Soymilk oligosaccharide hydrolysis by Aspergillus oryzae α-galactosidase immobilized in calcium alginate

Prashanth, S.; Mulimani, V. H.

doi:10.1016/j.procbio.2004.04.011

Cited by 73 publications

(74 citation statements)

References 27 publications

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“…Aspergillus oryzae capable of producing extracellular α-galactosidase was isolated by Prashanth and Mulimani (2005). The fungus was grown on potato dextrose agar (PDA) slants and stored at 4 0C .…”

Section: Microorganismmentioning

confidence: 99%

Production of α-Galactosidase by Aspergillus oryzae through solid-state fermentation and its application in soymilk Galactooligosaccharide hydrolysis

Kapnoor

Mulimani

2010

Braz. arch. biol. technol.

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Section: Microorganismmentioning

confidence: 99%

Production of α-Galactosidase by Aspergillus oryzae through solid-state fermentation and its application in soymilk Galactooligosaccharide hydrolysis

Kapnoor

Mulimani

2010

Braz. arch. biol. technol.

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“…Alginate obtained from brown algae was broadly used as polymer for the immobilization, encapsulation and entrapment of enzymes [23][24][25]. Though calcium alginate beads have been used for the entrapment of enzymes, they are not preferred due to their large pore size that may result in enzyme leakage.…”

Section: Resultsmentioning

confidence: 99%

Immobilization of β-galactosidase from Lactobacillus plantarum HF571129 on ZnO nanoparticles: characterization and lactose hydrolysis

Ethiraj

Mohanasrinivasan

Devi

et al. 2015

Bioprocess Biosyst Eng

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β-Galactosidase from Lactobacillus plantarum HF571129 was immobilized on zinc oxide nanoparticles (ZnO NPs) using adsorption and cross-linking technique. Immobilized β-galactosidase showed broad-spectrum pH optima at pH 5-7.5 and temperature 50-60 °C. Fourier transform infrared spectroscopy (FTIR) and field emission scanning electron microscopy (FESEM) showed that β-galactosidase successfully immobilized onto supports. Due to the limited diffusion of high molecular weight substrate, K m of immobilized enzyme slightly increased from 6.64 to 10.22 mM, while V max increased from 147.5 to 192.4 µmol min(-1) mg(-1) as compared to the soluble enzyme. The cross-linked adsorbed enzyme retained 90 % activity after 1-month storage, while the native enzyme showed only 74 % activity under similar incubation conditions. The cross-linked β-galactosidase showed activity until the seventh cycle and maintained 88.02 % activity even after the third cycle. The activation energy of thermal deactivation from immobilized biocatalyst was 24.33 kcal/mol with a half-life of 130.78 min at 35 °C. The rate of lactose hydrolysis for batch and packed bed was found to be 0.023 and 0.04 min(-1).

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“…Various studies on the immobilization of β-galactosidase derived from fungi have been published (Gaur et al, 2006;Prashanth and Mulimani, 2005;Neri et al, 2009), and Aspergillus oryzae has been subjected to numerous tests (Parizia and Foster, 1983;Haider and Hussain, 2009;Zeng et al, 2009;Guidini et al, 2010;Illanes et al, 2010). Galactose has an inhibitory effect on the activity of beta-galactosidase, which is important in the design of enzymatic reactors (Ozdural et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Optimization of the immobilization process of β-galatosidade by combined entrapment-cross-linking and the kinetics of lactose hydrolysis

Freitas

Santos

Ribeiro

et al. 2012

Braz. J. Chem. Eng.

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-The immobilization of Aspergillus oryzae β-galactosidase was achieved by entrapment in sodium alginate and gelatin and cross-linking with glutaraldehyde. The optimal concentrations of the aforementioned variables in the immobilization process were determined using an orthogonal central composite design with an orthogonal axial value of 1.35313. The concentrations of alginate, gelatin and glutaraldehyde that provided the greatest enzymatic activity were 6.60%, 4.05% and 3.64% (w/v), respectively. The stability of the immobilized enzyme under the optimal conditions was evaluated through daily activity assays. After 25 uses, a 20% decrease in the enzymatic activity was observed, indicating that the immobilization process could be used to produce a stable biocatalyst. This study investigates the influence of lactose and product concentrations on kinetic reaction hydrolysis. The concentration ranges for the studied variables were 10 to 56 g/L for lactose and 0 to 11.5 g/L for glucose and galactose. Only galactose presented a competitive inhibitory effect.

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Soymilk oligosaccharide hydrolysis by Aspergillus oryzae α-galactosidase immobilized in calcium alginate

Cited by 73 publications

References 27 publications

Production of α-Galactosidase by Aspergillus oryzae through solid-state fermentation and its application in soymilk Galactooligosaccharide hydrolysis

Production of α-Galactosidase by Aspergillus oryzae through solid-state fermentation and its application in soymilk Galactooligosaccharide hydrolysis

Immobilization of β-galactosidase from Lactobacillus plantarum HF571129 on ZnO nanoparticles: characterization and lactose hydrolysis

Optimization of the immobilization process of β-galatosidade by combined entrapment-cross-linking and the kinetics of lactose hydrolysis

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