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. 2013 Oct;20(4):373-81.
doi: 10.1016/j.sjbs.2013.04.001.

Characterization and kinetic properties of the purified Trematosphaeria mangrovei laccase enzyme

M Mabrouk Atalla  1 , H Kheiralla Zeinab, R Hamed Eman, A Youssry Amani, A Abd El Aty Abeer
Affiliations

Characterization and kinetic properties of the purified Trematosphaeria mangrovei laccase enzyme

M Mabrouk Atalla et al. Saudi J Biol Sci. 2013 Oct.

Abstract

The properties of Trematosphaeria mangrovei laccase enzyme purified on Sephadex G-100 column were investigated. SDS-PAGE of the purified laccase enzyme showed a single band at 48 kDa. The pure laccase reached its maximal activity at temperature 65 °C, pH 4.0 with K m equal 1.4 mM and V max equal 184.84 U/mg protein. The substrate specificity of the purified laccase was greatly influenced by the nature and position of the substituted groups in the phenolic ring. The pure laccase was tested with some metal ions and inhibitors, FeSO4 completely inhibited laccase enzyme and also highly affected by (NaN3) at a concentration of 1 mM. Amino acid composition of the pure enzyme was also determined. Carbohydrate content of purified laccase enzyme was 23% of the enzyme sample. The UV absorption spectra of the purified laccase enzyme showed a single peak at 260-280 nm.

Keywords: Characterization; Laccase; Marine-derived fungi; Trematosphaeria mangrovei.

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Figures

Figure 1
Figure 1
(SDS–PAGE) polyacrylamide disk electrophoresis of pure laccase from T. mangrovei. Lane 1: protein standard, lane 2: purified laccase enzyme.
Figure 2
Figure 2
Effect of different temperatures of the reaction on pure laccase activity.
Figure 3
Figure 3
Effect of different pH values of the reaction on pure laccase enzyme activity.
Figure 4
Figure 4
Thermal stability at pH 4.0 of the pure laccase enzyme from T. mangrovei.
Figure 5
Figure 5
pH stability at 65 °C of the pure laccase enzyme from T. mangrovei.
Figure 6
Figure 6
Effect of different enzyme concentrations on pure enzyme activity.
Figure 7
Figure 7
Effect of substrate concentrations on pure enzyme activity.
Figure 8
Figure 8
Effect of metal ions on T. mangrovei laccase activity. The enzyme activity without added metal ions was taken as 100% activity.
Figure 9
Figure 9
Effect of inhibitors on T. mangrovei laccase activity. Activity without inhibitors added was taken as 0% inhibition.
Figure 10
Figure 10
Amino acid analysis of the purified laccase enzyme. Total of amino acids = 100%.
Figure 11
Figure 11
UV absorption spectra of purified laccase enzyme.
None
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