CINDEFI   05381
CENTRO DE INVESTIGACION Y DESARROLLO EN FERMENTACIONES INDUSTRIALES
Unidad Ejecutora - UE
artículos
Título:
A CONTRIBUTION TO THE CHARACTERIZATION OF PROTOPECTINASE SE, AN ENDOPOLYGALACTURONASE WITH PECTIN-RELEASING ACTIVITY FROM Geotrichum klebahnii
Autor/es:
CAVALITTO, S E; HOURS R A; MIGNONE C F
Revista:
REVISTA MEXICANA DE INGENIERIA QUIMICA
Editorial:
UNIV AUTONOMA METROPOLITANA-IZTAPALAPA
Referencias:
Lugar: México D.F.; Año: 2014 vol. 13 p. 75 - 81
ISSN:
1665-2738
Resumen:
Hydrolysis of polygalacturonic acid (1.8 g.L1 ) with 1.25 mg.L1 of a commercial preparation (Pectinase SE from Shikibo Ltd., Japan) containing protopectinase SE (PPase-SE) activity for 80 min released a reducing power equivalent to 400 mg.L1 of galacturonic acid monohydrate, yielding oligogalacturonates with an average polymerization degree of around 4. Thermostability of PPase-SE was positively aected by enzyme concentration. Enzyme activity of a solution containing 12.5 mg.L1 of Pectinase SE in 20 mM sodium acetate buer, pH 5.0, quickly dropped to less than 20 % after 80 s of vortexing. Enzyme pre-incubation (37°C, 30 min) with Ca2+, Mg2+, Co2+, Cu2+, Fe2+, Zn2+ and Mn2+ (0.1, 1.0 and 10.0 mM) did not aect the activity except in the case of Cu2+ (10 mM). Ca2+ (2.5 mM) and Mg2+ (2.5 mM) in the reaction mixture caused inhibition and activation, respectively. Ca2+ inhibition was partially reverted by Mg2+. The enzyme is not inhibited by products. Km and Vmax value for PGA was determined to be 0.198 0.013 g.L1 and 0.0509 0.0032 mol.mL1.min1 respectively. This Km value is one of the lowest reported for microbial PGases from dierent origins.