Comparison of pectolytic enzymes covalently bound to synthetic ion exchangers using different methods of binding

Kmínková, M.; Kučera, Jiří

doi:10.1016/0141-0229(83)90096-0

Cited by 36 publications

(8 citation statements)

References 7 publications

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“…Therefore, it is necessary to produce pectic oligosaccharides in bioreactors based on immobilized pectinase. Until now, pectinase has been immobilized on various supports including nylon (Lozano et al 1987), ionexchange resin (Kminkova and Kucera 1983), silk (Zhu et al 1998), and chitin (Iwasaki et al 1998). However, there have been few studies on the details of the immobilizing conditions and the significant losses of activity that occur during immobilization.…”

Section: Introductionmentioning

confidence: 98%

Optimization of covalent immobilization of pectinase on sodium alginate support

Wang

et al. 2007

Biotechnol Lett

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Pectinase was immobilized on a sodium alginate support using glutaraldehyde and retained 66% activity. The optimal pH for activity shifted from 3.0 to 3.5 after immobilization; however, the optimum temperature remained unchanged at 40 degrees C. The immobilized enzyme also had a higher thermal stability and reusability than the free enzyme, and retained 80% of initial activity after 11 batch reactions.

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Section: Introductionmentioning

confidence: 98%

Optimization of covalent immobilization of pectinase on sodium alginate support

Wang

et al. 2007

Biotechnol Lett

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“…The immobilization techniques provide a promising approach for enzymes to retain their stability, make the use of expensive enzymes economically viable and enhance their reusability. 2 To date, the pectinase enzyme has been immobilized on various supports such as Nylon, 3 ion-exchange resins, 4 silk, 5 g-Al 2 O 3 , 6 and macroporous polyacrylamide. 1 Immobilization of pectinase onto nanoparticles bearing high specific surface area increases their activity in the catalysis.…”

Section: Introductionmentioning

confidence: 99%

Magnetite Nanoparticles Immobilized Pectinase: Preparation, Characterization and Application for the Fruit Juices Clarification

Mosafa

Shahedi

2013

J Chinese Chemical Soc

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In this work, pectinase was immobilized on the surface of silica-coated magnetite nanoparticles via covalent attachment. The magnetite-immobilized enzyme was characterized by Fourier transform infrared spectroscopy, X-ray powder diffraction, scanning electron microscopy and vibrating sample magnetometery techniques. Response Surface Methodology using Minitab Software was applied for statistical designing of operating conditions in order to immobilize pectinase on magnetic nanoparticles. The optimal conditions were obtained at 30 o C and pH 5.5 with 42.97 µl pectinase for 2 h. The immobilization yield was 50.6% at optimized conditions. Compared to the free pectinase, the immobilized pectinase was found to exhibit enhanced enzyme activity, better tolerance to the variation of pH and temperature, and improved storage stability. Both free and immobilized samples reduced the viscosity of apple juice from 1.12 to 0.88 and 0.92 mm 2 s -1 , respectively, after 30 min at their optimum temperature. Furthermore, the immobilized enzyme could be reused six consecutive cycles and the efficiency loss in viscosity reduction was found to be only 8.16%.

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“…Its immobilization and application like bioreactor in continuous industrial processes, therefore, could offer considerable advantage in biotechnology processes [14,15]. However, in this kind of enzymatic reactor, there are large diffusion problems [16], and the mass transfer is primordial to obtain a good reproducibility.…”

Section: Introductionmentioning

confidence: 99%