Sol-gel immobilization of serine proteases for application in organic solvents

D.J. van Unen; Johannes F.J. Engbersen; David Reinhoudt

doi:10.1002/bit.1173

Sol-gel immobilization of serine proteases for application in organic solvents

D.J. van Unen, Johannes F.J. Engbersen, David Reinhoudt

Faculty of Science and Technology

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Abstract

The serine proteases α-chymotrypsin, trypsin, and subtilisin Carlsberg were immobilized in a sol-gel matrix and the effects on the enzyme activity in organic media are evaluated. The percentage of immobilized enzyme is 90% in the case of α-chymotrypsin and the resulting specific enzyme activity in the transesterification of N-acetyl-L-phenylalanine ethyl ester with 1-propanol in cyclohexane is 43 times higher than that of a nonimmobilized lyophilized α-chymotrypsin. The activities of trypsin and subtilisin Carlsberg are enhanced with 437 and 31 times, respectively. The effect of immobilization on the enzyme activity is highest in hydrophobic solvents.

Original language	Undefined
Pages (from-to)	154-158
Journal	Biotechnology and bioengineering
Volume	75
Issue number	2
DOIs	https://doi.org/10.1002/bit.1173
Publication status	Published - 2001

Keywords

organic solvents
serine proteases
Sol-gel
IR-59871
immobilization
METIS-202976
Transesterification

Access to Document

10.1002/bit.1173

Cite this

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title = "Sol-gel immobilization of serine proteases for application in organic solvents",

abstract = "The serine proteases α-chymotrypsin, trypsin, and subtilisin Carlsberg were immobilized in a sol-gel matrix and the effects on the enzyme activity in organic media are evaluated. The percentage of immobilized enzyme is 90% in the case of α-chymotrypsin and the resulting specific enzyme activity in the transesterification of N-acetyl-L-phenylalanine ethyl ester with 1-propanol in cyclohexane is 43 times higher than that of a nonimmobilized lyophilized α-chymotrypsin. The activities of trypsin and subtilisin Carlsberg are enhanced with 437 and 31 times, respectively. The effect of immobilization on the enzyme activity is highest in hydrophobic solvents.",

keywords = "organic solvents, serine proteases, Sol-gel, IR-59871, immobilization, METIS-202976, Transesterification",

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T1 - Sol-gel immobilization of serine proteases for application in organic solvents

AU - van Unen, D.J.

AU - Engbersen, Johannes F.J.

AU - Reinhoudt, David

N1 - 660

PY - 2001

Y1 - 2001

N2 - The serine proteases α-chymotrypsin, trypsin, and subtilisin Carlsberg were immobilized in a sol-gel matrix and the effects on the enzyme activity in organic media are evaluated. The percentage of immobilized enzyme is 90% in the case of α-chymotrypsin and the resulting specific enzyme activity in the transesterification of N-acetyl-L-phenylalanine ethyl ester with 1-propanol in cyclohexane is 43 times higher than that of a nonimmobilized lyophilized α-chymotrypsin. The activities of trypsin and subtilisin Carlsberg are enhanced with 437 and 31 times, respectively. The effect of immobilization on the enzyme activity is highest in hydrophobic solvents.

AB - The serine proteases α-chymotrypsin, trypsin, and subtilisin Carlsberg were immobilized in a sol-gel matrix and the effects on the enzyme activity in organic media are evaluated. The percentage of immobilized enzyme is 90% in the case of α-chymotrypsin and the resulting specific enzyme activity in the transesterification of N-acetyl-L-phenylalanine ethyl ester with 1-propanol in cyclohexane is 43 times higher than that of a nonimmobilized lyophilized α-chymotrypsin. The activities of trypsin and subtilisin Carlsberg are enhanced with 437 and 31 times, respectively. The effect of immobilization on the enzyme activity is highest in hydrophobic solvents.

KW - organic solvents

KW - serine proteases

KW - Sol-gel

KW - IR-59871

KW - immobilization

KW - METIS-202976

KW - Transesterification

U2 - 10.1002/bit.1173

DO - 10.1002/bit.1173

M3 - Article

SN - 0006-3592

VL - 75

SP - 154

EP - 158

JO - Biotechnology and bioengineering

JF - Biotechnology and bioengineering

IS - 2

ER -