Purification and partial characterization of an exo-polygalacturonase from Paecilomyces variotii liquid cultures.

Abstract:

:An extracellular polygalacturonase (PG) produced from Paecilomyces variotii was purified to homogeneity through two chromatography steps using DEAE-Fractogel and Sephadex G-100. The molecular weight of P. variotii PG was 77,300 Da by gel filtration and SDS-PAGE. PG had isoelectric point of 4.37 and optimum pH 4.0. PG was very stable from pH 3.0 to 6.0. The extent of hydrolysis of different pectins by the purified enzyme was decreased with an increase in the degree of esterification. PG had no activity toward non-pectic polysaccharides. The apparent K(m) and V(max) values for hydrolyzing sodium polypectate were 1.84 mg/mL and 432 micromol/min/mg, respectively. PG was found to have temperature optimum at 65 degrees Celsius and was totally stable at 45 degrees Celsius for 90 min. Half-life at 55 degrees Celsius was 50.6 min. Almost all the examined metal cations showed partial inhibitory effects under enzymatic activity, except for Na(+1), K(+1), and Co(+2) (1 mM) and Cu(+2) (1 and 10 mM).

authors

de Lima Damásio AR,da Silva TM,Maller A,Jorge JA,Terenzi HF,Polizeli Mde L

doi

10.1007/s12010-009-8682-0

subject

Has Abstract

pub_date

2010-03-01 00:00:00

pages

1496-507

issue

5

eissn

0273-2289

issn

1559-0291

journal_volume

160

pub_type

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