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Cited by 19 publications
(8 citation statements)
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“…Urease is a biocatalyst that serves to hydrolyze urea into ammonia and carbon dioxide. It plays a role, among other things, to improve the quality of alcoholic beverages by lowering the level of urea, the precursor of carcinogenic ethyl carbamate (Liu et al, 2012), to detect heavy metals in milk (Kaur et al, 2014), to be antifungal (Postal et al, 2012), in hemodialysis, and space missions to be life support (Iyer et al, 2018).…”
Section: Introductionmentioning
confidence: 99%
“…Urease is a biocatalyst that serves to hydrolyze urea into ammonia and carbon dioxide. It plays a role, among other things, to improve the quality of alcoholic beverages by lowering the level of urea, the precursor of carcinogenic ethyl carbamate (Liu et al, 2012), to detect heavy metals in milk (Kaur et al, 2014), to be antifungal (Postal et al, 2012), in hemodialysis, and space missions to be life support (Iyer et al, 2018).…”
Section: Introductionmentioning
confidence: 99%
“…On the other hand, as was noted above, glycerol and glycerol-based solutions are commonly used in biosensor experiments involving proteins [2,19,22]. In addition, glycerol-containing solutions are used in studies of enzymes; namely, enzymes are dissolved in glycerol-containing solutions to preserve their native structure [23][24][25][26]. In the course of operations with such biological objects, the glycerol-containing solutions are aspirated and injected into a measuring cell using injectors.…”
Section: Introductionmentioning
confidence: 99%
“…A high K m indicates that the enzyme does not bind efficiently with the substrate, and V max will only be reached if the substrate concentration is high enough to saturate the enzyme. G. max urease in this study shows a higher affinity for its substrate than the ureases from B. abortus,13 mM [16], B. badius, 7.69mM [17] and Canavlia ensiformis, 19.10 mM [18] but less affinity than jack beans urease, 4.6mM [19], Phaseolus vulgaris (2.1 mM ) [20] and H. pylori whose urease has one of the lowest Km values (0.3 mM) [21]. The findings here, suggest that the extracted urease has good affinity for the substrate (urea) under the conditions tested.…”
Section: Enzyme Activity and Kinetic Characteristicsmentioning
confidence: 51%