Immobilization of catalase on chitosan film

Çetinus, Şenay Akkuş; Öztop, H. Nursevin

doi:10.1016/s0141-0229(99)00189-1

Cited by 75 publications

(26 citation statements)

References 6 publications

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“…It was found that the quantity of immobilized trypsin was 6 mg/g dried support, which is of the same order of magnitude of covalently immobilized trypsin and other proteases to other materials, such as porous zirconia (Huckel et al, 1996) and a chitosan film (Akkus Centinus, Oztop, 2000), and is characteristic of supports that have low specific surface area.…”

Section: Quantity Of Immobilized Trypsinmentioning

confidence: 85%

Cotton gauze bandage: a support for protease immobilization for use in biomedical applications

Seabra¹,

Gil²

2007

Rev. Bras. Cienc. Farm.

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Section: Quantity Of Immobilized Trypsinmentioning

confidence: 85%

Cotton gauze bandage: a support for protease immobilization for use in biomedical applications

Seabra¹,

Gil²

2007

Rev. Bras. Cienc. Farm.

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“…from which it can be seen that the K m value of ICATG was smaller than that of the free catalase. Çetinus et al 22 immobilized bovine liver catalase on glutaraldehyde pretreated chitosan films. The catalytic efficiencies (k cat /K m ) of free catalase and ICATG were 1.4×10 3 and 2.9 m 3 s −1 mol −1 , respectively.…”

Section: Effect Of Immobilization On the Kinetic Constantsmentioning

confidence: 99%

Immobilization and characterization of bovine liver catalase on eggshell

Alptekin

Tükel

Yıldırım

2008

JSCS

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Bovine liver catalase immobilized on eggshell particles was characterized and the reusability of the immobilized catalase was investigated in a batch type reactor. For immobilized catalase onto ground eggshell (ICATG), the optimum initial amount of catalase was 85 mg g -1 of eggshells, the optimum pH was 6.0 (75 mM citrate buffer) and the temperature was 30 °C. The V max and K m values of ICATG were determined as 29.1±1.2 U/mg of protein and 41.9±2.7 mM, respectively. The reusability of ICATG was tested and the remaining activity of ICATG was found to be 73 % of the initial activity after 80 cycles of batch operation. The amount of catalase bound onto the carrier was estimated by using the results of induced coupled plasma measurements. The catalytic efficiencies (k cat /K m ) of free catalase and ICATG were found to be 1.4×10 6 and 2.8×10 3 dm 3 s -1 mol -1 , respectively. Catalase immobilization onto eggshell is economic and has good reusability. Hence, it can be concluded that eggshell is an efficient carrier for immobilizing catalase.

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“…It has also been widely used as a support for enzyme immobilization because it offers many advantages, including low cost, good biocompatibility, low nonspecific adsorption, and ease of fabrication into various forms (powders, gel beads, fibers, capsules, and membranes) 3. Enzymes such as catalase,4 tyrosinase,5 dextranase,6 and β‐galactosidase7 have been immobilized on commercial crustacean chitosan.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of α‐amylase onto chitosan and its amino acid condensation adducts

El‐Ghaffar

Hashem

2009

J of Applied Polymer Sci

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a-Amylase from Bacillus subtilis was immobilized on insoluble chitosan and its amino acid (L-glutamic acid and 4-aminobutyric acid) condensation adducts with the direct covalent attachment method and with glutaric dialdehyde (GDA) as a crosslinking agent. The immobilization process was carried out at 25 C and pH 6.9, and the maximum retained activity was obtained with 3 mg of a-amylase. The properties of the immobilized a-amylase were investigated and compared with those of the free aamylase. For the assays carried out via the crosslinking method at 25 C and pH 6.9, the retained activities were found to be 68.59, 97.36, and 79.50% for chitosan, chitosan-L-glutamic acid, and chitosan-4-aminobutyric acid crosslinked with 1% GDA, respectively. The immobilized a-amylase had better stability and higher retained activities with respect to the pH, temperature, and storage stability than the free a-amylase. In the repeated-use experiments, the a-amylase immobilized with chitosan-GDA (1%) retained about 46.45% of its original activity after 25 uses. In contrast, the activities of a-amylase immobilized on chitosan-L-glutamic acid-GDA (1%) and chitosan-4-aminobutyric acid-GDA (1%) did not change after 11 and 8 uses, respectively. The retained activities after 25 uses were 79 and 71% with respect to the original activity for the aforementioned carriers.

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Immobilization of catalase on chitosan film

Cited by 75 publications

References 6 publications

Cotton gauze bandage: a support for protease immobilization for use in biomedical applications

Cotton gauze bandage: a support for protease immobilization for use in biomedical applications

Immobilization and characterization of bovine liver catalase on eggshell

Immobilization of α‐amylase onto chitosan and its amino acid condensation adducts

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