Immobilization of α-amylase from Bacillus licheniformis on developed support using microbial transglutaminase

Wang, Hong Wei; Kim, In Hae; Park, Chang-Su; Lee, Jae-Hwa

doi:10.1007/s11814-008-0131-1

Cited by 7 publications

(1 citation statement)

References 17 publications

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“…Enzymes can be immobilized by various methods, including physical adsorption, entrapment and covalent binding (Wang et al 2008;Tran and Balkus, 2011;Dicosimo et al 2013;Sheldon and van Pelt, 2013). Covalent bonding methods have been widely studied because of the high bonding strength that occurs between the enzyme and the solid support (Park et al 2001;Soares et al 2003;Lee et al 2007).…”

Section: Effects Of Immobilizing Methodsmentioning

confidence: 99%

Optimal immobilization of β-glucosidase into chitosan beads using response surface methodology

Zhou¹,

Wang²,

Wu³

et al. 2013

Electron. J. Biotechnol.

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Background: β-Glucosidase is known as an effective catalyst for the hydrolysis of various glycosides and immobilization is one of the most efficient strategies to improve its activity recovery and properties. Results: Crosslinking-adsorption-crosslinking method was employed to immobilize β-glucosidase into chitosan beads and response surface methodology (RSM) was used to optimize the immobilized conditions of the maximum activity recovery. Enzyme concentration and adsorption time were found to be significant influence factors, and the maximum activity recovery (50.75%) obtained from response surface methodology was in excellent agreement with experimental value (50.81%). Furthermore, various characteristics of immobilized β-glucosidase were evaluated. Compared to the free β-glucosidase, the immobilized enzyme exhibited broader pH and temperature ranges, enhanced thermal stability, better storage stability and reusability and higher accessibility of the substrate to the immobilized β-glucosidase. Conclusion: Response surface methodology (RSM) was proved to be much economical for optimum immobilization of β-glucosidase into chitosan beads.

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Section: Effects Of Immobilizing Methodsmentioning

confidence: 99%

Optimal immobilization of β-glucosidase into chitosan beads using response surface methodology

Zhou¹,

Wang²,

Wu³

et al. 2013

Electron. J. Biotechnol.

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Improvement of the catalytic performance of immobilized penicillin acylase through assembly of macromolecular reagents in nanopore to create a crowding environment

Zhou

Wang

et al. 2009

Korean J. Chem. Eng.

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Macromolecular reagents were co-assembled with penicillin acylase (PA) and immobilized in mesocellular siliceous foams (MCFs) to resemble living cells. Types and concentrations of macromolecules were studied. The catalytic characteristic and stability of PA preparations were also investigated. PA assembled with dextran 10 k in MCFs showed maximum specific activity, 1.32-fold of that of the solely immobilized PA. The optimum pH of dextran and BSA derivatives shifted to neutrality, and the optimum temperature increased by 10 o C. Also, Km of BSA derivative of PA declined 56.7% compared to solely immobilized PA, while the Kcat/Km of PA assembled with BSA was enhanced to 147%. After incubation at 50 o C for 6 h, residual activity of PA assembled with BSA exhibited 53.0%. The ficoll derivative showed 82.8% of its initial activity at 4 o C after 8-week storage. The results indicated that macromolecular reagents assembled with PA in MCFs could dramatically improve the catalytic performance and stability of im-mobilized enzyme.

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Enhancement of glucose isomerase activity by pretreatment with substrates prior to immobilization

Yue

Kim

Park

et al. 2011

Korean J. Chem. Eng.

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To improve the activity of covalently immobilized glucose isomerase, the effects of glucose isomerase pretreatment with D-glucose or D-xylose prior to immobilization were investigated. Glucose isomerase was pretreated with D-glucose or D-xylose to prevent loss of activity, followed by immobilization on a silica gel surface. Pretreated immobilized glucose isomerase (PIGI) with 2.0 M D-xylose (194.0 U/g matrix) had higher activity than PIGIs with D-glucose. The optimal temperature, reaction time, and agitation speed for glucose isomerase pretreatment were 60 o C, 45 min, and 200 rpm, respectively. Consequently, the activity of PIGI with D-xylose was 254.9 U/g matrix, which is about 2.5 times higher than that of non-pretreated immobilized glucose isomerase (non-PIGI). PIGI also showed better reusability than non-PIGI, with 75.2% of its original activity being retained after 10 reuses.

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Immobilization of α-amylase from Bacillus licheniformis on developed support using microbial transglutaminase

Cited by 7 publications

References 17 publications

Optimal immobilization of β-glucosidase into chitosan beads using response surface methodology

Optimal immobilization of β-glucosidase into chitosan beads using response surface methodology

Improvement of the catalytic performance of immobilized penicillin acylase through assembly of macromolecular reagents in nanopore to create a crowding environment

Enhancement of glucose isomerase activity by pretreatment with substrates prior to immobilization

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