Purification and characterization of a novel tannase produced by Kluyveromyces marxianus using olive pomace as solid support, and its promising role in gallic acid production

2018 ◽  
Vol 107 ◽  
pp. 2342-2350 ◽  
Author(s):  
Abeer E. Mahmoud ◽  
Shadia A. Fathy ◽  
Mona M. Rashad ◽  
Magda K. Ezz ◽  
Amira T. Mohammed
2004 ◽  
Vol 91 (3) ◽  
pp. 245-252 ◽  
Author(s):  
Bernardo Ramı́rez-Zavala ◽  
Yuridia Mercado-Flores ◽  
César Hernández-Rodrı́guez ◽  
Lourdes Villa-Tanaca

1998 ◽  
Vol 64 (12) ◽  
pp. 4743-4747 ◽  
Author(s):  
Mitsuhiro Zeida ◽  
Marco Wieser ◽  
Toyokazu Yoshida ◽  
Tsuyoshi Sugio ◽  
Toru Nagasawa

ABSTRACT Oxygen-sensitive gallic acid decarboxylase from Pantoea(formerly Enterobacter) agglomerans T71 was purified from a cell extract after stabilization by reducing agents. This enzyme has a molecular mass of approximately 320 kDa and consists of six identical subunits. It is highly specific for gallic acid. Gallic acid decarboxylase is unique among similar decarboxylases in that it requires iron as a cofactor, as shown by plasma emission spectroscopy (which revealed an iron content of 0.8 mol per mol of enzyme subunit), spectrophotometric analysis (absorption shoulders at 398 and 472 nm), and inhibition of the enzyme activity by 2,2′-bipyridyl, o-phenanthroline, and EDTA. Another interesting feature of this strain is the fact that it contains a tannase, which is used together with the gallic acid decarboxylase in a two-enzyme resting cell bioconversion to synthesize valuable pyrogallol from readily available tannic acid.


2020 ◽  
Vol 176 ◽  
pp. 105718
Author(s):  
Jonathan Trapala ◽  
Ismael Bustos-Jaimes ◽  
Paloma Manzanares ◽  
Eduardo Bárzana ◽  
Carmina Montiel

Sign in / Sign up

Export Citation Format

Share Document