Transesterification catalyzed by trypsin supported on MCM-41

J. M. Gómez; J. Deere; D. Goradia; J. Cooney; E. Magner; B. K. Hodnett

doi:10.1023/A:1024057605239

Transesterification catalyzed by trypsin supported on MCM-41

J. M. Gómez, J. Deere, D. Goradia, J. Cooney, E. Magner, B. K. Hodnett

Research output: Contribution to journal › Article › peer-review

Abstract

Trypsin supported on MCM-41 is demonstrated as a stable catalyst for the transesterfication of N-acetyl-L-tyrosine ethyl ester with propan-1-ol. An enzyme loading of 5 micromoles of trypsin per gram of silicate was readily achieved. The ultimate enzyme loading was shown to depend strongly on enzyme purity. The adsorbed enzyme exhibited the same turnover frequency for the transesterification reaction as native trypsin, the catalyst could be reused without loss of activity following separation by centrifuging and the enzyme did not leach during testing.

Original language	English
Pages (from-to)	183-186
Number of pages	4
Journal	Catalysis Letters
Volume	88
Issue number	3-4
DOIs	https://doi.org/10.1023/A:1024057605239
Publication status	Published - Jun 2003

Keywords

Enzyme
MCM-41
Mesoporous
Stability
Transesterification
Trypsin

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abstract = "Trypsin supported on MCM-41 is demonstrated as a stable catalyst for the transesterfication of N-acetyl-L-tyrosine ethyl ester with propan-1-ol. An enzyme loading of 5 micromoles of trypsin per gram of silicate was readily achieved. The ultimate enzyme loading was shown to depend strongly on enzyme purity. The adsorbed enzyme exhibited the same turnover frequency for the transesterification reaction as native trypsin, the catalyst could be reused without loss of activity following separation by centrifuging and the enzyme did not leach during testing.",

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T1 - Transesterification catalyzed by trypsin supported on MCM-41

AU - Gómez, J. M.

AU - Deere, J.

AU - Goradia, D.

AU - Cooney, J.

AU - Magner, E.

AU - Hodnett, B. K.

PY - 2003/6

Y1 - 2003/6

N2 - Trypsin supported on MCM-41 is demonstrated as a stable catalyst for the transesterfication of N-acetyl-L-tyrosine ethyl ester with propan-1-ol. An enzyme loading of 5 micromoles of trypsin per gram of silicate was readily achieved. The ultimate enzyme loading was shown to depend strongly on enzyme purity. The adsorbed enzyme exhibited the same turnover frequency for the transesterification reaction as native trypsin, the catalyst could be reused without loss of activity following separation by centrifuging and the enzyme did not leach during testing.

AB - Trypsin supported on MCM-41 is demonstrated as a stable catalyst for the transesterfication of N-acetyl-L-tyrosine ethyl ester with propan-1-ol. An enzyme loading of 5 micromoles of trypsin per gram of silicate was readily achieved. The ultimate enzyme loading was shown to depend strongly on enzyme purity. The adsorbed enzyme exhibited the same turnover frequency for the transesterification reaction as native trypsin, the catalyst could be reused without loss of activity following separation by centrifuging and the enzyme did not leach during testing.

KW - Enzyme

KW - MCM-41

KW - Mesoporous

KW - Stability

KW - Transesterification

KW - Trypsin

UR - http://www.scopus.com/inward/record.url?scp=0141986641&partnerID=8YFLogxK

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DO - 10.1023/A:1024057605239

M3 - Article

AN - SCOPUS:0141986641

SN - 1011-372X

VL - 88

SP - 183

EP - 186

JO - Catalysis Letters

JF - Catalysis Letters

IS - 3-4

ER -

Transesterification catalyzed by trypsin supported on MCM-41

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Keywords

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