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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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主要な著者: Lee, Kong H., Lee, Pat M., Siaw, Yew S., Morihara, Kazuyuki
フォーマット: 論文
出版事項: Society of Chemical Industry 1993
オンライン･アクセス:http://psasir.upm.edu.my/id/eprint/116304/
https://onlinelibrary.wiley.com/doi/10.1002/jctb.280560408
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spelling my.upm.eprints.1163042025-03-25T01:07:48Z http://psasir.upm.edu.my/id/eprint/116304/ 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
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
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.
format Article
author Lee, Kong H.
Lee, Pat M.
Siaw, Yew S.
Morihara, Kazuyuki
spellingShingle Lee, Kong H.
Lee, Pat M.
Siaw, Yew S.
Morihara, Kazuyuki
Kinetics of aspartame precursor synthesis catalysed by Pseudomonas aeruginosa elastase
author_facet Lee, Kong H.
Lee, Pat M.
Siaw, Yew S.
Morihara, Kazuyuki
author_sort Lee, Kong H.
title Kinetics of aspartame precursor synthesis catalysed by Pseudomonas aeruginosa elastase
title_short 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_sort kinetics of aspartame precursor synthesis catalysed by pseudomonas aeruginosa elastase
publisher Society of Chemical Industry
publishDate 1993
url http://psasir.upm.edu.my/id/eprint/116304/
https://onlinelibrary.wiley.com/doi/10.1002/jctb.280560408
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score 13.251813

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