Catalytic properties of glucoamylase immobilized on synthetic carbon material Sibunit

Коваленко, Г. А.; Perminova, L. V.; Terent’eva, T. G.; Плаксин, Г. В.

doi:10.1134/s0003683807040023

Cited by 12 publications

(10 citation statements)

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“…Similarly, Reshmi et al (2006) reported a shift of optimum pH from 5.0 to 7.0-6.0 to 8.0 following a-amylase immobilization on alumina. Kovalenko et al (2007) reported that the immobilization of glucose by sorption on a carbon support subunit narrowed the pH range, from the optimum pH of 3.0-6.0 for the soluble enzyme to 4.5-6.0. This was attributed to the preferential adsorption of certain enzyme species present in impure enzyme solution and their structural rearrangements.…”

Section: Immobilization On Ph Activity and Stabilitymentioning

confidence: 98%

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: Immobilization On Ph Activity and Stabilitymentioning

confidence: 98%

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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“…Free glucoamylase immobilised on activated carbon, bulk catalytic filamentous carbon, Sibunit and polymeric supports worked optimally at slightly lower operational temperatures i.e. 65-70 ℃ [4,6,7,24,25]. The same sit-uation was observed on the immobilised glucoamylase on magnetic chitosan nanocarriers where the optimal temperature was 65 ℃ [19].…”

Section: Effect Of Operational Factorsmentioning

confidence: 58%

“…In general, immobilisation of the free glucoamylase on inorganic support tended to reduce its initial specific activity. Glucoamylase adsorbed on Sibunit retained up to 20% of the initial activity of the dissolved enzyme [4,24]. Lower glucoamylase specific activity (< 10%) was obtained when it was immobilised on polymeric compounds [6,7,25].…”

Section: Glucoamylase On Supportmentioning

confidence: 99%

“…The functionalised magnetic nanoparticles having larger diameter (< 30 nm) obtained the specific activity as high as of 1,408.6 U.g -1 [18]. The mesoporous carbons, which had relatively higher surface area as described above, only gave the specific activity of 84-540 U.g -1 [4,24]. Although the poly(GMAco-EGDMA) had higher pore sizes, the glucoamylase immobilised on this support showed lower specific activity (700-1,100 U.g -1 ) [6,25], which could be caused by this support had lower surface area than the MCF silica.…”

Section: Glucoamylase On Supportmentioning

confidence: 99%

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The Optimised Statistical Model for Enzymatic Hydrolysis of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica

Agustian

Hermida

2019

Bull. Chem. React. Eng. Catal.

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Enzymatic hydrolysis of starches using free glucoamylase to reducing sugars have difficulties in recovering and recycling of the enzyme, hence immobilisation on inert supports were widely studied. However, effectiveness of the immobilised glucoamylase were merely observed only on soluble starches. It was considered a valuable thing to know performance of glucoamylase on Mesostructured Cellular Foam (MCF) silica in hydrolysing of tapioca. An optimised study on enzymatic hydrolysis of tapioca using glucoamylase on MCF silica (9.2T-3D) and its kinetics were described including justification of the predicted model as it was required to develop in large scale operations. Central Composite Design was used to model the process by studying effects of three factors on DE values after enzyme immobilisation. Immobilisation of glucoamylase on this support gave up to 82% efficiency with the specific activity of 1,856.78 U.g -1 . Its used to hydrolysis of tapioca resulted DE values of 1.740-76.303% (w/w) where the highest DE was obtained at pH of 4.1, temperature of 70 ℃ and agitation speed of 140 rpm. The optimisation produced a polynomial quadratic model having insignificant lack-of-fit and low standard deviation, so that it was applicable and reliable in simulating the DE with only 0.80% of data were not described. Temperature affected the process highly, but the buffer pH, agitation speed and factorial interactions were considered not important. KM value for immobilised enzyme was better than the free glucoamylase, however, its reaction rate was slower than the free glucoamylase catalysis.

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“…It is known that substrate stabilizes GA (Kovalenko et al 2007). The thermostability of bone adsorbed GA in the presence of substrate (t 1/2 =293 h) was estimated from its operational stability in the hydrolysis of 30% w/w cassava maltodextrin (Fig.…”

Section: Properties Of Ga Bone Derivativementioning

confidence: 98%

Bone-Bound Glucoamylase as a Biocatalyst in Bench-Scale Production of Glucose Syrups from Liquefied Cassava Starch

Carpio

Escobar

Batista‐Viera

et al. 2008

Food Bioprocess Technol

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This research assesses the bench-scale application of a non-conventional support, bone particles, for glucoamylase (GA) immobilization and its subsequent use in cassava starch hydrolysis. Upon determining the appropriate conditions to immobilize GA onto chicken bone particles, such as pH, ionic strength, particle size, and enzyme load, bench-scale immobilization of commercial GA without further purification was performed. Under the selected conditions, 270 GA units per gram of support were adsorbed. Optimal temperature and thermal stability of immobilized GA were only slightly different from those of the free enzyme, while optimal pH became more acidic by about one unit. The feasibility of the use of this immobilized biocatalyst for high glucose syrup production from liquefied cassava starch, at bench scale in batch process using a stirred-tank reactor, was demonstrated. Repeated use of the GA-bone derivative showed that similar conversions to those achieved with soluble enzyme (dextrose equivalent=98) were reached until the third batch and over 90% until the 25th batch.

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Catalytic properties of glucoamylase immobilized on synthetic carbon material Sibunit

Cited by 12 publications

References 0 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

The Optimised Statistical Model for Enzymatic Hydrolysis of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica

Bone-Bound Glucoamylase as a Biocatalyst in Bench-Scale Production of Glucose Syrups from Liquefied Cassava Starch

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