Make proper surfaces for immobilization of enzymes: Immobilization of lipase and α-amylase on modified Na-sepiolite

Mortazavi, Seyed Bagher; Aghaei, Hamidreza

doi:10.1016/j.ijbiomac.2020.07.103

Cited by 75 publications

(23 citation statements)

References 143 publications

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“…Furthermore, temperature has a greater impact on both free and immobilized ROL enzyme activities than AOA. The immobilized lipase , and α-amylases , were more stable at elevated temperatures and changing pH values than their free counterparts. The improved thermostability of ROL and AOA immobilized on SiO 2 opals was most likely due to the rigidity of the secondary structures of enzyme molecules, which prevents them from unfolding further at different temperatures .…”

Section: Resultsmentioning

confidence: 97%

“…To measure the enzyme activity of AOA@opal-SiO 2 , 0.5 mL of different concentrations of AOA@opal-SiO 2 was added into 1 mL of phosphate buffer (20 mM, pH 7) with 10 mg/mL dissolved starch used as the substrate and incubated at 25 °C for 10 min. Then, 1 mL of DNS solution was prepared by the addition of 1 g of DNS, 30 g of sodium potassium tartrate, and 20 mL of 2 M NaOH in distilled water to 100 mL, and the reaction mixture was immediately placed in a boiling water bath for 5 min . The absorbance was determined at 540 nm using a standard curve of maltose measured using a spectrophotometer (Multiskan SkyHigh, Thermo Fisher Scientific, USA).…”

Section: Methodsmentioning

confidence: 99%

“…Then, 1 mL of DNS solution was prepared by the addition of 1 g of DNS, 30 g of sodium potassium tartrate, and 20 mL of 2 M NaOH in distilled water to 100 mL, and the reaction mixture was immediately placed in a boiling water bath for 5 min. 26 The absorbance was determined at 540 nm using a standard curve of maltose measured using a spectrophotometer (Multiskan SkyHigh, Thermo Fisher Scientific, USA). One unit of AOA activity was defined as the amount of required enzyme that released 1 μmol of maltose per minute at 25 °C.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

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A SiO₂ Microcarrier with an Opal-like Structure for Cross-Linked Enzyme Immobilization

Luo

Jin

et al. 2021

Langmuir

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The opal-like SiO 2 microcarriers with different pore diameters named opal-SiO 2 I and opal-SiO 2 II were synthesized and utilized as microcarriers to immobilize Rhizopus oryzae lipase (ROL) and Aspergillus oryzae α-amylases (AOA). ROL and AOA can be more stably immobilized on the cross-linked SiO 2 opals by neopentyl glycol diglycidyl ether (NGDE), which is the first attempt to use it as a cross-linking agent compared with glutaraldehyde. According to the morphology analysis, multiple layers of SiO 2 monodisperse microspheres were regularly packed and formed an opal-like structure, and enzymes were well scattered and immobilized throughout the SiO 2 opals. The results showed that the performance of enzymes immobilized on opal-SiO 2 II with a larger specific surface area was much better than that of opal-SiO 2 I.

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Section: Resultsmentioning

confidence: 97%

Section: Methodsmentioning

confidence: 99%

Section: ■ Materials and Methodsmentioning

confidence: 99%

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A SiO₂ Microcarrier with an Opal-like Structure for Cross-Linked Enzyme Immobilization

Luo

Jin

et al. 2021

Langmuir

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“…Also, immobilization enhances the efficiency of lipase by increasing its purity, activity, specificity, selectivity, and resistance to inhibitors. 7 , 15…”

Section: Introductionmentioning

confidence: 99%

“…Microbial lipases are largely applied in biocatalysis due to their versatility, catalytic properties, and high stability in the reaction media . Lipase catalyzes various reactions such as hydrolysis, esterification, and transesterification …”

Section: Introductionmentioning

confidence: 99%

Effect of Different TiO₂ Morphologies on the Activity of Immobilized Lipase for Biodiesel Production

2021

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Lipase catalytic activity is greatly influenced by immobilization on nanoparticles. In this study, lipase from Aspergillus niger was immobilized on TiO 2 nanoparticles with different morphologies: microspheres, nanotubes, and nanosheets. All TiO 2 samples were prepared by a hydrothermal method. Lipase/TiO 2 nanocomposites were prepared by a physical adsorption method through hydrophobic interactions. The prepared composites were characterized by Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), scanning electron microscopy (SEM), and high-resolution transmission electron microscopy (HRTEM). The catalytic activity of free and immobilized lipases was tested using sunflower oil in the presence of methanol to produce biodiesel at 40 °C for 90 min. The lipase immobilized on TiO 2 microspheres showed the highest activity compared to the lipase immobilized on TiO 2 nanotubes and nanosheets. To optimize the lipase-to-microsphere ratio, lipase was immobilized on TiO 2 microspheres in different microspheres/lipase, w/w, (S/L) ratios of 1:1, 1:0.75, 1:0.5, and 1:0.25. It was noticed that the hydrolytic activity follows the order 1:0.25 > 1:0.5 > 1:75 > 1:1. The immobilization yield activities were found to be 113, 123, 125, and 130% for the microspheres/lipase (S/L) ratios of 1:1, 1:0.75, 1:0.5, and 1:0.25, respectively.

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Chitosan‐Based Porous Composites for Bone Tissue Engineering

Шарикова

Антипова

Луканина

et al. 2022

Macromolecular Symposia

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This paper highlights the idea of creating highly porous composite materials for osteogenesis purposes based on chitosan with various functional fillers: reduced graphene oxide (rGO) and tricalcium phosphate (TCP). RGO filler is a carbon based electrical conductor with a high aspect ratio, therefore it is preferred for growth of osteoblasts populations with concomitant electrical stimulation. TCP is the main building block of bone tissue; hence composites filled with it can be used to accelerate the process of osteosynthesis. This paper considers the aspects of the functional agents influence on the morphological, electrically conductive, and mechanical characteristics of composites based on chitosan.

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Make proper surfaces for immobilization of enzymes: Immobilization of lipase and α-amylase on modified Na-sepiolite

Cited by 75 publications

References 143 publications

A SiO₂ Microcarrier with an Opal-like Structure for Cross-Linked Enzyme Immobilization

A SiO₂ Microcarrier with an Opal-like Structure for Cross-Linked Enzyme Immobilization

Effect of Different TiO₂ Morphologies on the Activity of Immobilized Lipase for Biodiesel Production

Chitosan‐Based Porous Composites for Bone Tissue Engineering

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Make proper surfaces for immobilization of enzymes: Immobilization of lipase and α-amylase on modified Na-sepiolite

Cited by 75 publications

References 143 publications

A SiO2 Microcarrier with an Opal-like Structure for Cross-Linked Enzyme Immobilization

A SiO2 Microcarrier with an Opal-like Structure for Cross-Linked Enzyme Immobilization

Effect of Different TiO2 Morphologies on the Activity of Immobilized Lipase for Biodiesel Production

Chitosan‐Based Porous Composites for Bone Tissue Engineering

Contact Info

Product

Resources

About

A SiO₂ Microcarrier with an Opal-like Structure for Cross-Linked Enzyme Immobilization

A SiO₂ Microcarrier with an Opal-like Structure for Cross-Linked Enzyme Immobilization

Effect of Different TiO₂ Morphologies on the Activity of Immobilized Lipase for Biodiesel Production