Characterization of cross‐linked immobilized arylesterase from  Gluconobacter oxydans  621H with activity toward cephalosporin C and 7‐aminocephalosporanic acid | Zendy

Inmaculada NavarroGonzález | Zendy; Francisco GarcíaCarmona | Zendy

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Characterization of cross‐linked immobilized arylesterase from Gluconobacter oxydans 621H with activity toward cephalosporin C and 7‐aminocephalosporanic acid

Author(s) -

Inmaculada NavarroGonzález,

Francisco GarcíaCarmona

Publication year - 2015

Publication title -

biotechnology progress

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.572

H-Index - 129

eISSN - 1520-6033

pISSN - 8756-7938

DOI - 10.1002/btpr.2178

Subject(s) - cephalosporin c , glutaraldehyde , arylesterase , chemistry , enzyme kinetics , enzyme , immobilized enzyme , kinetics , chromatography , nuclear chemistry , michaelis–menten kinetics , biochemistry , enzyme assay , cephalosporin , active site , pon1 , physics , quantum mechanics , genotype , gene , antibiotics

Cross‐linked enzyme aggregates (CLEAs) were prepared from several precipitant agents using glutaraldehyde as a cross‐linking agent with and without BSA, finally choosing a 40% saturation of ammonium sulfate and 25 mM of glutaraldehyde. The CLEAs obtained under optimum conditions were biochemically characterized. The immobilized enzyme showed higher thermal activity and a broader range of pH and organic solvent tolerance than the free enzyme. Arylesterase from Gluconobacter oxydans showed activity toward cephalosporin C and 7‐aminocephalosporanic acid. The CLEAs had a Kcat /K M of 0.9 M −1 /S −1 for 7‐ACA (7‐aminocephalosporanic acid) and 0.1 M −1 /S −1 for CPC (cephalosporin c), whereas free enzyme did not show a typical Michaelis–Menten kinetics. © 2015 American Institute of Chemical Engineers Biotechnol. Prog. , 32:36–42, 2016

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