US EPA

2283430 

Journal Article 

Pentynyl dextran as a support matrix for immobilization of serine protease subtilisin Carlsberg and its use for transesterification of N-acetyl-L-phenylalanine ethyl ester in organic media 

Tahir, MN; Cho, E; Mischnick, P; Lee, JY; Yu, JH; Jung, S 

2014 

Yes 

Bioprocess and Biosystems Engineering
ISSN: 1615-7591
EISSN: 1615-7605 

Springer Verlag 

37 

4 

687-695 

English 

23978850 

10.1007/s00449-013-1038-8 

WOS:000334930800011 

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). 

Enzyme catalysis; Immobilization; N-acetyl-L-phenyl ethyl ester; Pentynyl dextran; Subtilisin Carlsberg; Transesterification