Immobilization of bromelain onto porous copoly(γ-methyl-l-glutamate/l-leucine) beads

Yodoya, Shinya; Takagi, Tetsuya; Kurotani, Michiyoshi; Hayashi, Takanori; Furuta, Mamoru; Oka, M.; Hayashi, Toshio

doi:10.1016/s0014-3057(02)00192-1

Cited by 35 publications

(18 citation statements)

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“…This shift could be explained as multi-point ionic interaction between enzymes and polymeric matrix due to the activation energy of the enzyme to reorganize an optimum conformation for binding to its substrate. One of the main reasons for enzyme immobilization is the anticipated increase in its stability to various deactivating force due to restricted conformational mobility of the molecules following immobilization [22][23][24].…”

Section: Resultsmentioning

confidence: 99%

A new method for immobilization of acetylcholinesterase

Tümtürk

Şahin

Demirel

2007

Bioprocess Biosyst Eng

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A new method for immobilization of acetylcholinesterase (AChE) to alginate gel beads by activating the carbonyl groups of alginate using carbodiimide coupling agent has been successfully developed. Maximum reaction rate (V (max)) and Michaelis-Menten constant (K (m)) were determined for the free and binary immobilized enzyme. The effects of pH, temperature, storage stability, reuse number and thermal stability on the free and immobilized AChE were also investigated. For the free and binary immobilized enzyme on the Ca-alginate gel beads, optimum pH values were found to be 7 and 8, respectively. Optimum temperatures for the free and immobilized enzyme were observed to be 30 and 35 degrees C, respectively. Upon 60 days of storage the preserved activity of free and immobilized enzyme were found as 4 and 68%, respectively. In addition, reuse number, and thermal stability of the free AChE were increased by as a result of binary immobilization.

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Section: Resultsmentioning

confidence: 99%

A new method for immobilization of acetylcholinesterase

Tümtürk

Şahin

Demirel

2007

Bioprocess Biosyst Eng

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“…Moreover, the immobilized β-glucosidase was found to possess 75% of its original activity, whereas the free enzyme remained at 35% at 60 °C. It was obvious that the immobilized β-glucosidase was more stable than the free β-glucosidase due to the increased rigidity of the enzyme after immobilization (Chiou and Wu 2004;Jung et al 2011;Yodoya et al 2003).…”

Section: Thermal Stabilitymentioning

confidence: 99%

Immobilization of β-glucosidase onto Magnetic Nanoparticles and Evaluation of the Enzymatic Properties

et al. 2013

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This paper reports on a novel and efficient β-glucosidase immobilization method using magnetic Fe 3 O 4 nanoparticles as a carrier. Based on response surface methodology, the optimal immobilization conditions obtained were: glutaraldehyde (GA) concentration, 0.20%; enzyme concentration, 50.25 μg/mL; cross-linking time, 2.21 h; and the maximum activity recovery reached 89.35%. The magnetic immobilized enzyme was characterized by Fourier transform infrared spectroscopy (FTIR), transmission electron microscope (TEM), and vibrating sample magnetometer (VSM). FTIR revealed that β-glucosidase was successfully immobilized on the magnetic nanoparticles. TEM showed that enzyme-magnetic nanoparticles possessed nano-scale size distribution. VSM confirmed that the enzyme-magnetic nanoparticles were superparamagnetic. The properties of the immobilized β-glucosidase were improved, and the immobilized β-glucosidase exhibited wider pH and temperature ranges of activation, higher accessibility of the substrate, better thermal stability, and better storage stability than that of the free enzyme. The enzyme-magnetic nanoparticles could be separated magnetically for easy reuse. Immobilization of β-glucosidase onto the magnetic nanoparticles has the potential for industrial application.

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“…Compared with the free laccase, the immobilized laccase provided a broader profile and its relative activity maintained more than 78% in the temperature range between 40°C and 70°C. The increased stability of the immobilized laccase was due to the restricted conformational mobility of the molecules after immobilization (Yodoya et al, 2003).…”

Section: Property Of Immobilized Laccasementioning

confidence: 99%