Acylation of subtilisin with long fatty acyl residues affects its activity and thermostability in aqueous medium

FEBS Letters

Ballesteros, Antonio¹  Plou, Francisco J.¹ 

[1] Departamento de Biocatalisis, Instituto de Catálisis, CSIC, Universidad Autónoma, 28049 Madrid, Spain

关键词: Subtilisin Carlsberg;    Chemical modification;    Enzyme hydrophobicity;    In vitro hydrophobization;    Enzyme stabilization;    pNPB;    p-nitrophenyl butyrate;    ATEE;    N-Acetyl-l-tyrosine ethyl ester;    PEG;    polyethylene glycol;    HLB;    hydrophile-lipophile balance;    Succ-;    Suceinyl;    pNA;    p-nitroanilide;    Ac-Tyr-NH2;    N-Acetyl-l-tyrosine amide;    PMSF;    phenylmethanesulfonyl fluoride;   

DOI  :  10.1016/0014-5793(94)80415-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Subtilisin Carlsberg has been artificially hydrophobized by acylation with octanoyl or palmitoyl chlorides. Samples with several degrees of substitution were obtained. Hydrophobization facilitates in some cases the binding of synthetic or natural substrates. Furthermore, derivatized subtilisins show improved thermal stability (15-fold at 45°C) in aqueous solution. As a result, octanoyl-subtilisin exhibits enhanced thermostability without losing biological activity.

【 授权许可】

Unknown