The research work was aimed at the development of an efficient method for the encapsulation of laccase extract, obtained from Coriolus hirsutus, in silica sol-gel matrix. The entrapment matrix was assessed in terms of its encapsulation efficiency (EE%), residual laccase specific activity and other kinetic parameters, protein leakage and enzyme reusability as well as its storage stability. The experimental results showed that the encapsulation of laccase resulted by an enhancement of its catalytic activity, with a residual specific activity of 320% and an EE of 90%. As an assessment of the matrix stability, as indicated by the protein release profile, a maximum leakage of 20.6% was obtained after a period of 24h at 25οC. In addition, the encapsulated laccase demonstrated a relative residual specific activity of 82.7% after 5 continuous enzymatic reaction cycles. The encapsulation of laccase also enhanced the storage stability of its activity, with a residual enzymatic activity of 102.7% as compared to 56.5% for the free one, after 6 weeks of storage at 4οC. The kinetic studies indicated that the Km value was 0.73 and 4.55 µmol for the free and encapsulated laccase, respectively, with a corresponding Vmax value of 41.26 and 311.10 µmol/mg protein/min and a catalytic efficiency (kcat) of 56.9 and 63.7 min-1, respectively. The overall findings suggest that the silica sol-gel could be an appropriate matrix for the encapsulation of laccase and would thereby promote the potential use of the enzyme in a wide range of biotechnological applications, including the food industry.

Enhancement of catalytic activity and stability of crude Laccase extract in Silica Sol-Gel

253rd National Meeting (2017)

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