• Journal of Microbiology and Biotechnology
• /
• v.29 no.11
• /
• pp.1749-1759
• /
• 2019

Aspergillus ochraceus biofilm, developed on an inert support, can produce tannase in Khanna medium containing 1.5% (w/v) tannic acid as the carbon source, at an initial pH of 5.0, for 72 h at 28℃. Addition of 0.1% (w/v) yeast extract increased enzyme production. The enzyme in the crude filtrate exhibited the highest activity at 30℃ and pH 6.0. At 50℃, the half-life (T50) was 60 min and it was 260 min at pH 6.0. In general, addition of detergents and surfactants did not affect tannase activity significantly. Tannase has potential applications in various biotechnological processes such as the production of propyl gallate and in the treatment of tannin-rich effluents. The content of tannins and total phenolic compounds in effluents from leather treatment was reduced by 56-83% and 47-64%, respectively, after 2 h of enzyme treatment. The content of tannins and total phenolic compounds in the sorghum flour treated for 120 h with tannase were reduced by 61% and 17%, respectively. Interestingly, the same A. ochraceus biofilm was able to produce tannase for three sequential fermentative process. In conclusion, fungal biofilm is an interesting alternative to produce high levels of tannase with biotechnological potential to be applied in different industrial sectors.

• Microbiology and Biotechnology Letters
• /
• v.18 no.6
• /
• pp.591-598
• /
• 1990

Six species under the basidiomycetes were screened for extracellular tannase (tannin acyl hydrolase EC 3.1. 1.20) production in submerged culture and Lenzites betulina was found to be most effective for the production of tannase. The optimum cultural conditions for tannase production were $25^{\circ}C$, pH 6.0 and 21 days of culture period, The efficient composition of culture medium for the production of tannase was performed in synthetic medium containing tannic acid, 2g; sucrose, 5g; bacto-peptone, 2g; ,$ KH_2PO_4, \;2g,\; MgSO_4.7H_2O \;0.5g,\; CuS0_4.5H_2O$, 2 mg; thiamine HCl, 100 ug and distilled water 100 ml, The tannase produced from Lenzites bdulin*r was 223.3 unit (umole of gaUic acidiml of brothlmin). The tannase had an optimal reaction conditions ofpH 6.0 and temperature of $40^{\circ}C$. The enzyme was stable at temperature below $40^{\circ}C$ and lost its activity by 50% above $60^{\circ}C$. And the stable pH range was 5.5 to 6.0.

• Journal of Microbiology and Biotechnology
• /
• v.22 no.2
• /
• pp.199-206
• /
• 2012

Naturally immobilized tannase (tannin acyl hydrolase, E.C. 3.1.1.20) has many advantages, as it avoids the expensive and laborious operation of isolation, purification, and immobilization, plus it is highly stable in adverse pH and temperature. However, in the case of cell-associated enzymes, since the enzyme is associated with the biomass, separation of the pure biomass is necessary. However, tannic acid, a known inducer of tannase, forms insoluble complexes with media proteins, making it difficult to separate pure biomass. Therefore, this study optimizes the production of cell-associated tannase using a "protein-tannin complex" free media. An exploratory study was first conducted in shake-flasks to select the inducer, carbon source, and nitrogen sources. As a result it was found that gallic acid induces tannase synthesis, a tryptose broth gives higher biomass, and lactose supplementation is beneficial. The medium was then optimized using response surface methodology based on the full factorial central composite design in a 3 l bioreactor. A $2^3$ factorial design augmented by 7 axial points (${\alpha}$ = 1.682) and 2 replicates at the center point was implemented in 17 experiments. A mathematical model was also developed to show the effect of each medium component and their interactions on the production of cell-associated tannase. The validity of the proposed model was verified, and the optimized medium was shown to produce maximum cell-associated tannase activity of 9.65 U/l, which is 93.8% higher than the activity in the basal medium, after 12 h at pH 5.0, $30^{\circ}C$. The optimum medium consists of 38 g/l lactose, 50 g/l tryptose, and 2.8 g/l gallic acid.

• Journal of Microbiology and Biotechnology
• /
• v.21 no.9
• /
• pp.960-967
• /
• 2011

Tannin acyl hydrolase, also known as tannase, is an enzyme with important applications in the food, feed, pharmaceutical, and chemical industries. However, despite a growing interest in the catalytic properties of tannase, its practical use is very limited owing to high production costs. Several studies have already demonstrated the advantages of solid-state fermentation (SSF) for the production of fungal tannase, yet the optimal conditions for enzyme production strongly depend on the microbial strain utilized. Therefore, the aim of this study was to improve the tannase production by a locally isolated A. niger strain in an SSF system. The SSF was carried out in packed-bed bioreactors using polyurethane foam as an inert support impregnated with defined culture media. The process parameters influencing the enzyme production were identified using a Plackett-Burman design, where the substrate concentration, initial pH, and incubation temperature were determined as the most significant. These parameters were then further optimized using a Box-Behnken design. The maximum tannase production was obtained with a high tannic acid concentration (50 g/l), relatively low incubation temperature ($30^{\circ}C$), and unique low initial pH (4.0). The statistical strategy aided in increasing the enzyme activity nearly 1.97-fold, from 4,030 to 7,955 U/l. Consequently, these findings can lead to the development of a fermentation system that is able to produce large amounts of tannase in economical, compact, and scalable reactors.