Production, purification and characterization of a Tannase from Aspergillus niger LCF 8

Barthomeuf, Chantal; Regerat, F; Pourrat, Henri

doi:10.1016/0922-338x(94)90242-9

Cited by 105 publications

(96 citation statements)

References 6 publications

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“…The maximum enzyme production is observed at pH 4.5, whereas highest growth occurs at pH 5.0. This result is comparable to findings of other reported organisms including fungi (Barthomeuf et al, 1994;Hadi et al, 1994;Mondal et al, 2001b) and bacteria (Kumar et al, 1999;. Actually most of the microbial extracellular enzymes are produced in greatest yield at a growth pH somewhere near the pH for maximum en- Production of tannase by Bacillus cereus 265 Fig.…”

Section: Resultssupporting

confidence: 81%

Production and characterization of tannase from Bacillus cereus KBR9.

Mondal

Banerjee

et al. 2001

J. Gen. Appl. Microbiol.

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A tannase-producing soil bacteria has been isolated and identified as Bacillus cereus. It can degrade tannic acid and produce maximum tannase (0.22 U/ml) at stationary phases of growth (24 h). Maximum growth and enzyme production occurred with initial medium pH of 4.5-5.0. Partial purified tannase showed optimum activity at pH 4.5 and 40°C. It remains stable up to 30°C and pH 4.5 to 5.0. The enzyme is salt tolerant, stable up to 2 M of NaCl and retains 82% original activity in 3 M.

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Section: Resultssupporting

confidence: 81%

Production and characterization of tannase from Bacillus cereus KBR9.

Mondal

Banerjee

et al. 2001

J. Gen. Appl. Microbiol.

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“…On the whole, the two characteristic curves seem to be synchronous, and thus the incubation time is chosen as 72 h for the next investigation. On the other hand, the tannase yield reaches the top when the pH value in fermentation broth is 5 between 4.5 and 6.6 consistent with the other reports (Barthomeuf et al 1994;Bradoo et al 1997). The trend of the pH curve goes reversely vs. that of the enzyme activity curve.…”

Section: Characterization Of Growth and Enzyme Production Of The Mutantsupporting

confidence: 80%

Improving Aspergillus niger tannase yield by N+ ion beam implantation

Jin¹,

Nie

Liu³

et al. 2013

Braz. arch. biol. technol.

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“…• C. The enzyme shares these properties with fungal tannases from A. niger and P. chrysogenum (Barthomeuf et al, 1994;. The K M value of 0.14 mM shows the high affinity of the A. adeninivorans tannase for tannic acid as substrate.…”

Section: Discussionmentioning

confidence: 87%

“…The enzyme is produced in the presence of tannic acid by various filamentous fungi, principally Aspergillus and Penicillium species Barthomeuf et al, 1994), by bacteria (Deschamps et al, 1983;Kumar et al, 1999;Mondal and Pati 2000) and by yeast (Aoki et al, 1976a(Aoki et al, , 1967bDeschamps, 1989) and is utilized in a number of industrial applications, including the manufacture of instant tea (Boadi and Neufeld, 2001), fruit juices and beer (Cantarelli et al, 1989) and wine and gallic acid (Lekha and Lonsane, 1997). Unfortunately, although biotechnologically useful, these tannases do not satisfy all requirements for optimal versatility in industrial processes.…”

Section: E Böer Et Almentioning

confidence: 99%

Atan1p—an extracellular tannase from the dimorphic yeast Arxula adeninivorans: molecular cloning of the ATAN1 gene and characterization of the recombinant enzyme

Böer¹,

Bode²,

Mock³

et al. 2009

Yeast

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The tannase-encoding Arxula adeninivorans gene ATAN1 was isolated from genomic DNA by PCR, using as primers oligonucleotide sequences derived from peptides obtained after tryptic digestion of the purified tannase protein. The gene harbours an ORF of 1764 bp, encoding a 587-amino acid protein, preceded by an N-terminal secretion sequence comprising 28 residues. The deduced amino acid sequence was similar to those of tannases from Aspergillus oryzae (50% identity), A. niger (48%) and putative tannases from A. fumigatus (52%) and A. nidulans (50%). The sequence contains the consensus pentapeptide motif (-Gly-X-Ser-X-Gly-) which forms part of the catalytic centre of serine hydrolases. Expression of ATAN1 is regulated by the carbon source. Supplementation with tannic acid or gallic acid leads to induction of ATAN1, and accumulation of the native tannase enzyme in the medium. The enzymes recovered from both wild-type and recombinant strains were essentially indistinguishable. A molecular mass of ∼320 kDa was determined, indicating that the native, glycosylated tannase consists of four identical subunits. The enzyme has a temperature optimum at 35-40• C and a pH optimum at ∼6.0. The enzyme is able to remove gallic acid from both condensed and hydrolysable tannins. The wildtype strain LS3 secreted amounts of tannase equivalent to 100 U/l under inducing conditions, while the transformant strain, which overexpresses the ATAN1 gene from the strong, constitutively active A. adeninivorans TEF1 promoter, produced levels of up to 400 U/l when grown in glucose medium in shake flasks.

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Production, purification and characterization of a Tannase from Aspergillus niger LCF 8

Cited by 105 publications

References 6 publications

Production and characterization of tannase from Bacillus cereus KBR9.

Production and characterization of tannase from Bacillus cereus KBR9.

Improving Aspergillus niger tannase yield by N+ ion beam implantation

Atan1p—an extracellular tannase from the dimorphic yeast Arxula adeninivorans: molecular cloning of the ATAN1 gene and characterization of the recombinant enzyme

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