Catalytical Properties of Free and Immobilized Aspergillus niger Tannase | Zendy

Abril Flores-Maltos | Zendy; Luis V. RodríguezDurán | Zendy; Jacqueline Renovato | Zendy; Juan C. Contreras | Zendy; Raúl Barbón | Zendy; Cristóbal N. Aguilar | Zendy

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Catalytical Properties of Free and Immobilized Aspergillus niger Tannase

Author(s) -

Abril Flores-Maltos,

Luis V. RodríguezDurán,

Jacqueline Renovato,

Juan C. Contreras,

Raúl Barbón,

Cristóbal N. Aguilar

Publication year - 2011

Publication title -

enzyme research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.439

H-Index - 39

eISSN - 2090-0406

pISSN - 2090-0414

DOI - 10.4061/2011/768183

Subject(s) - tannase , aspergillus niger , aspergillus , medicine , microbiology and biotechnology , chemistry , biology , biochemistry , gallic acid , antioxidant

A fungal tannase was produced, recovered, and immobilized by entrapment in calcium alginate beads. Catalytical properties of the immobilized enzyme were compared with those of the free one. Tannase was produced intracellularly by the xerophilic fungus Aspergillus niger GH1 in a submerged fermentation system. Enzyme was recovered by cell disruption and the crude extract was partially purified. The catalytical properties of free and immobilized tannase were evaluated using tannic acid and methyl gallate as substrates. K M and V max values for free enzyme were very similar for both substrates. But, after immobilization, K M and V max values increased drastically using tannic acid as substrate. These results indicated that immobilized tannase is a better biocatalyst than free enzyme for applications on liquid systems with high tannin content, such as bioremediation of tannery or olive-mill wastewater.

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