Thermal inactivation of free and immobilized inulinase

Artyukhov, V. G.; Kovaleva, T. A.; Holyavka, M. G.; Bityutskaya, L. A.; Grechkina, M. V.

doi:10.1134/s0003683810040034

Cited by 17 publications

(6 citation statements)

References 10 publications

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“…Such functional foods include oligosaccharides with prebiotic properties and fructose with health benefits [1] . However, homogenous hydrolytic enzymes face limitations such as instability to various ‘environmental factors during the production process [2] . Additionally, homogeneous enzymes are not appropriate for multiple uses as a result of laborious separation from the reagent and reaction productions.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of thermostable exo-inulinase from mutant thermophilic Aspergillus tamarii-U4 using kaolin clay and its application in inulin hydrolysis

Garuba

Abiodun

Onilude

2018

Journal of Genetic Engineering and Biotechnology

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In this study, attempts were made to immobilize purified exo-inulinase from mutant thermophic Aspergillus tamarii-U4 onto Kaolinite clay by covalent bonding cross-linked with glutaraldehyde with an immobilization yield of 66% achieved. The free and immobilized inulinases were then characterized and characterization of the enzymes revealed that temperature and pH optima for the activity of the free and immobilized enzymes were both 65 °C and pH 4.5 respectively. The free inulinase completely lost its activity after incubation at 65 °C for 6 h while the immobilized inulinase retained 16.4% of its activity under the same condition of temperature and incubation time. The estimated kinetic parameters Km and Vmax for the free inulinase as estimated from Lineweaver-Burk plots were 0.39 mM and 4.21 µmol/min for the free inulinase and 0.37 mM and 4.01 µmol/min for the immobilized inulinase respectively. Inulin at 2.5% (w/v) and a flow rate of 0.1 mL was completely hydrolysed for 10 days at 60 °C in a continuous packed bed column and the operational stability of the system revealed that the half-life of the immobilized inulinase was 51 days. These properties make the immobilized exo-inulinase from Aspergillus tamarii-U4 a potential candidate for the production of fructose from inulin hydrolysis.

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Section: Introductionmentioning

confidence: 99%

Immobilization of thermostable exo-inulinase from mutant thermophilic Aspergillus tamarii-U4 using kaolin clay and its application in inulin hydrolysis

Garuba

Abiodun

Onilude

2018

Journal of Genetic Engineering and Biotechnology

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“…Immobilization imposes no significant activity loss (based on specific activity analysis) in spite of the mass transfer restrictions. Activity improvement of inulinase after immobilization has been recently stated by Kovaleva et al (2009), Artiukhov et al (2010) and a, b. The hydrolytic activity of free and immobilized inulinases were assayed in three repeats at one day intervals up to 6 days and the corresponding half-lives are presented in inset to Fig.…”

Section: Resultsmentioning

confidence: 74%

Immobilization of inulinase from Aspergillus niger on octadecyl substituted nanoporous silica: Inulin hydrolysis in a continuous mode operation

Karimi

Habibi-Rezaei

Rezaei

et al. 2016

Biocatalysis and Agricultural Biotechnology

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Inulinase hydrolyzes inulin and produce high fructose syrup in a single-step reaction. However, finding the best working conditions and the highest inulinase stability, especially in continuous mode operations are of critical value. Native (endo-inulinase (EC 3.2.1.7)) and chemically modified inulinases (endo-inulinase stabilized with pyridoxal 5'-phosphate /ascorbic acid in a semi-rational chemical modification approach) were immobilized on octadecyl substituted nanoporous silica (with the average pore size of 66 nm) by using dioxane to extend the hydrophobic interactions between inulinase refolding intermediates and the hydrophobic alkyl moieties of the support. Native and modified inulinases revealed their maximum surface hydrophobicity at 40 and 50 % dioxane in water, respectively. Immobilized inulinases (native and modified) showed 7.89 and 3.73 fold increase in their half lives compared to the free native sample., higher reusability compared to free inulinases (native and modified) and also could retain their activities after 10 hydrolysis cycles in a continuous mode of experimental conditions.

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“…Protein content in enzyme conjugates with Na-CMC or Na-CMC- g -PDMAEMA copolymer was determined by the Lowry method [ 26 ] with the following modification: at the first stage of the analysis, the bonds between the modified polysaccharide and the enzyme molecules were broken. For this end, the immobilized enzymes were treated with a 0.7 M solution of K, Na-tartrate prepared with 1 M NaOH at 50 °C for 10 min [ 27 ]. The absence of enzyme degradation was controlled spectrophotometrically on a UV-2550PC spectrophotometer (Shimadzu Scientific Instruments, Kyoto, Japan).…”

Section: Methodsmentioning

confidence: 99%

Carboxymethyl Cellulose-Based Polymers as Promising Matrices for Ficin Immobilization

et al. 2023

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The present work is devoted to research on the interaction between carboxymethyl cellulose sodium salt and its derivatives (graft copolymer of carboxymethyl cellulose sodium salt and N,N-dimethyl aminoethyl methacrylate) with cysteine protease (ficin). The interaction was studied by FTIR and by flexible molecular docking, which have shown the conjugates’ formation with both matrices. The proteolytic activity assay performed with azocasein demonstrated that the specific activities of all immobilized ficin samples are higher in comparison with those of the native enzyme. This is due to the modulation of the conformation of ficin globule and of the enzyme active site by weak physical interactions involving catalytically valuable amino acids. The results obtained can extend the practical use of ficin in biomedicine and biotechnology.

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Thermal inactivation of free and immobilized inulinase

Cited by 17 publications

References 10 publications

Immobilization of thermostable exo-inulinase from mutant thermophilic Aspergillus tamarii-U4 using kaolin clay and its application in inulin hydrolysis

Immobilization of thermostable exo-inulinase from mutant thermophilic Aspergillus tamarii-U4 using kaolin clay and its application in inulin hydrolysis

Immobilization of inulinase from Aspergillus niger on octadecyl substituted nanoporous silica: Inulin hydrolysis in a continuous mode operation

Carboxymethyl Cellulose-Based Polymers as Promising Matrices for Ficin Immobilization

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