Kinetics of aspartame precursor synthesis catalysed by Pseudomonas aeruginosa elastase
Elastase isolated from Pseudomonas aeruginosa IFO 3455 was found to be an efficient protease to catalyse the synthesis of N‐benzyloxycarbonyl‐aspartyl‐phenylalanine methyl ester, the precursor of the dipeptide sweetener, aspartame. The influence of methanol as a cosolvent in this synthetic reaction...
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| Format: | Article |
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Society of Chemical Industry
1993
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| Online Access: | http://psasir.upm.edu.my/id/eprint/115723/ |
| _version_ | 1848866848103202816 |
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| author | Lee, Kong H. Lee, Pat M. Siaw, Yew S. Morihara, Kazuyuki |
| author_facet | Lee, Kong H. Lee, Pat M. Siaw, Yew S. Morihara, Kazuyuki |
| author_sort | Lee, Kong H. |
| building | UPM Institutional Repository |
| collection | Online Access |
| description | Elastase isolated from Pseudomonas aeruginosa IFO 3455 was found to be an efficient protease to catalyse the synthesis of N‐benzyloxycarbonyl‐aspartyl‐phenylalanine 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 25°C for a reaction time of about 3 h. However, the activity of the enzyme was greatly reduced in 90% methanol. The values of K and k2 for N‐benzyloxycarbonyl‐aspartic acid were 0·17 mol dm−3 and 11·9 mol dm−3 s−1 respectively. |
| first_indexed | 2025-11-15T14:27:07Z |
| format | Article |
| id | upm-115723 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-15T14:27:07Z |
| publishDate | 1993 |
| publisher | Society of Chemical Industry |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-1157232025-03-11T02:33:52Z http://psasir.upm.edu.my/id/eprint/115723/ Kinetics of aspartame precursor synthesis catalysed by Pseudomonas aeruginosa elastase Lee, Kong H. Lee, Pat M. Siaw, Yew S. Morihara, Kazuyuki Elastase isolated from Pseudomonas aeruginosa IFO 3455 was found to be an efficient protease to catalyse the synthesis of N‐benzyloxycarbonyl‐aspartyl‐phenylalanine 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 25°C for a reaction time of about 3 h. However, the activity of the enzyme was greatly reduced in 90% methanol. The values of K and k2 for N‐benzyloxycarbonyl‐aspartic acid were 0·17 mol dm−3 and 11·9 mol dm−3 s−1 respectively. Society of Chemical Industry 1993 Article PeerReviewed Lee, Kong H. and Lee, Pat M. and Siaw, Yew S. and Morihara, Kazuyuki (1993) Kinetics of aspartame precursor synthesis catalysed by Pseudomonas aeruginosa elastase. Journal of Chemical Technology & Biotechnology, 56 (4). pp. 375-381. ISSN 0268-2575; eISSN: 1097-4660 https://onlinelibrary.wiley.com/doi/10.1002/jctb.280560408 10.1002/jctb.280560408 |
| spellingShingle | Lee, Kong H. Lee, Pat M. Siaw, Yew S. Morihara, Kazuyuki Kinetics of aspartame precursor synthesis catalysed by Pseudomonas aeruginosa elastase |
| title | Kinetics of aspartame precursor synthesis catalysed by Pseudomonas aeruginosa elastase |
| title_full | Kinetics of aspartame precursor synthesis catalysed by Pseudomonas aeruginosa elastase |
| title_fullStr | Kinetics of aspartame precursor synthesis catalysed by Pseudomonas aeruginosa elastase |
| title_full_unstemmed | Kinetics of aspartame precursor synthesis catalysed by Pseudomonas aeruginosa elastase |
| title_short | Kinetics of aspartame precursor synthesis catalysed by Pseudomonas aeruginosa elastase |
| title_sort | kinetics of aspartame precursor synthesis catalysed by pseudomonas aeruginosa elastase |
| url | http://psasir.upm.edu.my/id/eprint/115723/ http://psasir.upm.edu.my/id/eprint/115723/ http://psasir.upm.edu.my/id/eprint/115723/ |