Acidophilic Tannase from Marine Aspergillus awamori BTMFW032

Beena, P.; Soorej, M B; Elyas, K. K.; Sarita, G Bhat; Chandrasekaran, M.

doi:10.4014/jmb.1004.04038

Cited by 51 publications

(29 citation statements)

References 38 publications

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“…For example, Ramirez-Coronel et al [39] reported an isoelectric point of 3.8 for the extracellular tannase produced in SSF by A. niger. More recently, Beena et al [11] characterized an Aspergillus awamori tannase with isoelectric point of 4.4. This is the first article that reports differential profiles of isoelectrofocusing points of extracellular tannases produced under SmF and SSF.…”

Section: Discussionmentioning

confidence: 98%

Differential Properties of Aspergillus niger Tannase Produced Under Solid-State and Submerged Fermentations

Renovato

Gutiérrez-Sánchez

Rodríguez‐Durán

et al. 2011

Appl Biochem Biotechnol

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Significant differences on structure, stability, and catalytic properties of tannase were found when this enzyme was produced under solid-state and submerged fermentations (SSF and SmF) by Aspergillus niger. The specific activity was 5.5 times higher on SSF than in SmF. Significant differences in isoelectric points of tannases were found. The pH optima for both types of enzyme was found at 6 and the pH stability of SSF and SmF tannase were at 6 and 5-8, respectively. The optimal temperature range was from 50 to 60 °C for SmF tannase and 60 °C for SSF tannase, and both enzyme types showed tolerance to high temperatures (60-70 °C). The SSF tannase showed a major specificity for methyl gallate substrate while SmF tannase for tannic acid. All metal ions tested, had an activity inhibition from 30-46% on SSF tannase. SDS-PAGE analysis as well as gel localization studies of both SSF and SmF purified tannases showed a single band with a molecular weight of 102 and 105 kDa, respectively. Different levels of glycosylation were found among SSF and SmF purified tannases. This is the first report about structural differences among tannase produced under SSF and SmF and this study provides basis for explanation of the stability and catalytic differences observed previously for this two tannase types.

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Section: Discussionmentioning

confidence: 98%

Differential Properties of Aspergillus niger Tannase Produced Under Solid-State and Submerged Fermentations

Renovato

Gutiérrez-Sánchez

Rodríguez‐Durán

et al. 2011

Appl Biochem Biotechnol

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“…From the results, it could be concluded that tannase from the novel isolate requires an acidic environment to be active, and in general fungal tannase is an acidic protein. There are reports describing the optimum pH to be 5.0 in case of tannase obtained from A. awamori (35), 5.5 in case of tannase obtained from A. flavus or Aspergillus oryzae, (36, 37), 2.0 and 8.0 in case from Aspergillus awamori (38), and 6.0 in case of tannase obtained from P. chrysogenum or Aspergillus niger (15,39,40). In this research, the optimum activity of tannase from Penicillium sp.…”

Section: Discussionmentioning

confidence: 99%

A New Native Source of Tannase Producer, Penicillium sp. EZ-ZH190: Characterization of the Enzyme

et al. 2013

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Background: Tannase can be obtained from the various sources for example tannin rich plants; however microbial sources are preferred for industrial production. In microbial sources, the Aspergillus and Penicillium genus and lactic acid bacteria mostly produce tannase. However, it has been identified that this enzyme is produced by many fungi and bacteria, but researches are continuing to find new species. Objectives: The aim of this study was to isolate a tannase-producing fungi from moldy tea leaves and to study some properties of its enzyme. Materials and Methods:The present study was done via two steps. At first, industrially important tannaseproducing fungi were isolated from moldy tea leaves using the simple agar plate method followed by the screening of organisms capable of producing tannase using the enrichment culture technique in modified Czapek Dox's agar. Finally, tannase obtained from the best isolate was partially purified and characterized. Results: Tannase produced by Penicillium sp. EZ-ZH190 isolated from moldy tea leaves was partially purified and characterized. Maximum enzyme production (4.33 U.mL -1 ) was recorded after 96 hours of incubation at 30 °C in submerged culture (100 rpm) utilizing 1 % (w/v) tannic acid as a sole carbon source. This tannase exhibited optimum activity at 35 °C and at pH of 5.5, and showed nearly 50 % of its maximal activity at 50 °C. In the present study, tannase from Penicillium sp. EZ-ZH190 had KM and Vmax values of 1.24 mM and 17.09 U.mL -1 , respectively, and showed more than 50 % stability at salt (NaCl) concentration of 1 M for 24 hours. Conclusions: Tannase productivity of Penicillium sp. EZ-ZH190 (0.045 U.mL -1 .h -1 ) is comparable with the maximum tannase productivity in the reported literatures, and the biochemical characteristics showed by Penicillium sp. EZ-ZH190 tannase are considered favorable for tannin biodegradation in the industry. So, we concluded that Penicillium sp. EZ-ZH190 is a good strain for use in the efficient production of tannase.

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“…and Co 2? , respectively, at 1:1 (v/v) ratio, in the enzyme reaction mixture for 30 min and the residual enzyme activity was estimated (Beena et al 2010).…”

Section: Positional Specificitymentioning

confidence: 99%

“…Impact of methanol, isopropanol, ethanol and hexane on lipase was also studied at 1, 2, 5, 10 % (v/v) level. The enzyme assay mixture containing the enzyme and organic solvent was incubated for 1 h and the residual enzyme activities were calculated (Beena et al 2010). …”

Section: Positional Specificitymentioning

confidence: 99%

Detergent compatible alkaline lipase produced by marine Bacillus smithii BTMS 11

Lailaja

Chandrasekaran

2013

World J Microbiol Biotechnol

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Bacillus smithii BTMS 11, isolated from marine sediment, produced alkaline and thermostable lipase. The enzyme was purified to homogeneity by ammonium sulfate precipitation and ion exchange chromatography which resulted in 0.51 % final yield and a 4.33 fold of purification. The purified enzyme was found to have a specific activity of 360 IU/mg protein. SDS-PAGE analyses, under non-reducing and reducing conditions, yielded a single band of 45 kDa indicating the single polypeptide nature of the enzyme and zymogram analysis using methylumbelliferyl butyrate as substrate confirmed the lipolytic activity of the protein band. The enzyme was found to have 50°C and pH 8.0 as optimum conditions for maximal activity. However, the enzyme was active over wide range of temperatures (30-80°C) and pH (7.0-10.0). Effect of a number of metal salts, solvents, surfactants, and other typical enzyme inhibitors on lipase activity was studied to determine the novel characteristics of the enzyme. More than 90 % of the enzyme activity was observed even after 3 h of incubation in the presence of commercial detergents Surf, Sunlight, Ariel, Henko, Tide and Ujala indicating the detergent compatibility of B. smithii lipase. The enzyme was also found to be efficient in stain removal from cotton cloths. Further it was observed that the enzyme could catalyse ester synthesis between fatty acids of varying carbon chain lengths and methanol with high preference for medium to long chain fatty acids showing 70 % of esterification. Results of the study indicated scope for application of this marine bacterial lipase in various industries.

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Acidophilic Tannase from Marine Aspergillus awamori BTMFW032

Cited by 51 publications

References 38 publications

Differential Properties of Aspergillus niger Tannase Produced Under Solid-State and Submerged Fermentations

Differential Properties of Aspergillus niger Tannase Produced Under Solid-State and Submerged Fermentations

A New Native Source of Tannase Producer, Penicillium sp. EZ-ZH190: Characterization of the Enzyme

Detergent compatible alkaline lipase produced by marine Bacillus smithii BTMS 11

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