Influence of the immobilization process on the activity of β-galactosidase bound to Nylon membranes grafted with glycidyl methacrylate

El-Masry, M.M.; Maio, Anna De; Martelli, Pier Luigi; Casadio, Rita; Moustafa, A. B.; Rossi, Sergio; Mita, D.G.

doi:10.1016/s1381-1177(01)00061-3

Cited by 36 publications

(24 citation statements)

References 28 publications

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“…Higher K m result (∼187 mM) for the same immobilized enzyme was obtained by other authors [24]. It should be taken into consideration that the modification of enzyme's structure may result in the loss of its specificity towards lactose.…”

Section: Kinetic Constants Of Free and Immobilized β-Galactosidasesupporting

confidence: 71%

“…The modified gel revealed the presence of carbonyl groups at 1,720 cm −1 which were expected to be for the glutaraldehyde-free aldehydic groups. The presence of glutaraldehyde -C=O was also confirmed visually, as it reacted with the chitosan -NH 2 group forming Schiff's base and changing color from pale yellow to brown-red according to the chitosan's pH [24]. The FTIR bands also revealed a decrease in intensity and a shift of the carrageenan -OSO 3 − absorption band from 1,446 to 1,390 cm −1 after reaction with chitosan, which was derived from the ionic interaction between the carrageenan and the chitosan.…”

Section: Carrageenan Coated With Chitosan Elucidation Structurementioning

confidence: 80%

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Lactose Hydrolysis by β-Galactosidase Covalently Immobilized to Thermally Stable Biopolymers

Elnashar

Yassin²

2008

Appl Biochem Biotechnol

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Lactose has been hydrolyzed using covalently immobilized beta-galactosidase on thermally stable carrageenan coated with chitosan (hydrogel). The hydrogel's mode of interaction was proven by Fourier transform infrared spectroscopy, differential scanning calorimetry (DSC), and Schiff's base formation. The DSC thermogram proved the formation of a strong polyelectrolyte complex between carrageenan and chitosan followed by glutaraldehyde as they formed one single peak. The modification of carrageenan improved the gel's thermal stability in solutions from 35 degrees C to 95 degrees C. The hydrogel has been proven to be efficient for beta-galactosidase immobilization where 11 U/g wet gel was immobilized with 50% enzyme loading capacity. Activity and stability of free and immobilized beta-galactosidase towards pH and temperature showed marked shifts in their optimum pH from 4.5-5 to 5-5.5 and temperature from 50 degrees C to 45-55 degrees C after immobilization, which reveals higher catalytic activity and reasonable stability at wider pHs and temperatures. The apparent K(m) of the immobilized enzyme increased from 13.2 to 125 mM, whereas the V(max) increased from 3.2 to 6.6 micromol/min compared to the free enzyme, respectively. The free and immobilized enzymes showed lactose conversion of 87% and 70% at 7 h, respectively. The operational stability showed 97% retention of the enzyme activity after 15 uses, which demonstrates that the covalently immobilized enzyme is unlikely to leach. The new carrier could be suitable for immobilization of other industrial enzymes.

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Section: Kinetic Constants Of Free and Immobilized β-Galactosidasesupporting

confidence: 71%

Section: Carrageenan Coated With Chitosan Elucidation Structurementioning

confidence: 80%

Lactose Hydrolysis by β-Galactosidase Covalently Immobilized to Thermally Stable Biopolymers

Elnashar

Yassin²

2008

Appl Biochem Biotechnol

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show abstract

“…Such enhancement in enzyme stability was due to the rigidity provided by immobilization to the enzyme. El-Masry et al [28] previously showed that ␤ galactosidase from A. oryzae immobilized via diazotization on nylon membranes grafted with glycidyl methacrylate had a higher temperature optimum than its soluble counterpart. This increased activity at higher temperatures showed significant stabilization against heat induced inactivation (Fig.…”

Section: Discussionmentioning

confidence: 99%

Immobilization of Aspergillus oryzae β galactosidase on zinc oxide nanoparticles via simple adsorption mechanism

Husain

Ansari

Alam

et al. 2011

International Journal of Biological Macromolecules

133

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“…BGAL from A. oryzae immobilized via diazotization on nylon membranes had a higher temperature optimum than its soluble counterpart [39]. The temperature optimum of the native enzyme remained unchanged upon the immobilization of BGAL from K. fragilis on cellulose beads [21].…”

Section: Effects Of Ph and Temperature On The Catalytic Activitymentioning

confidence: 95%

Immobilization of β-d-galactosidase from Kluyveromyces lactis on functionalized silicon dioxide nanoparticles: Characterization and lactose hydrolysis

Verma

Barrow

Kennedy³

et al. 2012

International Journal of Biological Macromolecules

106

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Influence of the immobilization process on the activity of β-galactosidase bound to Nylon membranes grafted with glycidyl methacrylate

Cited by 36 publications

References 28 publications

Lactose Hydrolysis by β-Galactosidase Covalently Immobilized to Thermally Stable Biopolymers

Lactose Hydrolysis by β-Galactosidase Covalently Immobilized to Thermally Stable Biopolymers

Immobilization of Aspergillus oryzae β galactosidase on zinc oxide nanoparticles via simple adsorption mechanism

Immobilization of β-d-galactosidase from Kluyveromyces lactis on functionalized silicon dioxide nanoparticles: Characterization and lactose hydrolysis

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