Immobilization of β-Glucosidase from Thermatoga maritima on Chitin-functionalized Magnetic Nanoparticle via a Novel Thermostable Chitin-binding Domain.

Bacterial Proteins / chemistry Chitin / chemistry Enzyme Stability Enzymes, Immobilized / chemistry Kinetics Magnetite Nanoparticles / chemistry Models, Molecular Oligosaccharides / biosynthesis Protein Domains Recombinant Fusion Proteins / chemistry Temperature Thermotoga maritima / enzymology beta-Glucosidase / chemistry

Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
03 02 2020
Historique:
received: 14 09 2019
accepted: 25 11 2019
entrez: 5 2 2020
pubmed: 6 2 2020
medline: 18 11 2020
Statut: epublish

Résumé

Enzyme immobilization is a powerful tool not only as a protective agent against harsh reaction conditions but also for the enhancement of enzyme activity, stability, reusability, and for the improvement of enzyme properties as well. Herein, immobilization of β-glucosidase from Thermotoga maritima (Tm-β-Glu) on magnetic nanoparticles (MNPs) functionalized with chitin (Ch) was investigated. This technology showed a novel thermostable chitin-binding domain (Tt-ChBD), which is more desirable in a wide range of large-scale applications. This exclusive approach was fabricated to improve the Galacto-oligosaccharide (GOS) production from a cheap and abundant by-product such as lactose through a novel green synthesis route. Additionally, SDS-PAGE, enzyme activity kinetics, transmission electron microscopy (TEM) and Fourier transform infrared spectroscopy (FT-IR) revealed that among the immobilization strategies for Thermotoga maritime-β-Glucosidase thermostable chitin-binding domain (Tm-β-Glu-Tt-ChBD) on the attractive substrate; Ch-MNPs had the highest enzyme binding capacity and GOS production ratio when compared to the native enzyme. More interestingly, a magnetic separation technique was successfully employed in recycling the immobilized Tm-β-Glu for repetitive batch-wise GOS without significant loss or reduction of enzyme activity. This immobilization system displayed an operative stability status under various parameters, for instance, temperature, pH, thermal conditions, storage stabilities, and enzyme kinetics when compared with the native enzyme. Conclusively, the GOS yield and residual activity of the immobilized enzyme after the 10

Identifiants

DOI: 10.1038/s41598-019-57165-5 PMID: 32015452 PMC: PMC6997207
pubmed: 32015452
doi: 10.1038/s41598-019-57165-5
pii: 10.1038/s41598-019-57165-5
pmc: PMC6997207
doi:

Substances chimiques

Bacterial Proteins 0
Enzymes, Immobilized 0
Magnetite Nanoparticles 0
Oligosaccharides 0
Recombinant Fusion Proteins 0
Chitin 1398-61-4
beta-Glucosidase EC 3.2.1.21

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1663

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Auteurs

Fawze Alnadari (F)

Department of Food Science and Engineering, School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Nanjing, 210023, Jiangsu, P.R. China.
Department of Food Science and Technology, Faculty of Agriculture, Sana'a University, Sana'a, Yemen.

Yemin Xue (Y)

Department of Food Science and Engineering, School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Nanjing, 210023, Jiangsu, P.R. China.

Liang Zhou (L)

Department of Food Science and Engineering, School of Food Science and Pharmaceutical Engineering, Nanjing Normal University, Nanjing, 210023, Jiangsu, P.R. China.

Yahya S Hamed (YS)

Food Technology Department, Faculty of Agriculture, Suez Canal University, Ismailia, 41522, Egypt.

Mohamed Taha (M)

Department of Biochemistry, Faculty of Agriculture, Benha University, Moshtohor, Toukh, 13736, Egypt.
Centre for Environmental Sustainability and Remediation, RMIT University, Bundoora, Melbourne, VIC, 3083, Australia.

Mohamed F Foda (MF)

State Key Laboratory of Agricultural Microbiology, College of Science, Huazhong Agricultural University, Wuhan, 430070, P. R. China. m.frahat@fagr.bu.edu.eg.
State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, 430070, P. R. China. m.frahat@fagr.bu.edu.eg.
Department of Biochemistry, Faculty of Agriculture, Benha University, Moshtohor, Toukh, 13736, Egypt. m.frahat@fagr.bu.edu.eg.

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines bactériennes › Immobilization of β-Glucosidase from...
questionsmedicales.fr › Glucides › Polyosides › Chitine › Immobilization of β-Glucosidase from...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Stabilité protéique › Stabilité enzymatique › Immobilization of β-Glucosidase from...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines immobilisées › Enzymes immobilisées › Immobilization of β-Glucosidase from...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Cinétique › Immobilization of β-Glucosidase from...
questionsmedicales.fr › Technologie, industrie et agriculture › Produits manufacturés › Nanostructures › Nanoparticules › Nanoparticules métalliques › Nanoparticules magnétiques d'oxyde de fer › Nanoparticules de magnétite › Immobilization of β-Glucosidase from...
questionsmedicales.fr › Techniques d'investigation › Modèles théoriques › Modèles moléculaires › Immobilization of β-Glucosidase from...
questionsmedicales.fr › Glucides › Polyosides › Oligosaccharides › Immobilization of β-Glucosidase from...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure tertiaire des protéines › Domaines protéiques › Immobilization of β-Glucosidase from...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines recombinantes › Protéines de fusion recombinantes › Immobilization of β-Glucosidase from...
questionsmedicales.fr › Environnement et santé publique › Environnement › Concepts météorologiques › Atmosphère › Temps (météorologie) › Température › Immobilization of β-Glucosidase from...
questionsmedicales.fr › Bactéries › Bactéries à Gram négatif › Bactéries anaérobies à Gram négatif › Bâtonnets à Gram négatif anaérobies droits, incurvés et spiralés › Thermotoga › Thermotoga maritima › Immobilization of β-Glucosidase from...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Hydrolases › Glycosidases › Glucosidases › Cellulases › bêta-Glucosidase › Immobilization of β-Glucosidase from...