Enhanced thermostability of the immobilized thermoalkalophilic esterase onto magnetic-cornstarch nanoparticle

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Küçük Resim

Tarih

2021

Dergi Başlığı

Dergi ISSN

Cilt Başlığı

Yayıncı

Wiley

Erişim Hakkı

info:eu-repo/semantics/closedAccess

Özet

The immobilization of the biocatalysts onto magnetic nanoparticles has been extensively applied as the external magnetic field facilitates the enzyme recovery from the reaction mixture. In the present study, glutaraldehyde-modified magnetite-cornstarch nanoparticles (MCNs) were successfully synthesized, elaborately characterized by ZetaSizer and surface-enhanced Raman spectroscopy, and used for the immobilization of a thermoalkalophilic esterase from Geobacillus sp. The optimal immobilization conditions were obtained at 65 degrees C, 2:3 molar ratios of Fe2+:Fe3+, and 1 g cornstarch resulted in approximately 90 nm magnetic particles in size. Also, immobilization yield and immobilization efficiency of the esterase were found as 74% and 82%, respectively. Scanning electron microscopy micrographs showed that MCNs were uniform, spherical in shape, and well dispersed and esterase immobilized MCNs displayed similar morphology as free MCNs. The maximum activity of free and immobilized esterase was obtained at 65 degrees C and pH 9. Immobilization onto glutaraldehyde-modified MCNs significantly enhanced the esterase thermostability. Additionally, the immobilized esterase kept its residual activity of 75% after three sequential cycles, suggesting that it has favorable operational stability.

Açıklama

Anahtar Kelimeler

Geobacillus sp, immobilization, magnetic nanoparticles, thermoalkalophilic esterase, Candida-Rugosa, Carboxyl Esterases, Lipase, Enzymes, Microspheres, Stability, Biodiesel, Alcohol, Oxidase, Laccase

Kaynak

Biotechnology And Applied Biochemistry

WoS Q Değeri

Q3

Scopus Q Değeri

Q3

Cilt

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