Exuberant Immobilization of Urease on an Inorganic SiO^sub 2^ Support Enhances the Enzymatic Activities by 3-fold for Perennial Utilization

Urease has been covalently immobilized on a 3-D networking silica gel (SG) using dimethyldichlorosilane (DMDCS) as second generation silane coupling reagent and m-nitroaniline as linker component in a robust methodology and subsequently characterized as [{Si(OSi)4(H2O)0.05}205.2]n=4{OSi(CH3)2–NH–C6H...

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Bibliographic Details
Published in:Bioconjugate chemistry 2019-01, Vol.30 (1), p.134
Main Authors: Mondal, Sneha, Malik, Susanta, Sarkar, Rimi, Roy, Dipika, Saha, Sanchari, Mishra, Shailja, Sarkar, Anindya, Chatterjee, Mousumi, Mandal, Bhabatosh
Format: Article
Language:English
Subjects:
Ammonia
Coupling (molecular)
Crosslinking
Enzymatic activity
Enzymes
Immobilization
Reagents
Silica
Silica gel
Silicon dioxide
Tyrosine
Urease
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Summary:Urease has been covalently immobilized on a 3-D networking silica gel (SG) using dimethyldichlorosilane (DMDCS) as second generation silane coupling reagent and m-nitroaniline as linker component in a robust methodology and subsequently characterized as [{Si(OSi)4(H2O)0.05}205.2]n=4{OSi(CH3)2–NH–C6H4–N═N-urease}·282.5H2O (molecular mass 263 445 g or 263.4 kDa). Selective coupling of tyrosine residue with an identifiable m-nitroaniline modified SG unit prevents enzyme–enzyme cross-linking leading to enhancement of enzymatic activity. The material worked at room temperature and its activity (luminescent and ammonia releasing efficiency) was enhanced by 3-fold (for both synthetic and real sample) compared to native enzyme values at neutral pH. Up to 30 days and 30 cycles, this 3-fold activity remains as such but reduces gradually to native enzyme level after 60 days and 60 cycles of reuse.
ISSN:1043-1802
1520-4812
DOI:10.1021/acs.bioconjchem.8b00796