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DC Field | Value | Language |
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dc.contributor.author | Essel, K. K. | - |
dc.contributor.author | Osei, Y. D. | - |
dc.date.accessioned | 2017-10-10T10:30:53Z | - |
dc.date.available | 2017-10-10T10:30:53Z | - |
dc.date.issued | 2014 | - |
dc.identifier.citation | Natural Products Chemistry and Research, 2 (6), 1-5 | en_US |
dc.identifier.issn | 2329-6836 | - |
dc.identifier.uri | https://csirspace.foodresearchgh.site/handle/123456789/233 | - |
dc.description.abstract | The effect of substrate concentration, pH, temperature and inhibitor (silver nitrate) on the activity of the enzyme invertase was studied using sucrose as the substrate. The invertase acted on the sucrose and converted it to product, glucose and fructose. From Lineweaver-Burk Plot, Vmax was found to be 1 mM/min and the Km approximately 24 mM. At temperature range of 25˚C to 650˚C, the optimum activity was at 450˚C. For a pH range of 3.5-6.0, the pH optimum activity was at 5.5. Inhibition studies showed that silver nitrate inhibited invertase competitively with apparent Km of 150 mM and Ki value of 160 mM | en_US |
dc.language.iso | en | en_US |
dc.publisher | OMICS International | en_US |
dc.subject | Invertase | en_US |
dc.subject | Commercial yeast | en_US |
dc.subject | Confectionery | en_US |
dc.title | Investigation of some kinetic properties of commercial invertase from yeast | en_US |
dc.type | Article | en_US |
dc.journalname | Natural Products Chemistry and Research | - |
Appears in Collections: | Food Research Institute |
Files in This Item:
File | Description | Size | Format | |
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NPCR_2_6_Essel_et al.pdf | 716.03 kB | Adobe PDF | View/Open |
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