Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
4357483 | Mycological Research | 2009 | 7 Pages |
Abstract
The present work describes the purification and characterization of a novel extracellular polygalacturonase, PGase I, produced by Pycnoporus sanguineus when grown on citrus fruit pectin. This substrate gave enhanced enzyme production as compared to sucrose and lactose. PGase I is an exocellular enzyme releasing galacturonic acid as its principal hydrolysis product as determined by TLC and orcinol-sulphuric acid staining. Its capacity to hydrolyze digalacturonate identified PGase I as an exo-polygalacturonase. SDS-PAGE showed that PGase I is an N-glycosidated monomer. The enzyme has a molecular mass of 42 kDa, optimum pH 4.8 and stability between pH 3.8 and 8.0. A temperature optimum was observed at 50-60 °C, with some enzyme activity retained up to 80 °C. Its activation energy was 5.352 cal molâ1. PGase I showed a higher affinity towards PGA than citric pectin (Km = 0.55 ± 0.02 and 0.72 ± 0.02 mg mlâ1, respectively). Consequently, PGase I is an exo-PGase, EC 3.2.1.82.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Agricultural and Biological Sciences (General)
Authors
Emma N. Quiroga, Melina A. Sgariglia, César F. Molina, Diego A. Sampietro, José R. Soberón, Marta A. Vattuone,