A novel method for the immobilization of glucoamylase to produce glucose from maltodextrin

Tanrıseven, Aziz; Uludağ, Yıldız Bozkurt; Doğan, Şenay

doi:10.1016/s0141-0229(02)00004-2

Cited by 40 publications

(24 citation statements)

References 9 publications

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“…Similar results were reported by Tanriseven et al (2002) for GA immobilized by adsorption to gelatinized corn starch and subsequent alginate fiber entrapment.…”

Section: Properties Of Ga Bone Derivativesupporting

confidence: 88%

“…3 Effect of adsorption temperature: 20°C (filled diamonds) and 51.5°C (empty squares) on the immobilized activity of GA onto bone (d p , 203 µm) free and immobilized GA followed Michaelis-Menten kinetics; however, adsorption onto bone support increased the K M about nine times (from 0.08 to 0.71 mg soluble starch ml −1 ). Different K M variations ranging from a 10% reduction to a 69% increment were reported for biocatalysts produced by GA adsorption onto active carbon (Rani et al 2000), bone particles of 600-2,000 µm (Schafhauser and Storey 1992b), gelatinized corn starch plus subsequent trapping in alginate fibers (Tanriseven et al 2002), and synthetic carbon material Sibunit® (Kovalenko and Perminova 2008). The K M increment determined in this study could be due to changes in GA three-dimensional conformation produced by immobilization and to the limited access of the macromolecular substrate (maltodextrin) to the active site of the enzyme (Bahar and Çelebi 1998;Brena 1996;Trevan 1980).…”

Section: Properties Of Ga Bone Derivativementioning

confidence: 99%

“…Several immobilization techniques such as cross-linking, covalent binding, and adsorption have been investigated to couple GA to insoluble supports (Arica et al 1998;Bahar and Çelebi 1998;Kovalenko et al 2006;Miller 1998;Rani et al 2000;Roig et al 1995;Sasvári and Asbóth 1999;Silva et al 2005;Tanriseven et al 2002;Torres et al 2004;Varavinit et al 2001). Although covalent coupling usually leads to very stable preparations compared to those obtained by physical adsorption and ionic binding, adsorption is selected for largescale applications mainly because of its comparative simplicity and economy (Kierstan and Coughlan 1991).…”

Section: Introductionmentioning

confidence: 99%

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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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“…Similar results were reported by Tanriseven et al (2002) for GA immobilized by adsorption to gelatinized corn starch and subsequent alginate fiber entrapment.…”

Section: Properties Of Ga Bone Derivativesupporting

confidence: 88%

Section: Properties Of Ga Bone Derivativementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

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 finding is interesting for industrial applications since costs can be reduced. Higher conversion rates are not reported in the literature due to the irregular structure of starch (TANRISEVEN; ULUDAG; DOGAN, 2002). Figure 4 shows the isomerization rate of glucose during the glucose to fructose conversion.…”

Section: Resultsmentioning

confidence: 91%

“…The maximum conversion occurred after 24 hours of reaction and no significant difference was observed after that. Most works report that this conversion rate is reached only after 48 hours of reaction PAPINI, 1970;CADMUS;HENSLEY, 1996;AKERBERG et al, 2000;TANRISEVEN;ULUDAG;DOGAN, 2002), indicating that the GA produced by A. niger isolated from Cerrado soil has high affinity with cassava starch. This finding is interesting for industrial applications since costs can be reduced.…”

Section: Resultsmentioning

confidence: 99%

Production of glucose and fructose syrups from cassava (Manihot esculenta Crantz) starch using enzymes produced by microorganisms isolated from Brazilian Cerrado soil

et al. 2010

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The high demands for sugars and the development of enzymatic technology have increased the production of sweeteners, especially for glucose and fructose syrups. This work describe a technology for glucose and fructose syrups from Brazilian cassava starch using enzymes produced by soil microrganisms isolated from the Brazilian Cerrado soil. Firstly, Aspergillus niger and Streptomyces sp. were isolated from the soil and used as glucoamylase (GA) and glucose isomerase (GI) producer sources. After characterization, GA and GI exhibited optimum pH 4.5 and 8.0, respectively. GA showed maximum activity at 60 ºC and GI at 85 ºC. GA and GI retained 65 and 80%, respectively, of initial activity after 180 minutes of incubation at 60 ºC. The kinetic parameters Km and Vmáx were 0.476 (mg.mL-1) and 8.58 (µmol/minute) for GA and 0.082 (M) and 48.20 (µmol/minute) for GI. The maximum glucose syrups production occurred after 24 hours of reaction with a 98% yield. The production of fructose syrups with 42% (w/v) was reached after 96 hours of reaction.

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Thermostable α‐amylase immobilization: Enhanced stability and performance for starch biocatalysis

Kumar

Rather

Gurramkonda

et al. 2015

Biotech and App Biochem

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The uses of thermostable starch hydrolytic biocatalysts are steadily increasing for the industrial application because of their obvious need for biocatalytic performance at elevated temperatures. The starch liquefaction and saccharification can be carried out simultaneously by the use of thermostable starch hydrolytic biocatalysts, thus minimizing the unit operations, time, and efforts. The cost factor hampers the industrialization of expensive soluble (free) enzymes for biocatalytic applications and the immobilization of enzymes offers promising alternative to the hurdle. The present investigation was aimed for immobilization of thermostable α-amylase using calcium alginate, and statistical optimization studies were carried out for enhanced biocatalytic performance. Initially, one-parameter at a time optimization studies were carried out for identification of significant factors influencing the immobilization. Furthermore, a statistical approach, response surface methodology, was applied for immobilization of α-amylase. The immobilized α-amylase in alginate microbeads showed enhanced stability to temperature and reusable property for up to seven cycles (with the retention of 50% initial activity). Finally, the kinetic behavior of free and immobilized enzyme showed the Km value of 1.2% and 2.6% (w/v) and Vmax of 1,020 and 1,030 U, respectively. Fifty percent reduction in affinity of the immobilized enzyme toward substrate was compensated by its longer stability.

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A novel method for the immobilization of glucoamylase to produce glucose from maltodextrin

Cited by 40 publications

References 9 publications

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

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

Production of glucose and fructose syrups from cassava (Manihot esculenta Crantz) starch using enzymes produced by microorganisms isolated from Brazilian Cerrado soil

Thermostable α‐amylase immobilization: Enhanced stability and performance for starch biocatalysis

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