Urease immobilization on magnetic micro/nano-cellulose dialdehydes: Urease inhibitory of Biginelli product in...

Micro/nano celluloses (MC)/NC) were magnetized by nanoγ-Fe₂O₃ into the nanoγ-Fe₂O₃@MC (NMMC) and nanoγ-Fe₂O₃@NC (NMMC) which oxidized to NMMCD and NMNCD dialdehydes for Schiff-base immobilization of urease as NMMCD/urease and NMMCD/urease. The relative enzyme-activity of the immobilized ureases were comparable with the free-urease, although 75%-80% of the enzyme activity preserved for NMMCD/urease and NMNCD/urease after six cycles. The compared catalytic activities of the NMMCD/urease and NMMCD/urease in Biginelli/Hantzsch reactions in water at 60 °C surprised us by 100% selectivity for the Biginelli product 3,4-dihydropyrimidin-2(1H)-one (DHPM₁). With the superiority of NMNCD/urease, this high selectivity using immobilized ureases is owing to the admirable urease inhibitory of the formed Biginelli product DHPM₁ by urea condensation instead of urea hydrolysis. The robust enzyme inhibitory of the DHPM₁ for free urease was also confirmed by phenol red test to show the deactivation of enzyme for enzymatic hydrolysis of urea and ammonia production in water.