Optimization of Tannase Biosynthesis from Two Local Aspergilli using Commercial Green Tea as Solid Substrate

Sherief, A.A.; El-Tanash, A. B.; Nour, Alshaymaa

doi:10.3923/biotech.2011.78.85

Cited by 3 publications

(1 citation statement)

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“…Despite of its importance, more work on different forms of tannase is needed to increase its application and clearly established its optimum temperature, pH conditions, thermal stability and operational stability. This research is an extension of a study on tannase production from some Aspergillus species under solid state fermentation using commercial green tea (Camellia sinensis L) as solid substrate (Sherief et al, 2011).…”

Section: Brazilian Journal Of Chemical Engineeringmentioning

confidence: 99%

Catalytic properties of immobilized tannase produced from Aspergillus aculeatus compared with the free enzyme

El-Tanash

Sherief

Nour

2011

Braz. J. Chem. Eng.

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-Aspergillus aculeatus tannase was immobilized on several carriers by entrapment and covalent binding with cross-linking. Tannase immobilized on gelatin with cross-linking agent showed the highest activity and immobilization yield. The optimum pH of the immobilized enzyme was shifted to a more acidic range compared with the free enzyme (from pH 5.5 to pH 5.0). The optimum temperature of the reaction was determined to be 50°C for the free enzyme and 60°C for the immobilized form. The thermal stability, as well as stability over a wide range of pH, was significantly improved by the immobilization process. The calculated K m of the immobilized tannase (11.8 mg ml -1 ) is higher than that of the free tannase (6.5 mg ml -1 ), while V max of the immobilized enzyme (0.32 U (µg protein) -1 ) is lower than that of the free tannase (2.7 U (µg protein) -1 ). The immobilized enzyme was able to retain 84 % of the initial catalytic activity after 5.0 cycles.

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Section: Brazilian Journal Of Chemical Engineeringmentioning

confidence: 99%