Purification and characterization of penicillin V acylase from Streptomyces lavendulae

被引：0

作者：

Torres, R ^{[1
]}

de la Mata, I ^{[1
]}

Castillón, MP ^{[1
]}

Arroyo, M ^{[1
]}

Torres, J ^{[1
]}

Acebal, C ^{[1
]}

机构：

[1] Univ Complutense Madrid, Fac Biol, Dept Bioquim & Biol Mol, E-28040 Madrid, Spain

来源：

STABILITY AND STABILIZATION OF BIOCATALYSTS | 1998年 / 15卷

关键词：

D O I：

暂无

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：

Penicillin V acylase was isolated and purified from culture supernatants of Streptomyces lavendulae. The enzyme that is largely extracellular was purified to homogeneity. Two substrates penicillin V and NIPOAB were used for inhibition studies. The kinetic constants were: K-M(penV)=4.9mM, V-max(penV)=0.47 mu mol.min(-1).mg(-1); K-M(NIPOAB)=11.9mM and V-max(NIPOAB)=4.94x10(3) mu mol.min(-1).mg(-1). Penicillin G, phenoxyacetic acid, phenylacetic acid and 6-APA were competitive inhibitors but they inhibited slightly the enzyme. This results were interesting for the possible use of this penicillin V acylase in industrial biorreactors.

引用

页码：719 / 724

页数：6

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