Essam F A Al-Jumaily
Baghdad University, Iraq
Title: Extraction and purification of extracellular glucosyltransferase (GTFs) from Streptococcus mutans serotype C isolate (H5)
Biography
Biography: Essam F A Al-Jumaily
Abstract
These isolates were tested for production of extracellular Glucosyltransferase (GTF) through determination of their enzyme specific activity. All isolates were able to produce the enzyme; Streptococci isolate (H5) which identified as Streptococcus mutans serotype C was selected as the best producible isolate for GTF with a specific activity of 2.6 U/mg. It was found that GTF of the chosen isolate (H5) was produced during the middle stationary phase (18-35 hours) and its maximal productivity was reached at 22 hours. Purification of S. mutans serotype (C) H5 GTF were done by ammonium sulfate, ion-exchange chromatography (DEAE-Sephacel column) and gel-filtration chromatography using Sepharose 6B column. The best percent saturation use for precipitating GTF by ammonium sulfate was 20-40% with specific activity 2.4 U/ml. Two purified GTF enzymes (GTF-I and GTF-II) were detected with specific activity 35.5 U/mg, 8.3 U/mg after 96.1 and 22.6 fold of purification respectively with yield 17.2%. Determination of purified GTF (GTF-I, GTF-II) molecular weight was done by using gel-filtration chromatography (sepharose 6B) column with presence of standards proteins. It was found that the molecular weight of GTF-I, GTF-II was 125819, 112201 Dalton respectively.
