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Aspartame Assay Kit

The Aspartame test kit is a simple and reliable method for the specific measurement and analysis of Aspartame in beverages and foodstuffs.

Suitable for manual, auto-analyser and microplate formats.

Content/Size SKU Price Qty In Stock
50 assays (manual) / 500 assays (microplate)
/ 500 assays (auto-analyser)
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  • Very cost effective
  • All reagents stable for > 12 months after preparation
  • Only enzymatic kit available
  • Measures aspartame and breakdown products (L-aspartate and aspartame acid)
  • Very specific
  • Very rapid reaction
  • Mega-Calc™ software tool is available from our website for hassle-free raw data processing
  • Standard included
  • Suitable for manual, microplate and auto-analyser formats

UV-method for the determination of Aspartame (and breakdown
products) in foodstuffs, beverages and other materials

                       (pH 12.5)
(1) Asp-Phe-O-Me → Asp-Phe + MeOH

                      (dipeptidase M)
(2) Asp-Phe + H2O → L-aspartate + L-phenylalanine

                      (glutamate-oxaloacetate transaminase)
(3) L-Aspartate + 2-oxoglutarate → L-glutamate + oxaloacetate

                                 (L-malate dehydrogenase)
(4) Oxaloacetate + NADH + H+ → L-malate + NAD+

Kit size:                            50 assays (manual) / 500 (microplate)
                                         / 500 (auto-analyser)
Method:                            Spectrophotometric at 340 nm
Reaction time:                  ~ 5 min
Detection limit:                 0.57 mg/L
Application examples:
Soft drinks, artificial sweeteners, candies, mints, chewing gum, dietetic
products, jam, chocolate and other materials
Method recognition:      Novel method

Enhancement of recombinant protein production in Escherichia coli by coproduction of aspartase.

Wang, Z. W., Chen, Y. & Chao, Y. P. (2006). Journal of Biotechnology, 124 (2), 403-411.
Read Abstract
As commonly recognized, the excretion of acetate by the aerobic growth of Escherichia coli on glucose is a manifestation of imbalanced flux between glycolysis and the tricarboxylic acid (TCA) cycle. Accordingly, this may restrict the production of recombinant proteins in E. coli, due to the limited amounts of precursor metabolites produced in TCA cycle. To approach this issue, an extra supply of intermediate metabolites in TCA cycle was made by conversion of aspartate to fumarate, a reaction mediated by the activity of L-aspartate ammonia-lyase (aspartase). As a result, in the glucose minimal medium containing aspartate, the production of two recombinant proteins, β-galactosidase and green fluorescent protein, in the aspartase-producing strain was substantially increased by 5-fold in association with 30–40% more biomass production. This preliminary study illustrates the great promise of this approach used to enhance the production of these two recombinant proteins.