Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA)

Milosavić, Nenad; Prodanović, Radivoje; Jovanović, Slobodan; Vujčić, Zoran

doi:10.1016/j.enzmictec.2006.10.018

Cited by 41 publications

(29 citation statements)

References 19 publications

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“…Coupling reactions involving epoxy groups and -NH 2 groups of enzymes had been widely reported [19][20][21]. The microspheres (1.0 g) were equilibrated in 50 ml phosphate buffer (0.1 M, pH 7.0) for 24 h. It was then transferred to the same fresh buffer (50 ml) containing CRL (0.1 g).…”

Section: Immobilization Of Lipasementioning

confidence: 99%

Characterization of Candida rugosa lipase immobilized onto magnetic microspheres with hydrophilicity

Yang

Bai

et al. 2008

Process Biochemistry

139

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Section: Immobilization Of Lipasementioning

confidence: 99%

Characterization of Candida rugosa lipase immobilized onto magnetic microspheres with hydrophilicity

Yang

Bai

et al. 2008

Process Biochemistry

139

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“…[2] For this purposes, enzymes have been immobilized onto solid supports materials, in order to improve the reusability properties of enzymes. [3] There have been intensive works to immobilize amyloglucosidase onto various matrices by using different methods such as, adsorption onto magnetic polystyrene beads [4], activated charcoal [2], macrostructured carbonized ceramics [5] and nonporous polystyrene/poly(sodium styrene sulfonate) microspheres [6]; covalent binding to polyglutaraldehyde-activated gelatin [7], macroporous poly(GMA-co-EGDMA) [3], magnetic nanoparticles [8]; and entrapment in alginate [9] and LentiKats®. [10] Enzymes have superior properties for industrial applications such as; they can catalyze the reactions under mild conditions with very high activity, also they have high enantio-and regio-selectivity and specificity towards their substrates.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of amyloglucosidase onto macroporous cryogels for continuous glucose production from starch

Uygun

Akduman

Ergönül

et al. 2015

Journal of Biomaterials Science, Polymer Edition

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Poly(methyl methacrylate-glycidyl methacrylate) [Poly(MMA-GMA)] cryogels were synthesized using monomers of methylmethacrylic acid and epoxy group bearing GMA via radical cryopolymerization technique. Synthesized cryogels were used for the immobilization of amyloglucosidase to the cryogel surface using epoxy chemistry. Characterizations of the free and immobilized amyloglucosidase were carried out by comparing the optimum and kinetic parameters of enzymes. For this, pH and temperature profiles of free and immobilized preparation were studied and, it was found that, optimum pH of enzyme was not change upon immobilization (pH 5.0), while optimum temperature of the enzyme shifted 10 °C to warmer region after immobilization (optimum temperatures for free and immobilized enzyme were 55 and 65 °C, respectively). Kinetic parameters of free and immobilized enzyme were also investigated and Km values of free and immobilized amyloglucosidase were found to be 2.743 and 0.865 mg/mL, respectively. Vmax of immobilized amyloglucosidase was found to be (0.496 µmol/min) about four times less than that of free enzyme (2.020 µmol/min). Storage and operational stabilities of immobilized amyloglucosidase were also studied and it was showed that immobilized preparation had much more stability than free preparation. In the present work, amyloglucosidase immobilized poly(MMA-GMA) cryogels were used for continuous glucose syrup production from starch for the first time. Efficiency of immobilized enzyme was investigated and released amount of glucose was found to be 2.54 mg/mL at the end of the 5 min of hydrolysis. The results indicate that the epoxy functionalized cryogels offer a good alternative for amyloglucosidase immobilization applications with increased operational and thermal stability, and reusability. Also, these cryogels can be used for immobilization of other industrially valuable enzymes beyond amyloglucosidase.

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“…Currently, a large variety of matrixes have been used in immobilized glucoamylase [7,[12][13][14]. The enzymes are linked to an insoluble matrix by chemical bonds, which generally produce very stable derivatives in which enzyme leakage is prevented.…”

Section: Introductionmentioning

confidence: 99%

Preparation of Cross-Linked Glucoamylase Aggregates Immobilization by Using Dextrin and Xanthan Gum as Protecting Agents

Jia

et al. 2016

Catalysts

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Abstract:In this paper glucoamylase from Aspergillus niger was immobilized by using a modified version of cross-linked enzyme aggregates (CLEA). The co-aggregates were cross-linked with glutaraldehyde; meanwhile dextrin and xanthan gum as protecting agents were added, which provides high affinity with the enzyme molecules. The immobilized glucoamylase was stable over a broad range of pH (3.0-8.0) and temperature (55-75˝C); dependence shows more catalytic activity than a free enzyme. The thermostability, kinetic behavior, and first-order inactivation rate constant (k i ) were investigated. The two types of protector made the immobilized glucoamylase more robust than the free form. Both of the immobilized enzymes have excellent recyclability, retaining over 45% of the relative activity after 24 runs. In addition, immobilized enzymes reduced only 40% of the initial activity after three months by the storability measure, indicating high activity.

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Immobilization of glucoamylase via its carbohydrate moiety on macroporous poly(GMA-co-EGDMA)

Cited by 41 publications

References 19 publications

Characterization of Candida rugosa lipase immobilized onto magnetic microspheres with hydrophilicity

Characterization of Candida rugosa lipase immobilized onto magnetic microspheres with hydrophilicity

Immobilization of amyloglucosidase onto macroporous cryogels for continuous glucose production from starch

Preparation of Cross-Linked Glucoamylase Aggregates Immobilization by Using Dextrin and Xanthan Gum as Protecting Agents

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