Urease covalently coupled to porous glass

Response surface analysis of nano-ureases from Canavalia ensiformis and Cajanus cajan

“…In the present case, lower glycosylation in case of urease from C. ensiformis is responsible for lesser immobilization efficiency than urease from C. cajan (www.brenda-enzymes.org). The immobilization efficiencies of urease obtained from C. ensiformis and C. cajan onto AuNps are significantly higher than previous reports on urease immobilization onto various matrices [9][10][11][12][13][14][15][16][17][21][22][23][24][25][26]. …”

“…Kayastha and Srivastava [21] reported a shift (pH 7.3-8.5) when the urease from C. cajan was immobilized covalently on chitosan. The urease from C. ensiformis immobilized on a fixed-bed reactor showed the displacement in pH from 6.6 to 7.6 [24], however, when immobilized on the porous glass beads and molecular sieve4A, the shift was reported toward acidic side [25,26]. The shift in pH optimum on enzyme immobilization is attributed due to change in local microenvironment of enzyme.…”

Immobilization of Urease from Pigeonpea (Cajanus cajan) on Agar Tablets and Its Application in Urea Assay

“…There was a shift of 0.2 U toward the basic side resulting from the binding of urease. Jack bean urease immobilized on porous glass beads and molecular sieve 4A showed a shift toward the acidic side [23,24]. However, for jack bean urease, immobilized on a fixed bed reactor showed a shift towards basic side [25].…”

Urease immobilized on nylon: preparation and properties

“…It was reported that urease had different pH optima ranging from 6.4 to 7.4 depending on the type of buffer used [25]. As reported by Pozniak [19], Iyengar and Rao [17] and Weetall and Hersh [26], when bound to a support, the optimum pH of urease shifted towards the more acidic side. However, when urease was activated with formaldehyde [27], the pH optimum shifted towards the alkaline side.…”