Immobilization of catalase onto chitosan and cibacron blue F3GA attached chitosan beads

Çetinus, Şenay Akkuş; Öztop, H. Nursevin; Saraydın, Dursun

doi:10.1016/j.enzmictec.2007.03.014

Cited by 46 publications

(24 citation statements)

References 21 publications

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“…These parameters are presented in Table 3. As expected, the K m value increased with immobilization (Çetinus Akkuş and Öztop 2003; Çetinus Akkuş and others 2007). This result can be attributed to the limited accessibility of sucrose molecules to the active sites of the immobilized invertase as a result of conformational change invertase caused by the immobilization and/or can be the hindrance due to hydrogel network.…”

Section: Resultssupporting

confidence: 70%

Acrylamide–Sepiolite Based Composite Hydrogels for Immobilization of Invertase

Öztop¹,

Hepokur²,

Saraydın³

2009

Journal of Food Science

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Novel composite hydrogels, poly(acrylamide)-sepiolite (PAS), poly(acrylamide/acrylic acid)-sepiolite (PAAS), and poly(acrylamide/itaconic acid)-sepiolite (PAIS) were prepared and used for the immobilization of invertase. The parameters of equilibrium swelling, diffusional exponent, and diffusion coefficient of these hydrogels were calculated from swelling experiments. Invertase was immobilized onto PAS, PAAS, and PAIS and immobilized invertases (PASI, PAASI, and PAISI) were prepared. Optimum pH values for free invertase, PASI, PAASI, and PAISI are found to be 5, 5.5, 4.5, and 6, respectively, and the optimum temperatures were 30, 50, 50, and 35 degrees C for free invertase PASI, PAASI, and PAISI. It was found that K(m) values of free invertase, PASI, PAASI, and PAISI were 11.3, 41.0, 94.5, and 56.0 mM, respectively. V(max) values were 2 mumol/min for free invertase, 8.10 mumol/min for PASI, 1.30 mumol/min for PAASI, and 0.42 mumol/min for PAISI, respectively. The invertase immobilized hydrogels showed excellent, temperature, storage, and operational stability.

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Section: Resultssupporting

confidence: 70%

Acrylamide–Sepiolite Based Composite Hydrogels for Immobilization of Invertase

Öztop¹,

Hepokur²,

Saraydın³

2009

Journal of Food Science

Self Cite

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“…As expected, the K m value increased with immobilization (Table 2). 17,18 This result can be attributed to the limited accessibility of the sucrose molecules to the active sites of the immobilized invertase, as a result of the conformational change that invertase suffer by the immobilization or to the hindrance due to the hydrogel network. It was found that the V max value of PM-I and PM/MA-I were higher than those of the free invertase (Table 2).…”

Section: Pm/mamentioning

confidence: 99%

The Properties of Immobilized Invertase Onto a New Support Material; Poly(Methacrylamide/Maleic Acid) Copolymeric Hydrogel

2018

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Poly (methacrylamide / maleic acid) PM/MA and poly (methacrylamide) PM hydrogels were prepared aiming to be used as a support for invertase. Spectrophotometric, thermal analysis methods, swelling and diffusion experiments were used for the characterization of hydrogels. The swelling of PM/MA was higher than that of PM in water. The diffusion of water within the hydrogel was found to be non-Fickian. Invertase was immobilized onto PM and PM/MA (samples named PM-I and PM/MA-I respectively). The optimum pH values were found to be; 6.0, 5.0 and 5.5 for free invertase, PM-I and PM/MA-I respectively. The optimum temperature values were found to be 30 °C, 35 °C and 40 °C for free invertase, PM-I and PM/MA-I respectively. The Michaelis constant (Km) and maximum velocity of the enzymes (Vmax) were Km: 11,75 mM, Vmax: 1,95 μmol min−1 for free invertase, Km: 67,24 mM, Vmax: 60,6 μmol min−1 for PM-I and Km: 74,55 mM, Vmax: 18,12 μmol min−1 for PM/MA-I. PM/MA-I showed excellent thermal, operational and storage stability.

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“…Cellulase was immobilized on chitosan with glutaraldehyde as a cross-linking agent by the covalent linkage method (Çetinus et al, 2007;Altun and Cetinus, 2007;Juang, 2007a, 2007b).…”

Section: Preparation Of Immobilized Cellulasementioning

confidence: 99%