2019
DOI: 10.1007/s11164-019-03748-w
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A fast and efficient stabilization of firefly luciferase on MIL-53(Al) via surface adsorption mechanism

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Cited by 15 publications
(19 citation statements)
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“…At pH 10.0, different kinetic behavior of ZIF-8@Luc was observed including a significant BL signal decrease (∼95% at 200 s). It has been reported that enzymes attached to positively charged supports, such as ZIF-8 at pH 7–8, present stronger activity at lower pH values. , On the other hand, when the heating process was carried out up to 50 °C, the BL signal of ZIF-8@Luc was reduced (80% signal loss) more than that of the free luciferase signal (40% signal loss), despite the thermal stability of ZIF-8. This could be due to the agglomeration of ZIF-8 occurring when the biocomposite is heated, thus leading to a decrease in the available catalytic sites of luciferase.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…At pH 10.0, different kinetic behavior of ZIF-8@Luc was observed including a significant BL signal decrease (∼95% at 200 s). It has been reported that enzymes attached to positively charged supports, such as ZIF-8 at pH 7–8, present stronger activity at lower pH values. , On the other hand, when the heating process was carried out up to 50 °C, the BL signal of ZIF-8@Luc was reduced (80% signal loss) more than that of the free luciferase signal (40% signal loss), despite the thermal stability of ZIF-8. This could be due to the agglomeration of ZIF-8 occurring when the biocomposite is heated, thus leading to a decrease in the available catalytic sites of luciferase.…”
Section: Resultsmentioning
confidence: 99%
“…Synthesis of ZIF-8@Luc and Method Optimization. The synthesis of the biocomposite was accomplished by taking the method described by Nowroozi-Nejad et al 31 as the starting point with several modifications and parameter optimization. The following conditions were studied in detail: type of stirring (magnetic, orbital, vortex-assisted), MOF nature (MIL-n, UiO-n, ZIF-n), amount of MOF (0.25−0.75 mg), and reaction time (15−60 min).…”
Section: ■ Materials and Methodsmentioning
confidence: 99%
“…In this study, the validity of this in situ one-step methodology for enzyme immobilization onto NH 2 -MIL-53(Al) is extended to lipase CaLB (from Candida antarctica), which indeed is one of the most widely investigated enzymes in different immobilization processes [34][35][36]. Apart from our own studies using nanocrystalline NH 2 -MIL-53(Al) supports for enzymes [20,21], the MIL-53(Al) family has proved to be efficient in the immobilization of: (i) Laccase on NH 2 -MIL-53(Al), using our one-step room-temperature methodology [37]; (ii) laccase on meso-MIL-53(Al) by post-synthesis methods [38]; and (iii) luciferase on non-functionalized MIL-53(Al), also by post-synthesis methodology [39]. We also found excellent results for lipase in situ immobilization on the semi-crystalline support Fe-BTC [23], suggesting that this enzyme could be easily immobilized onto MOF supports.…”
Section: Introductionmentioning
confidence: 99%
“…In addition, the molecules of solvent trapped in the MOF pores reduce the specific surface area. On the other hand, the Al-MOF powders have been agglomerated and the gas penetration does not occur completely ( Rahmani and Rahmani, 2018 ; Nowroozi-Nejad et al, 2019 ).…”
Section: Resultsmentioning
confidence: 99%
“…Therefore, we have chosen one type of Al-MOFs as a carrier for the anti-proliferative herbal extract. The Al-MOFs seem to be more effective against the proliferation of breast cancer cells when compared with herbal extraction ( Nowroozi-Nejad et al, 2019 ).…”
Section: Resultsmentioning
confidence: 99%