Abstract:
:In this study, serine protease (subtilisin Carlsberg) was immobilized on pentynyl dextran (PyD, O-alkynyl ether of dextran, 1) and used for the transesterification of N-acetyl-L-phenylalanine ethyl ester (2) with different aliphatic (1-propanol, 1-butanol, 1-pentanol, 1-hexanol) and aromatic (benzyl alcohol, 2-phenyl ethanol, 4-phenyl-1-butanol) alcohols in tetrahydrofuran (THF). The effect of carbon chain length in aliphatic and aromatic alcohols on initial and average transesterification rate, transesterification activity of immobilized enzyme and yield of the reaction under selected reaction conditions was investigated. The transesterification reactivity of the enzyme and yield of the reaction increased as the chain length of the alcohols decreased. Furthermore, almost no change in yield was observed when the immobilized enzyme was repeatedly used for selected alcohols over six cycles. Intrinsic fluorescence analysis showed that the catalytic activity of the immobilized enzyme in THF was maintained due to retention of the tertiary structure of the enzyme after immobilization on PyD (1).
journal_name
Bioprocess Biosyst Engjournal_title
Bioprocess and biosystems engineeringauthors
Tahir MN,Cho E,Mischnick P,Lee JY,Yu JH,Jung Sdoi
10.1007/s00449-013-1038-8subject
Has Abstractpub_date
2014-04-01 00:00:00pages
687-95issue
4eissn
1615-7591issn
1615-7605journal_volume
37pub_type
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journal_title:Bioprocess and biosystems engineering
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