Biotechnological applications of penicillin acylases:: state-of-the-art

被引:150
作者
Arroyo, M [1 ]
de la Mata, I [1 ]
Acebal, C [1 ]
Castillón, MP [1 ]
机构
[1] Univ Complutense Madrid, Dept Bioquim & Biol Mol 1, Fac Ciencias Biol, E-28040 Madrid, Spain
关键词
D O I
10.1007/s00253-002-1113-6
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
This review describes the most recent developments in the biotechnological applications of penicillin acylases. This group of enzymes is involved mainly in the industrial production of 6-aminopenicillanic acid and the synthesis of semisynthetic beta-lactam antibiotics. In addition, penicillin acylases can also be employed in other useful biotrans formations, such as peptide synthesis and the resolution of racemic mixtures of chiral compounds. Particular emphasis is placed on advances in detection of new enzyme specificities towards other natural penicillins, enzyme immobilization, and optimization of enzyme-catalyzed hydrolysis and synthesis in the presence of organic solvents.
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收藏
页码:507 / 514
页数:8
相关论文
共 100 条
[1]   Stabilization of immobilized enzymes against water-soluble organic cosolvents and generation of hyper-hydrophilic micro-environments surrounding enzyme molecules [J].
Abian, O ;
Mateo, C ;
Fernández-Lorente, G ;
Palomo, JM ;
Fernández-Lafuente, R ;
Guisán, JM .
BIOCATALYSIS AND BIOTRANSFORMATION, 2001, 19 (5-6) :489-503
[2]  
ACEBAL C, 2001, Patent No. 0129202
[3]   Effect of cosolvent and pH on the kinetically controlled synthesis of cephalexin with immobilised penicillin acylase [J].
Aguirre, C ;
Toledo, M ;
Medina, V ;
Illanes, A .
PROCESS BIOCHEMISTRY, 2002, 38 (03) :351-360
[4]   The role of hydrophobic active-site residues in substrate specificity and acyl transfer activity of penicillin acylase [J].
Alkema, WBL ;
Dijkhuis, AJ ;
de Vries, E ;
Janssen, DB .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2002, 269 (08) :2093-2100
[5]   Characterization of the β-lactam binding site of penicillin acylase of Escherichia coli by structural and site-directed mutagenesis studies [J].
Alkema, WBL ;
Hensgens, CMH ;
Kroezinga, EH ;
de Vries, E ;
Floris, R ;
van der Laan, JM ;
Dijkstra, BW ;
Janssen, DB .
PROTEIN ENGINEERING, 2000, 13 (12) :857-863
[6]   A kinetic examination of penicillin acylase stability in water-organic solvent systems at different temperatures [J].
Arroyo, M ;
Torres-Guzmán, R ;
De la Mata, I ;
Castillón, MP ;
Acebal, C .
BIOCATALYSIS AND BIOTRANSFORMATION, 2002, 20 (01) :53-56
[7]   Chromogenic analogues of penicillin dihydroF and penicillin K for the continuous spectrophotometric determination of aliphatic penicillin acylase activity [J].
Arroyo, M ;
Torres-Guzmán, R ;
Torres-Bacete, J ;
de la Mata, I ;
Castillón, MP ;
Acebal, C .
BIOTECHNOLOGY LETTERS, 2002, 24 (13) :1045-1048
[8]   Kinetic mechanism of penicillin V acylase activation by short-chain alcohols [J].
Arroyo, M ;
Torres-Guzmán, R ;
Torres-Bacete, J ;
de la Mata, I ;
Castillón, MP ;
Acebal, C .
ENZYME AND MICROBIAL TECHNOLOGY, 2001, 29 (4-5) :312-318
[9]   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
[10]   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