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Urease immobilization on arylamine glass beads and its characterization.

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Title Urease immobilization on arylamine glass beads and its characterization.
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Creator Mangaldas, K.M.; Rajput, Y.S; Sharma, R.
 
Subject Urease, immobilization, arylamine glass beads.
 
Description Not Available
Jack bean urease has been immobilized on arylamine glass beads (200-400 mesh size, 75-100 Å pore size) and its properties
compared with soluble enzyme. The binding of urease was 13.71 mg per gram beads. The Km for soluble and immobilized
urease for urea was 4.20 mM and 8.81 mM, respectively. Vmax values of urease decreased from 200 to 43.48 μmol of ammonia
formed per min per mg protein at 37°C on immobilization. Both pH and buffer ions influenced the activities of soluble as well
as immobilized urease. Soluble urease exhibited pH optima at 5.5 and 8.0. However, immobilized urease showed one
additional pH optimum at 6.5. In comparison to phosphate buffer, citrate buffer was inhibitory to urease activity. Immobilization
of urease on arylamine glass beads resulted in improved thermal, storage and operational stability. Because of inertness of
support and stability of immobilized urease, the preparation can find applications in ‘artificial kidney’ and urea estimation in
biological fluids viz., blood, milk etc.
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Date 2021-08-26T08:27:39Z
2021-08-26T08:27:39Z
2010-01-01
 
Type Research Paper
 
Identifier Not Available
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http://krishi.icar.gov.in/jspui/handle/123456789/60726
 
Language English
 
Relation Not Available;
 
Publisher Not Available