A novel method for the immobilization of glucoamylase onto polyglutaraldehyde-activated gelatin

Tanrıseven, Aziz; Ölçer, Zehra

doi:10.1016/j.bej.2007.10.011

Cited by 49 publications

(41 citation statements)

References 20 publications

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“…A concentration of 12% glutaraldehyde gave the highest residual RSDA activity; therefore, further studies were carried out using this concentration. Glutaraldehyde forms highly reactive functional groups, which could be detrimental to enzyme activity and/or stability if inadequate concentrations are applied (Tanriseven and Ö lçer 2008). Application of glutaraldehyde quantities below optimum could result to the formation of insufficient amount of aldehyde groups necessary for enzyme rigidification.…”

Section: Resultsmentioning

confidence: 98%

“…The activated carrier was washed repeatedly with distilled water for 10 min and reacted with glutaraldehyde (10 ml, 25% w/v) in acetate buffer (10 ml, 25 mM, pH 6) for 30 min at 30°C. The untreated glutaraldehyde was removed from activated carrier by washing repeatedly with acetate buffer (Tanriseven and Ö lçer 2008).…”

Section: Polyglutaraldehyde Activation Of Carriermentioning

confidence: 99%

“…Soluble polyglutaraldehyde was prepared by the method of Tanriseven and Ö lçer (2008). Glutaraldehyde solution (20 ml 25% w/v, pH 10.5) was polymerized by the addition of 0.6 ml of 1 M NaOH solution and incubating at room temperature for 20 min.…”

Section: Preparation Of Soluble Polyglutaraldehyde Solutionmentioning

confidence: 99%

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Stabilization of a raw starch digesting amylase from Aspergillus carbonarius via immobilization on activated and non-activated agarose gel

Nwagu

Okolo

Aoyagi

2011

World J Microbiol Biotechnol

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Applications of raw starch digesting amylases (RSDAs) are limited due to instability, product inhibition of enzyme and contamination. RSDA from Aspergillus carbonarius was stabilized through immobilization on agarose gel by adsorption, spontaneous crosslinking and conjugation using glycidol, glutaraldehyde or polyglutaraldehyde. Effects of immobilization on kinetics, catalytic, storage and operational stability of immobilized enzyme were evaluated. Polyglutaraldehyde activated agarose RSDA (PGAg-RSDA) gave the highest immobilization yield (100%) with expressed activity of 86.7% while that of glycidol activated RSDA (GlyAg-RSDA) was 80.4%. A shift in pH from optimum of 5 for the soluble enzyme to 6 for RSDA adsorbed on agarose followed by crosslinking with glutaraldehyde (AgRSDA-CROSS) and simultaneous adsorption and crosslinking (AgRSDA-RET), and pH 7 for PGAg-RSDA was seen. PGAg-RSDA and AgRSDA-CROSS were most pH stable and retained over 82% of their activities between pH 3.5 and 9 compared to 59% for the soluble enzyme. Thermoinactivation studies showed that immobilized RSDAs with the exception of GAg-RSDA retained over 90% of their activities at 60°C for 120 min while soluble enzyme retained only 76% activity under the same condition. AgRSDA-CROSS, PGAg-RSDA, Gly-RSDA and GAg-RSDA retained approximately 100% of their activities after 30 days storage at 4°C. GlyAg-RSDA retained 99.6%, PGAg-RSDA 94%, AgRSDA-CROSS 90%, GAg-RSDA 86.5% and Ag-RSDA-RET 80% activity after 10 batch reactions. Immobilization stabilized RSDA and permits processing at higher temperatures to reduce contamination.

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Section: Resultsmentioning

confidence: 98%

Section: Polyglutaraldehyde Activation Of Carriermentioning

confidence: 99%

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Stabilization of a raw starch digesting amylase from Aspergillus carbonarius via immobilization on activated and non-activated agarose gel

Nwagu

Okolo

Aoyagi

2011

World J Microbiol Biotechnol

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“…Maltose and maltohexaose were used as active site conformational templates during the harsh cross-linking process [33]. Compared with conventional methods (i.e., covalent or non-covalent combination, embedding, CLEC), the immobilized enzyme and carrier-bound CLEA of glucoamylase with tailor-made properties (e.g., enhanced activity, thermostability, and storage stability) have been designed by a simple and effective technology [31,[34][35][36]. Two types of immobilized enzyme exhibited the expected increase in stability and tolerance compared to the native enzyme.…”

Section: Discussionmentioning

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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“…Naganagouda et al (2007) immobilized α-galactosidase in a mixture of gelatin, sodium alginate and glycerol crosslinked with glutaraldehyde 5%, obtaining 64.3% immobilization. Tanriseven and Olcer (2008) immobilized glucoamylase in gelatin cross-linked with polyglutaraldeyde and obtained an immobilization yield of 85%. …”

Section: Immobilization Yield (Iy)mentioning

confidence: 99%

Influence of bloom number and plastifiers on gelatin matrices produced for enzyme immobilization

Kempka

Souza

et al. 2014

Braz. J. Chem. Eng.

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-In this study the immobilization of lipase in matrices produced with gelatin with different Bloom values and with the addition of plastifiers was investigated to evaluate the influence of the Bloom value, as well as the capacity of the plastifiers to maintain the enzyme immobilized and the immobilization yield. The results indicated the need for crosslinking of the matrices with glutaraldehyde due to the high solubility in water, explained by the amino acid profile, which confirms the solubility of gelatin. Mannitol showed greater efficiency in the lipase immobilization, since it led to more porous structures and more uniform pores. These structures were also influenced by the gelatin concentration; greater concentrations associated with intermediate concentrations of plastifier led to matrices with a greater immobilization yield (87.92%). The X-ray diffraction analysis revealed that the structure of the immobilization matrices was partially crystalline.

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A novel method for the immobilization of glucoamylase onto polyglutaraldehyde-activated gelatin

Cited by 49 publications

References 20 publications

Stabilization of a raw starch digesting amylase from Aspergillus carbonarius via immobilization on activated and non-activated agarose gel

Stabilization of a raw starch digesting amylase from Aspergillus carbonarius via immobilization on activated and non-activated agarose gel

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

Influence of bloom number and plastifiers on gelatin matrices produced for enzyme immobilization

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