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Effect of immobilization on the penicillin binding and reactivity properties of DD‐peptidase from Streptomyces R61
Author(s) -
Eng Grace Y.,
Maxwell Robert J.
Publication year - 1996
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/(sici)1099-1352(199634/12)9:5/6<706::aid-jmr326>3.0.co;2-w
Subject(s) - chemistry , tripeptide , enzyme , substrate (aquarium) , penicillin , surface plasmon resonance , binding site , streptomyces , reactivity (psychology) , combinatorial chemistry , stereochemistry , chromatography , biochemistry , antibiotics , peptide , bacteria , biology , ecology , materials science , genetics , nanoparticle , nanotechnology , medicine , alternative medicine , pathology
An affinity gel matrix containing an enzyme (DD‐peptidase) with specific β‐lactam binding properties was characterized with respect to its binding and reactivity behavior with penicillin. The data show that immobilization of DDP by reaction with the enzymes susceptible amino groups resulted in changes in catalytic activity on a tripeptide substrate, penicillin binding efficiency and pH stability of drug binding. Properties unaffected by immobilization were the drug–enzyme complex stability, binding reaction mechanism, drug selectivity and method of complex desorption. The affinity of DDP for penicillin‐G was investigated by surface plasmon resonance. These characteristics were compared with those of the soluble enzyme. Conditions for elution of the bound drug were determined and a method for immobilizing Streptomyces DDP by which its binding site structure is sustained was also evaluated.