42395
Tannase from Aspergillus ficuum
powder, white, ≥150 U/g
Synonym(s):
Tannin acyl Hydrolase
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About This Item
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biological source
Aspergillus sp. (A. ficuum)
Quality Level
form
powder
specific activity
≥150 U/g
impurities
25 mM potassium phosphate
250 mM NaCl
50% glycerol
color
white
storage temp.
2-8°C
General description
Tannase is an enzyme that is produced by several organisms such as plants, bacteria, fungi, and yeast. This enzyme is also found in plant sources such as tannin-rich vegetables, especially in the leaves, fruits, branches, and bark.
Application
Tannase from Aspergillus ficuum has been used:
- as a standard to determine the tannase activity of bacterial isolates
- to study its effects on the inhibitory activity of tannic acid on biofilm formation
- to obtain Proanthocyanidins (PA) by enzymatic hydrolysis of grape skin and seeds
Biochem/physiol Actions
Tannase catalyzes the ester bonds located in complex tannins, gallo-tannins, and gallic acid esters, which results in the release of gallic acid. This enzyme can be used as a clarifying agent in the manufacture of beer, tea, wine, and juices and to treat tannin-polluting agricultural waste and industrial effluents.
Unit Definition
1 U corresponds to the amount of enzyme which changes the absorbance at 310 nm by 1.0 per minute at pH 4.7 and 30°C (tannic acid as substrate, final volume 3 ml)
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Luis V Rodríguez-Durán et al.
Journal of microbiology and biotechnology, 21(9), 960-967 (2011-09-29)
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
Tadashi Takahashi et al.
Eukaryotic cell, 11(4), 507-517 (2012-01-31)
Loop-out-type recombination is a type of intrachromosomal recombination followed by the excision of a chromosomal region. The detailed mechanism underlying this recombination and the genes involved in loop-out recombination remain unknown. In the present study, we investigated the functions of
Bhakti Bajpai et al.
Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 39(4), 708-711 (2008-10-01)
In a new approach to microbial gallic acid production by Aspergillus fischeri MTCC 150, 40gL(-1) of tannic acid was added in two installments during the bioconversion phase of the process (25gL(-1) and 15gL(-1) at 32 and 44h respectively). The optimum
Amrita Banerjee et al.
The protein journal, 31(4), 306-327 (2012-03-31)
The tannase protein sequences of 149 bacteria and 36 fungi were retrieved from NCBI database. Among them only 77 bacterial and 31 fungal tannase sequences were taken which have different amino acid compositions. These sequences were analysed for different physical
I Darah et al.
Applied biochemistry and biotechnology, 165(7-8), 1682-1690 (2011-09-29)
Agitation speed was found to influence the tannase production and fungal growth of Aspergillus niger FETL FT3. The optimal agitation speed was at 200 rpm which produced 1.41 U/ml tannase and 3.75 g/l of fungal growth. Lower or higher agitation
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