The hydrophobic domain of penicillin acylase is negatively charged

Difficulties in hydrophobic chromatography of penicillin acylase due to electrostatic charges have been overcome by modification of the phenyl sepharose matrix. Phenyl sepharose-diamines showed very strong binding and resulted in poorer recoveries of penicillin acylase, while phenyl sepharose-glycin...

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Bibliographic Details
Published inEnzyme and microbial technology Vol. 13; no. 2; pp. 139 - 141
Main Authors Karyekar, Sunil.K., Hegde, M.V.
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier Inc 1991
Elsevier Science
Subjects
Biological and medical sciences
Biotechnology
Enzyme engineering
Fundamental and applied biological sciences. Psychology
hydrophobic chromatography
hydrophobic domain
Improved methods for extraction and purification of enzymes
Methods. Procedures. Technologies
Penicillin acylase
hydrophobic domain
Penicillin acylase
hydrophobic chromatography
Elution
Chemical modification
Hydrophobicity
Adsorption
Hydrophobic chromatography
Enzyme
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Summary:Difficulties in hydrophobic chromatography of penicillin acylase due to electrostatic charges have been overcome by modification of the phenyl sepharose matrix. Phenyl sepharose-diamines showed very strong binding and resulted in poorer recoveries of penicillin acylase, while phenyl sepharose-glycine, which has an ionized COO − group, gave 94%–95% recovery. The results suggest the possible presence of a negative charge in the hydrophobic domain of penicillin acylase.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:0141-0229
1879-0909
DOI:10.1016/0141-0229(91)90169-B