Magnetic layered double hydroxide nanosheet as a biomolecular vessel for enzyme immobilization

Tahsiri, Zahra; Niakousari, Mehrdad; Hosseini, Seyed Mohammad Hashem; Majdinasab, Marjan

doi:10.1016/j.ijbiomac.2022.04.111

Cited by 8 publications

(2 citation statements)

References 36 publications

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“…The first was the control (with no added enzyme), while 2% (W/W) of free ficin and immobilised one were added to other two samples, respectively. All solutions were incubated at 60 °C and pH 7 To provide an optimum condition for enzyme activity in the 300 min of hydrolysis (Tahsiri et al ., 2022). At 60‐min interval, the solution was centrifuged at 10 000 g for 10 min at 4 °C, and the supernatant was freeze‐dried to obtain the protein hydrolysate.…”

Section: Methodsmentioning

confidence: 99%

Production and features of antioxidative hydrolysate from wild almond protein isolate using ficin immobilised on the layered double hydroxide

Tahsiri

Niakousari

2023

Int J of Food Sci Tech

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Summary Protein hydrolysates from wild almond protein isolate (WAPI) with different degrees of hydrolysis (DH) were synthesised using free and immobilised ficin on the magnetic layered double hydroxide and characterised. The highest DH values after 3 h of achieving 11.69 ± 0.15 and 11.37 ± 0.12, respectively, and gained hydrolysate were collected for further analysis. The zeta potential for the hydrolysis of free and immobilised ficin over hydrolysing time due to differences in molecular mass distribution decreased. By increasing the hydrolysing time in the case of free and immobilised ficin, the emulsion activity index gradually decreased, whereas the amount of emulsion stability index did not. The immobilised form of ficin‐treated hydrolysate showed a suitable level of DPPH radical scavenging and appeared to be effective in enhancing the oxidative stability of linoleic acid, sunflower oil and O/W emulsion. Thus WAPI hydrolysates that were treated with immobilised ficin could serve as an alternative antioxidant for food applications.

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Section: Methodsmentioning

confidence: 99%

Production and features of antioxidative hydrolysate from wild almond protein isolate using ficin immobilised on the layered double hydroxide

Tahsiri

Niakousari

2023

Int J of Food Sci Tech

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“…The host layer comprises hydroxy-octahedral coordination divalent/trivalent metal ions with intercalated anions between the layers. Because of their hydrophilicity, temperature resistance, and ability to allow rapid mass and electron transport, , LDHs have been selected by researchers as potential carriers for enzyme immobilization. − Conventional LDHs are typically two-dimensional clays, and enzymes can mostly be immobilized on their surface via adsorption or interspersed between layers via coprecipitation with the possibility of leakage or inactivation. , Inspired by the advantages of enzyme encapsulation, the use of three-dimensional LDHs with unique properties for enzyme encapsulation is foreseen to drastically improve the catalytic activity of enzymes and overcome the shortcomings of the currently available encapsulation carriers. However, LDHs have rarely been explored as carriers to develop an enzyme encapsulation strategy.…”

Section: Introductionmentioning

confidence: 99%

Enhancing Enzyme Activity Using Hydrophilic Hollow Layered Double Hydroxides as Encapsulation Carriers

Gan

et al. 2023

ACS Appl. Mater. Interfaces

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Enzyme immobilization enables the fabrication of flexible and powerful biocatalytic systems that can meet the needs of green and efficient development in various fields. However, restricted electron and mass transfer during enzymatic reactions and disruption of the enzyme structure during encapsulation limit the wide application of the immobilized enzyme systems. Herein, we report an encapsulation strategy based on hollow-shell-layered double hydroxides (LDHs; ZnCo-LDH) for green and nondestructive enzyme immobilization. Benefiting from the protective and enzyme-friendly microenvironment provided by the hydrophilic hollow structure of ZnCo-LDH, the encapsulated enzyme maintains a nearly natural enzyme biostructure and enhanced stability. Notably, mesoporous ZnCo-LDH with excellent electrical properties considerably facilitates electron and mass transport during enzymatic reactions, exhibiting 5.56 times the catalytic efficiency of free enzymes or traditional enzyme encapsulation systems. The current study broadens the family of encapsulated carriers and alleviates the trade-off between enzyme stability and catalytic activity in the encapsulated state, presenting a promising avenue for the industrial application of the enzyme.

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Immobilization of Ficin Enzyme onto Surface-Modified Iron Oxide Nanoparticles: Characterization and Catalytic Activity

Shooli,

Aminlari,

Sahraeian

et al. 2024

J Clust Sci

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Magnetic layered double hydroxide nanosheet as a biomolecular vessel for enzyme immobilization

Cited by 8 publications

References 36 publications

Production and features of antioxidative hydrolysate from wild almond protein isolate using ficin immobilised on the layered double hydroxide

Production and features of antioxidative hydrolysate from wild almond protein isolate using ficin immobilised on the layered double hydroxide

Enhancing Enzyme Activity Using Hydrophilic Hollow Layered Double Hydroxides as Encapsulation Carriers

Immobilization of Ficin Enzyme onto Surface-Modified Iron Oxide Nanoparticles: Characterization and Catalytic Activity

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