A kinetic examination of penicillin acylase stability in water-organic solvent systems at different temperatures

被引：17

作者：

Arroyo, M ^{[1
]}

Torres-Guzmán, R ^{[1
]}

De la Mata, I ^{[1
]}

Castillón, MP ^{[1
]}

Acebal, C ^{[1
]}

机构：

[1] Univ Complutense Madrid, Fac Ciencias Biol, Dept Bioquim & Biol Mol 1, Madrid, Spain

来源：

BIOCATALYSIS AND BIOTRANSFORMATION | 2002年 / 20卷 / 01期

关键词：

penicillin acylase; Streptomyces lavendulae; organic solvents; monophasic systems; enzyme stability;

D O I：

10.1080/10242420210158

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have studied the thermal stability of penicillin acylase from Streptomyces lavendulae in water-organic solvent monophasic systems at the range of temperatures between 40 and 60degreesC. We found a linear correlation between the log P value of the solvent and the activation free energy for denaturation (DeltaG(d)) at all temperatures tested. Thermodynamic analysis of the results indicates that solvents with log P less than or equal to -2.3 have protective effects, whereas solvents with log P greater than or equal to -1.8 are deleterious for penicillin acylase.

引用

页码：53 / 56

页数：4

共 23 条

[1] Prediction of penicillin V acylase stability in water-organic co-solvent monophasic systems as a function of solvent composition [J].

Arroyo, M ;

Torres-Guzmán, R ;

de la Mata, I ;

Castillón, MP ;

Acebal, C .

ENZYME AND MICROBIAL TECHNOLOGY, 2000, 27 (1-2) :122-126

[2] Interaction of penicillin V acylase with organic solvents:: catalytic activity modulation on the hydrolysis of penicillin V [J].

Arroyo, M ;

Torres, R ;

de la Mata, I ;

Castillón, MP ;

Acebal, C .

ENZYME AND MICROBIAL TECHNOLOGY, 1999, 25 (3-5) :378-383

[3] Activation and stabilization of penicillin V acylase from Streptomyces lavendulae in the presence of glycerol and glycols [J].

Arroyo, M ;

Torres-Guzmán, R ;

de la Mata, I ;

Castillón, MP ;

Acebal, C .

BIOTECHNOLOGY PROGRESS, 2000, 16 (03) :368-371

[4]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[5] THE EFFECT OF POLYOL COMPOUNDS ON THE THERMOSTABILITY OF PENICILLIN-G ACYLASE FROM A MUTANT OF ESCHERICHIA-COLI ATCC-11105 [J].

ERARSLAN, A .

PROCESS BIOCHEMISTRY, 1995, 30 (02) :133-139

[6] Facile synthesis of artificial enzyme nano-environments via solid-phase chemistry of immobilized derivatives: Dramatic stabilization of penicillin acylase versus organic solvents [J].

Fernandez-Lafuente, R ;

Rosell, CM ;

Caanan-Haden, L ;

Rodes, L ;

Guisan, JM .

ENZYME AND MICROBIAL TECHNOLOGY, 1999, 24 (1-2) :96-103

[7] The presence of methanol exerts a strong and complex modulation of the synthesis of different antibiotics by immobilized Penicillin G acylase [J].

Fernández-Lafuente, R ;

Rosell, CM ;

Guisán, JM .

ENZYME AND MICROBIAL TECHNOLOGY, 1998, 23 (05) :305-310

[8] ENZYME REACTION-ENGINEERING - SYNTHESIS OF ANTIBIOTICS CATALYZED BY STABILIZED PENICILLIN-G ACYLASE IN THE PRESENCE OF ORGANIC COSOLVENTS [J].

FERNANDEZLAFUENTE, R ;

ROSELL, CM ;

GUISAN, JM .

ENZYME AND MICROBIAL TECHNOLOGY, 1991, 13 (11) :898-905

[9] MECHANISM OF PROTEIN STABILIZATION BY GLYCEROL - PREFERENTIAL HYDRATION IN GLYCEROL-WATER MIXTURES [J].

GEKKO, K ;

TIMASHEFF, SN .

BIOCHEMISTRY, 1981, 20 (16) :4667-4676

[10] Acetonitrile-protein interactions: amino acid solubility and preferential solvation [J].

Gekko, K ;

Ohmae, E ;

Kameyama, K ;

Takagi, T .

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1998, 1387 (1-2) :195-205

← 1 2 3 →