Purification of an exopolygalacturonase from Penicillium viridicatum RFC3 produced in submerged fermentation

13Citations
Citations of this article
19Readers
Mendeley users who have this article in their library.

Abstract

An exo-PG obtained from Penicillium viridicatum in submerged fermentation was purified to homogeneity. The apparent molecular weight of the enzyme was 92 kDa, optimum pH and temperature for activity were pH 5 and 50-55°C. The exo-PG showed a profile of an exo-polygalacturonase, releasing galacturonic acid by hydrolysis of pectin with a high degree of esterification (D.E.). Ions Ca 2+ enhanced the stability of enzyme and its activity by 30%. The K m was 1.30 in absence of Ca 2+ and 1.16mg mL -1 in presence of this ion. In relation to the Vmax the presence of this ion increased from 1.76 to 2.07 μmol min -1mg -1. Copyright © 2009 Eleni Gomes et al.

Cite

CITATION STYLE

APA

Gomes, E., Leite, R. S. R., Da Silva, R., & Silva, D. (2009). Purification of an exopolygalacturonase from Penicillium viridicatum RFC3 produced in submerged fermentation. International Journal of Microbiology. https://doi.org/10.1155/2009/631942

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free