Kinetics of aspartame precursor synthesis catalysed by Pseudomonas aeruginosa elastase
✍ Scribed by Kong H. Lee; Pat M. Lee; Yew S. Siaw; Kazuyuki Morihara
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2007
- Tongue
- English
- Weight
- 612 KB
- Volume
- 56
- Category
- Article
- ISSN
- 0268-2575
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✦ Synopsis
Elastase isolated from Pseudomonas aeruginosa I F 0 3455 was found to be an efficient protease to catalyse the synthesis of N-benzyloxycarbonyl-aspartylphenylalanine methyl ester, the precursor of the dipeptide sweetener, aspartame. The influence of methanol as a cosolvent in this synthetic reaction was investigated. It was found that the synthesis of the dipeptide precursor was most efficient in 25% (v/v) methanol, pH 7.0 at about 25OC for a reaction time of about 3 h. However, the activity of the enzyme was greatly reduced in 90 YO methanol. The values of K and k, for N-benzyloxycarbonyl-aspartic acid were 0.17 mol dm-3 and 11.9 mol dm-3 s-' respectively.