Production and Purification of Laccase Enzyme by Klebsiella pneumoniae K7

Abstract

Sixty-four isolate were klebsiella pneumoniae. Fourteen bacteria isolates “Kelbsiella species” were taken from soil and water hospital in the period between October to December 2018, those isolated were cultured on a blood agar to test their ability to hydrolytic due to formation the inhibition  zone . Twenty one isolates of K. pneumoniae were selected to be cultured in mineral salt agar for testing their efficiency to produce laccase enzyme .The efficient isolate was diagnosed depending on phenotypic, microscopic and biochemical tests to be Klebsiella pneumoniae K7. Laccases (benzenediol: oxygen oxidoreductases; EC: 1.10.3.2) are  subfamily of multicopper oxidases (MCOs) from Klebsiella pneumoniae K7 has been partially characterized by many researchers. In this paper, we purified laccase to homogeneity from Klebsiella pneumoniae K7  with about 10.82 ; 5.12 purification fold and a 34.14; 21.46% recovery by ion-exchange and gel-filtration chromatographic respectively.  The molecular weight of the Laccase as determined by gel filtration chromatography using Sephacryl S-200 gel was 120 KDalton.

Keywords: Laccases , Klebsiella pneumoniae, molecular weight, purification.

DOI: 10.7176/CMR/10-5-03

Publication date:May 31^st 2020