Multipoint Immobilization at the Inert Center of Urease on Homofunctional Diazo-Activated Silica Gel: A Way of Restoring Room-Temperature Catalytic Sustainability for Perennial Utilization

Autor:	Bhabatosh Mandal, Sneha Mondal, Biswajit Hansda, Shailja Mishra, Ankit Ghosh, Tirtha Biswas, Basudev Das, Tanay kumar Mondal, Pallavi Kumari
Rok vydání:	2022
Předmět:	Borates Enzyme Stability Spectroscopy Fourier Transform Infrared Electrochemistry Temperature Silica Gel General Materials Science Surfaces and Interfaces Hydrogen-Ion Concentration Condensed Matter Physics Enzymes Immobilized Urease Spectroscopy
Zdroj:	Langmuir : the ACS journal of surfaces and colloids. 38(22)
ISSN:	1520-5827
Popis:	At present, enzyme immobilization is a big issue. It improves enzyme stability, activity, specificity, or selectivity, particularly the enantioselectivity compared to the native enzymes, and by solving the separation problem, it helps in recovering the catalyst with good reusability as desired in vitro. Motivated by these facts, in this work, Jack bean urease (JBU) is immobilized on three-dimensional (3D)-network silica gel (SG) via multipoint covalent bonding employing dimethyldichlorosilane (DMDCS) and
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35501c543379baab550962ba265188c2 https://pubmed.ncbi.nlm.nih.gov/35609014 Zobrazit plný text záznamu