-tional groups of lignin derivatives were charac-terized through FT-IR analysis. The immobiliza-tion of three proteases (papain, trypsin and pepsin) on lignin and lignin derivatives was carried out using adsorption technique. The influence of contact time and pH on the enzyme adsorption by different adsorbents was inves-tigated. Furthermore, enzyme activity recovery was also evaluated. Results showed that lignin and lignin derivatives could adsorb proteases effectively and the adsorption capacity of lingo- phenol and lignin-aminophenol was higher than that of pure lignin. Meanwhile, the activity re-covery of papain and pepsin immobilized on lignin derivatives was very high. This pheno- menon suggested that there is a supramole- cular interaction between enzymes and lignin derivatives which do not inhibit enzyme activity. Therefore, lignophenol and lignin-aminophenol are both promising adsorbents for enzyme im-mobilization under acid and neutral conditions

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Immobilization of papain on mesoporous silica: pH effect

Cited by 20 publications

References 10 publications

Immobilization of Cyclooxygenase-2 on Silica Gel Microspheres: Optimization and Characterization

Immobilization of Cyclooxygenase-2 on Silica Gel Microspheres: Optimization and Characterization

Study on a carboxyl‐activated carrier and its properties for papain immobilization

Preparation of lignin derivatives and their application as protease adsorbents

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