Akademik Veri Yönetim Sistemi
JOURNAL OF WATER PROCESS ENGINEERING, cilt.31, 2019 (SCI-Expanded)
The potential use of laccase enzyme, which is affected by different environmental conditions, in industrial applications remains a key challenge. One of the most important aims of the enzyme immobilization is to increase the stability and reusability of enzymes. In order to increase the stability and recovery rate of the laccase from Weissella viridescens LB37 which was identified from sausage samples by 16S rRNA gene sequence analysis, it was covalently bound on chitosan beads magnetized with Fe3O4 NPs via cross linker L-glutaraldehyde and was applied in decolorization of various synthetic dyes. The laccase enzyme was purified from W. viridescens LB37 using triplet phase system (TPP). In the presence of Fe3O4 NPs, basic chitosan molecules were bound to the intermediate arm, c-glutaraldehyde and then the purified laccase enzyme was immobilized to the prepared magnetic chitosan NPs (MAG-CTS NPs). Based on the results, the appropriate conditions for the method of embedding-covalent were found to be as follows: pH - 6.0, temperature - 30 degrees C, concentration of glutaraldehyde - 1% and immobilization time - 1 h. As a result, the relative activity of immobilized laccase (IMB-LAC) on MAG-CTS NPs increased by 2-fold at pH 6.0 and nearly 2-fold in a 30 degrees C water bath after 30 min, compared to free laccase. It has also been determined that 47% relative activity of the IMB-LAC remained in 10 cycle reusability. Also high removal capacity was determined for Direct blue 15, Evans blue, Reactive black 5 and Acid red 37 azo dyes using IMB-LAC.