Preparation and characterization of κ-carrageenase immobilized onto magnetic iron oxide nanoparticles
Background Carboxyl-functionalized magnetic nanoparticles were synthesized via chemical co-precipitation method and modified with oleic acid which was oxidized by potassium permanganate, and κ-carrageenase from Pseudoalteromonas sp. ASY5 was subsequently immobilized onto them. The immobiliz...
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Pontificia Universidad Católica de Valparaíso
2016
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oai:scielo:S0717-345820160001000012016-05-11Preparation and characterization of κ-carrageenase immobilized onto magnetic iron oxide nanoparticlesXiao,AnfengXu,CaiyunLin,YanNi,HuiZhu,YanbingCai,Huinong Carrageenase Characterization Immobilization Nanoparticles Background Carboxyl-functionalized magnetic nanoparticles were synthesized via chemical co-precipitation method and modified with oleic acid which was oxidized by potassium permanganate, and κ-carrageenase from Pseudoalteromonas sp. ASY5 was subsequently immobilized onto them. The immobilization conditions were further optimized, and the characterizations of the immobilized κ-carrageenase were investigated. Results The κ-carrageenase was immobilized onto magnetic iron oxide nanoparticles, and the bonding was verified by Fourier transform infrared spectroscopy. The optimal conditions for κ-carrageenase immobilization were 2.5% (w/v) glutaraldehyde, 13.9 U κ-carrageenase for 20 mg of magnetic nanoparticles, a 2-h cross-linking time, and a 2-h immobilization time at 25°C. Under these conditions, the activity of the immobilized enzyme and the enzyme recovery rate were 326.0 U · g- 1 carriers and 46.9%, respectively. The properties of the immobilized κ-carrageenase were compared with those of the free enzyme. The optimum temperatures of the free and immobilized κ-carrageenase were 60 and 55°C, respectively, and the optimum pH of κ-carrageenase did not change before and after immobilization (pH 7.5). After immobilization, κ-carrageenase exhibited lower thermal stability and improved pH stability, as well as better storage stability. The immobilized κ-carrageenase maintained 43.5% of the original activity after being used 4 times. The kinetic constant value (Km) of κ-carrageenase indicates that the immobilized enzyme had a lower binding affinity for the substrate. Conclusions Under optimal conditions, the activity of the immobilized enzyme and enzyme recovery rate were 326.0 U · g- 1·κ-carrageenase-CMNPs and 46.9%, respectively. The thermal, pH, and storage stabilities of κ-carrageenase-CMNPs were relatively higher than those of free κ-carrageenase.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.19 n.1 20162016-01-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000100001en10.1016/j.ejbt.2015.10.001 |
| institution |
Scielo Chile |
| collection |
Scielo Chile |
| language |
English |
| topic |
Carrageenase Characterization Immobilization Nanoparticles |
| spellingShingle |
Carrageenase Characterization Immobilization Nanoparticles Xiao,Anfeng Xu,Caiyun Lin,Yan Ni,Hui Zhu,Yanbing Cai,Huinong Preparation and characterization of κ-carrageenase immobilized onto magnetic iron oxide nanoparticles |
| description |
Background Carboxyl-functionalized magnetic nanoparticles were synthesized via chemical co-precipitation method and modified with oleic acid which was oxidized by potassium permanganate, and κ-carrageenase from Pseudoalteromonas sp. ASY5 was subsequently immobilized onto them. The immobilization conditions were further optimized, and the characterizations of the immobilized κ-carrageenase were investigated. Results The κ-carrageenase was immobilized onto magnetic iron oxide nanoparticles, and the bonding was verified by Fourier transform infrared spectroscopy. The optimal conditions for κ-carrageenase immobilization were 2.5% (w/v) glutaraldehyde, 13.9 U κ-carrageenase for 20 mg of magnetic nanoparticles, a 2-h cross-linking time, and a 2-h immobilization time at 25°C. Under these conditions, the activity of the immobilized enzyme and the enzyme recovery rate were 326.0 U · g- 1 carriers and 46.9%, respectively. The properties of the immobilized κ-carrageenase were compared with those of the free enzyme. The optimum temperatures of the free and immobilized κ-carrageenase were 60 and 55°C, respectively, and the optimum pH of κ-carrageenase did not change before and after immobilization (pH 7.5). After immobilization, κ-carrageenase exhibited lower thermal stability and improved pH stability, as well as better storage stability. The immobilized κ-carrageenase maintained 43.5% of the original activity after being used 4 times. The kinetic constant value (Km) of κ-carrageenase indicates that the immobilized enzyme had a lower binding affinity for the substrate. Conclusions Under optimal conditions, the activity of the immobilized enzyme and enzyme recovery rate were 326.0 U · g- 1·κ-carrageenase-CMNPs and 46.9%, respectively. The thermal, pH, and storage stabilities of κ-carrageenase-CMNPs were relatively higher than those of free κ-carrageenase. |
| author |
Xiao,Anfeng Xu,Caiyun Lin,Yan Ni,Hui Zhu,Yanbing Cai,Huinong |
| author_facet |
Xiao,Anfeng Xu,Caiyun Lin,Yan Ni,Hui Zhu,Yanbing Cai,Huinong |
| author_sort |
Xiao,Anfeng |
| title |
Preparation and characterization of κ-carrageenase immobilized onto magnetic iron oxide nanoparticles |
| title_short |
Preparation and characterization of κ-carrageenase immobilized onto magnetic iron oxide nanoparticles |
| title_full |
Preparation and characterization of κ-carrageenase immobilized onto magnetic iron oxide nanoparticles |
| title_fullStr |
Preparation and characterization of κ-carrageenase immobilized onto magnetic iron oxide nanoparticles |
| title_full_unstemmed |
Preparation and characterization of κ-carrageenase immobilized onto magnetic iron oxide nanoparticles |
| title_sort |
preparation and characterization of κ-carrageenase immobilized onto magnetic iron oxide nanoparticles |
| publisher |
Pontificia Universidad Católica de Valparaíso |
| publishDate |
2016 |
| url |
http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000100001 |
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| _version_ |
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