Biochemical Characterization of CTX-M-15 ESβL purified from clinical strain of Klebsiella pneumoniae SJ16
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Published:2021-08-06
Issue:
Volume:
Page:4080-4084
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ISSN:0974-360X
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Container-title:Research Journal of Pharmacy and Technology
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language:en
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Short-container-title:RJPT
Author:
Yassen Layla T.1, Hamed Saad L.1, Abdulsattar Ban O.1, Hussein Asmaa A.2
Affiliation:
1. Mustansiriyah University, College of Science, Department of Biology, Baghdad, Iraq. 2. Al-Nahrain University, College of Science, Department of Biotechnology, Baghdad, Iraq.
Abstract
The aim of this study was purification and characterization of CTX-M-15 as a medically important enzyme from locally Klebsiella pneumoniae isolate, CTX-M-15 enzyme was subjected to two purification steps including: precipitation with 80% ammonium sulfate saturation and gel filtration chromatography by using Sepharose -6B column. Specific activity of purified enzyme has been increment up to 21.9 IU/mg with 7.3 purification folds and 69% enzyme recapture. Characterization study of purified enzyme demonstrated that the M.wt. of CTX-M-15 produced by K. pneumoniae was almost 32.2 kDa. The maximal enzyme activity at (pH 7.0), and enzyme settled at pH 6-7. The enzyme also revealed a full activity at a range of temperature between 30-37oC. Enzyme activity has inhibited powerfully in the existence of EDTA and calcium chloride, when added separately at a constant concentration. Moreover, copper chloride, and ferric chloride also caused a strong inhibition to the enzyme activity while cloxacillin showed a minor effect on enzyme activity.
Publisher
A and V Publications
Subject
Pharmacology (medical),Pharmacology, Toxicology and Pharmaceutics (miscellaneous)
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