Purification and characterization of tannase and tannase gene from Enterobacter sp.

Sharma, Kanti Prakash; John, P. J.

doi:10.1016/j.procbio.2010.08.016

Cited by 51 publications

(24 citation statements)

References 22 publications

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“…In comparison to it, few number of tannase genes have been cloned, sequenced, and expressed from different source organism [17,37]. The purification and characterization of tannase and tannase gene has also been reported [30]. Recently, construction of metagenomic library for screening of tannase gene has also been reported [36].…”

Section: Introductionmentioning

confidence: 99%

Characterization of Tannase Protein Sequences of Bacteria and Fungi: An In Silico Study

et al. 2012

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Section: Introductionmentioning

confidence: 99%

Characterization of Tannase Protein Sequences of Bacteria and Fungi: An In Silico Study

et al. 2012

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“…1.20), is an enzyme that cleaves ester linkages in hydrolysable tannins [8,9] to produce glucose and gallic acid [10]. Tannase is an extracellular, inducible enzyme produced in the presence of tannic acid by fungi, bacteria and yeasts [11,12].…”

Section: Introductionmentioning

confidence: 99%

A new process for simultaneous production of tannase and phytase by Paecilomyces variotii in solid-state fermentation of orange pomace

Madeira

Macedo

2011

Bioprocess Biosyst Eng

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The production of enzymes such as tannases and phytases by solid-state fermentation and their use in animal feed have become a subject of great interest. In the present work, Paecilomyces variotii was used to produce tannase and phytase simultaneously. Solid-state fermentation, a process initially designed for tannase production, was implemented here using orange pomace as substrate. Orange pomace is the waste product of the large orange juice industry in Brazil, and it has also been used as an ingredient in animal feed. In addition to enzymatic production, biotransformation of the phenolic content and antioxidant capacity of the orange pomace were analyzed after fermentation. Fermentation conditions, namely moisture level and tannic acid concentration rate, were studied using CCD methodology. The response surface obtained indicated that the highest tannase activity was 5,000 U/gds after 96 h at 59% (v/w) and 3% (w/w) and that of phytase was 350 U/gds after 72 h at 66% (v/w) and 5.8% (w/w) of moisture level and tannic acid concentration, respectively. The amount of tannase production was similar to the levels achieved in previous studies, but this was accomplished with a 7% (w/w) reduction in the amount of supplemental tannic acid required. These results are the first to show that P. variotii is capable of producing phytase at significant levels. Moreover, the antioxidant capacity of orange pomace when tested against the free radical ABTS was increased by approximately tenfold as a result of the fermentation process.

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“…To our knowledge, the only bacterial tannases that have been analyzed genetically are those from Staphylococcus lugdunensis (6), Lactobacillus plantarum (7,8), and Enterobacter sp. (9). In addition, L. plantarum tannase has been biochemically and structurally characterized (7,8,10).…”

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Tannin Degradation by a Novel Tannase Enzyme Present in Some Lactobacillus plantarum Strains

Jiménez

Esteban-Torres

Mancheño

et al. 2014

Appl Environ Microbiol

107

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bLactobacillus plantarum is frequently isolated from the fermentation of plant material where tannins are abundant. L. plantarum strains possess tannase activity to degrade plant tannins. An L. plantarum tannase (TanB Lp , formerly called TanLp1) was previously identified and biochemically characterized. In this study, we report the identification and characterization of a novel tannase (TanA Lp ). While all 29 L. plantarum strains analyzed in the study possess the tanB Lp gene, the gene tanA Lp was present in only four strains. Upon methyl gallate exposure, the expression of tanB Lp was induced, whereas tanA Lp expression was not affected. TanA Lp showed only 27% sequence identity to TanB Lp , but the residues involved in tannase activity are conserved. Optimum activity for TanA Lp was observed at 30°C and pH 6 in the presence of Ca 2؉ ions. TanA Lp was able to hydrolyze gallate and protocatechuate esters with a short aliphatic alcohol substituent. Moreover, TanA Lp was able to fully hydrolyze complex gallotannins, such as tannic acid. The presence of the extracellular TanA Lp tannase in some L. plantarum strains provides them an advantage for the initial degradation of complex tannins present in plant environments.

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Purification and characterization of tannase and tannase gene from Enterobacter sp.

Cited by 51 publications

References 22 publications

Characterization of Tannase Protein Sequences of Bacteria and Fungi: An In Silico Study

Characterization of Tannase Protein Sequences of Bacteria and Fungi: An In Silico Study

A new process for simultaneous production of tannase and phytase by Paecilomyces variotii in solid-state fermentation of orange pomace

Tannin Degradation by a Novel Tannase Enzyme Present in Some Lactobacillus plantarum Strains

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