2018
DOI: 10.1016/j.btre.2018.02.004
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Inulin hydrolysis by inulinase immobilized covalently on magnetic nanoparticles prepared with wheat gluten hydrolysates

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Cited by 23 publications
(18 citation statements)
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References 24 publications
(26 reference statements)
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“…On the other hand, for the immobilized enzyme, the yield of fructose was observed to be 18.2 g/L at 30°C which increased to 35.8 g/L at 60°C. This higher optimum temperature for immobilized inulinase could be explained by the increase in structural rigidity and decrease in flexibility of the covalently immobilized inulinase [47]. However, a further increase in the temperature led to a decrease in fructose yield and at 80°C; a fructose yield of 10.2 g/L and 20.4 g/L was obtained with the free and immobilized inulinase, respectively.…”
Section: Hydrolysis Of Inulinmentioning
confidence: 96%
“…On the other hand, for the immobilized enzyme, the yield of fructose was observed to be 18.2 g/L at 30°C which increased to 35.8 g/L at 60°C. This higher optimum temperature for immobilized inulinase could be explained by the increase in structural rigidity and decrease in flexibility of the covalently immobilized inulinase [47]. However, a further increase in the temperature led to a decrease in fructose yield and at 80°C; a fructose yield of 10.2 g/L and 20.4 g/L was obtained with the free and immobilized inulinase, respectively.…”
Section: Hydrolysis Of Inulinmentioning
confidence: 96%
“…Therefore, thermostable inulinases are desirable biocatalysts for the chemical and food industry. In this context, Torabizadeh and Mahmoudi [25], covalently attached inulinase from Aspergillus niger onto wheat gluten hydrolysates (WGHs)-functionalized Fe 3 O 4 MNPs in the presence of glutaraldehyde as a cross-linking agent. As-developed inulinase was found to be active over a broader pH and temperature ranges, and also exhibited pronounced storage and thermal stability.…”
Section: Biotransformation Of Inulin To High Fructose Syrupmentioning
confidence: 99%
“…As-developed inulinase was found to be active over a broader pH and temperature ranges, and also exhibited pronounced storage and thermal stability. The inulinase showed 12.3 folds rise in enzyme half-life value following immobilization on MNPs at 75 • C and retained 70% of its preliminary catalytic activity after 12 continuous inulin hydrolysis cycles [25]. More recently, Mohammadi et al [23] fabricated unique biocompatible support i.e., glutathione-coated gold MNPs (GSH-AuMNPs) and used for the covalent immobilization of the inulinase enzyme (Figure 4).…”
Section: Biotransformation Of Inulin To High Fructose Syrupmentioning
confidence: 99%
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“…Previously, inulinase has been immobilized on various supports, e.g. biopolymers (chitin, chitosan, alginate) [16][17][18][19][20], synthetic polymers (polyurethane foam, polyvinyl alcohol) [21,22], inorganic supports (MWCNT, silica nanoparticles) [3,[23][24][25], or hybrids consisting of organic and inorganic parts (poly-d-lysine coated CaCO 3 microparticles, magnetic nanoparticles with wheat gluten hydrolysates, magnetite chitosan microparticles) [26][27][28]. Generally speaking, nanomaterials are currently widely used for immobilization of proteins.…”
Section: Introductionmentioning
confidence: 99%