Stability Improvement of Immobilized a-amylase using Nano Pore Zeolite

Maedeh, Talebi; Vaezifar, Sedigheh; Jafary, Fariba; Fazilati, Mohamad; Motamedi, Shima

doi:10.15171/ijb.1261

Cited by 38 publications

(17 citation statements)

References 27 publications

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“…The ionic interactions generated between enzyme and the carrier imparted a higher conformational stability to the immobilized enzyme. Many reports are there showing the storage stability of immobilized α-amylase [50][51][52]. …”

Section: Effect Of Storage Time On Activity Of Immobilized Enzymesmentioning

confidence: 99%

Enhanced Stability of Α-Amylase via Immobilization onto Chitosan-Tio2 Nanocomposite

Mohanan¹

2017

NSTOA

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Section: Effect Of Storage Time On Activity Of Immobilized Enzymesmentioning

confidence: 99%

Enhanced Stability of Α-Amylase via Immobilization onto Chitosan-Tio2 Nanocomposite

Mohanan¹

2017

NSTOA

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“…Nonetheless, the immobilization procedure may result in conformational changes, which might affect the catalytic efficiency of enzymes. It should be noted that in order to design an exceptionally effective immobilized enzyme nanobiocatalyst for biotechnological applications, its stability should be excellent at lower and higher temperature ranges, and in both acidic and basic pH ranges [ 36 ]. The pH activity profiles for soluble β-galactosidase and the enzyme bound to PVA-modified AuNPs are shown in Figure 5 .…”

Section: Resultsmentioning

confidence: 99%

Stabilization of β-Galactosidase on Modified Gold Nanoparticles: A Preliminary Biochemical Study to Obtain Lactose-Free Dairy Products for Lactose-Intolerant Individuals

Alshanberi

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Ansari³

2021

Molecules

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The unique chemical, optical, and electrical characteristics of nanoparticles make their utilization highly successful in every field of biological sciences as compared to their bulk counterpart. These properties arise as a result of their miniature size, which provides them an excellent surface area-to-volume ratio, inner structure, and shape, and hence increases their surface characteristics. Therefore, this study was undertaken to engineer gold nanoparticles (AuNPs) for improving their catalytic activity and stability in biotechnological processes. The characterization of AuNPs was performed by XRD, UV spectra, and TEM. The synthesized AuNPs were surface-modified by polyvinyl alcohol (PVA) for binding the enzyme in excellent yield. The developed immobilized enzyme system (PVA-AuNPs-β-galactosidase) displayed pH optima at pH 7.0 and temperature optima at 40 °C. Moreover, the stability of PVA-AuNPs-β-galactosidase was significantly enhanced at wider pH and temperature ranges and at higher galactose concentrations, in contrast to the free enzyme. β-galactosidase bound to PVA-modified AuNPs exhibited greater operational activity, even after its sixth reuse. The developed nanosystem may prove useful in producing lactose-free dairy products for lactose-intolerant patients.

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“…Talebi et.al . previously reported the efficiency of immobilized α‐amylase onto a nano‐zeolite support was 58.44% . Yang et.al .…”

Section: Resultsmentioning

confidence: 99%

Preparation of a Poly(ethylene glycol)‐Based Cross‐Linked Network from a Click Reaction for Enzyme Immobilization

2019

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In this study, a polyethylene glycol (PEG)‐maleimide film was prepared by a thiol‐ene click reaction. The covalent immobilization of amylase was carried out onto the PEG‐maleimide based photo‐curable network via epoxy and C=O groups without any linker. The epoxy and carbonyl groups on the PEG backbone improved the affinity of the enzyme. The immobilization yield of amylase onto the film was 72.46%. The immobilization capacity was also determined as 313 mg/g. The thermal stability of amylase improved via covalent attachment. Immobilized amylase showed maximum activity at 40 °C and pH 6.5. The immobilized amylase continued to retain 66% of its initial activity after 30 days.

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Stability Improvement of Immobilized a-amylase using Nano Pore Zeolite

Cited by 38 publications

References 27 publications

Enhanced Stability of Α-Amylase via Immobilization onto Chitosan-Tio2 Nanocomposite

Enhanced Stability of Α-Amylase via Immobilization onto Chitosan-Tio2 Nanocomposite

Stabilization of β-Galactosidase on Modified Gold Nanoparticles: A Preliminary Biochemical Study to Obtain Lactose-Free Dairy Products for Lactose-Intolerant Individuals

Preparation of a Poly(ethylene glycol)‐Based Cross‐Linked Network from a Click Reaction for Enzyme Immobilization

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